CO1A2_HUMAN
ID CO1A2_HUMAN Reviewed; 1366 AA.
AC P08123; P02464; Q13897; Q13997; Q13998; Q14038; Q14057; Q15177; Q15947;
AC Q16480; Q16511; Q7Z5S6; Q9UEB6; Q9UEF9; Q9UM83; Q9UMI1; Q9UML5; Q9UMM6;
AC Q9UPH0;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 7.
DT 03-AUG-2022, entry version 238.
DE RecName: Full=Collagen alpha-2(I) chain;
DE AltName: Full=Alpha-2 type I collagen;
DE Flags: Precursor;
GN Name=COL1A2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ASN-249; THR-276; VAL-483;
RP ALA-549; HIS-678; GLY-743; PHE-1022; GLU-1189; PRO-1198 AND HIS-1354.
RX PubMed=2824475; DOI=10.1016/s0021-9258(18)47691-0;
RA de Wet W.J., Bernard M.P., Benson-Chanda V., Chu M.-L., Dickson L.A.,
RA Weil D., Ramirez F.;
RT "Organization of the human pro-alpha 2(I) collagen gene.";
RL J. Biol. Chem. 262:16032-16036(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], REVIEW ON OI VARIANTS, AND VARIANTS ALA-549;
RP HIS-678 AND HIS-1354.
RX PubMed=9016532; DOI=10.1093/nar/25.1.181;
RA Dalgleish R.;
RT "The human type I collagen mutation database.";
RL Nucleic Acids Res. 25:181-187(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-270; VAL-483; HIS-678;
RP GLY-743; PHE-1022; GLU-1189; PRO-1198 AND HIS-1354.
RX PubMed=9443882; DOI=10.1086/301689;
RA Korkko J.M., Ala-Kokko L., De Paepe A., Nuytinck L., Earley J.J.,
RA Prockop D.J.;
RT "Analysis of the COL1A1 and COL1A2 genes by PCR amplification and scanning
RT by conformation-sensitive gel electrophoresis identifies only COL1A1
RT mutations in 15 patients with osteogenesis imperfecta type I:
RT identification of common sequences of null-allele mutations.";
RL Am. J. Hum. Genet. 62:98-110(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-549.
RC TISSUE=Skin, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-765, AND VARIANTS HIS-678 AND GLY-743.
RC TISSUE=Placenta;
RX PubMed=3421913; DOI=10.1042/bj2520633;
RA Kuivaniemi H., Tromp G., Chu M.-L., Prockop D.J.;
RT "Structure of a full-length cDNA clone for the prepro alpha 2(I) chain of
RT human type I procollagen. Comparison with the chicken gene confirms unusual
RT patterns of gene conservation.";
RL Biochem. J. 252:633-640(1988).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-93, AND VARIANT PRO-59.
RX PubMed=4011429; DOI=10.1093/nar/13.10.3427;
RA Dickson L.A., de Wet W., Di Liberto M., Weil D., Ramirez F.;
RT "Analysis of the promoter region and the N-propeptide domain of the human
RT pro alpha 2(I) collagen gene.";
RL Nucleic Acids Res. 13:3427-3438(1985).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
RA Akai J., Kimura A., Arai K., Uehara K., Hata R.;
RT "Fine structural analysis of the unique 5' region of the human COL1A2 gene
RT containing two regions of dinucleotide repeats adjacent to the
RT transcriptional start site.";
RL Connect. Tissue Res. 30:1-6(1998).
RN [8]
RP PROTEIN SEQUENCE OF 32-111, HYDROXYLATION AT PRO-47; PRO-50; PRO-62;
RP PRO-65; PRO-68; PRO-71; PRO-102 AND PRO-108, AND VARIANT EDSARTH2
RP 76-ASN--MET-93 DEL.
RX PubMed=3680255; DOI=10.1016/s0021-9258(18)49266-6;
RA Wirtz M.K., Glanville R.W., Steinmann B., Rao V.H., Hollister D.W.;
RT "Ehlers-Danlos syndrome type VIIB. Deletion of 18 amino acids comprising
RT the N-telopeptide region of a pro-alpha 2(I) chain.";
RL J. Biol. Chem. 262:16376-16385(1987).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-93, PROTEIN SEQUENCE OF 23-96,
RP HYDROXYLATION AT PRO-47; PRO-50; PRO-62; PRO-65; PRO-68 AND PRO-71,
RP PYROGLUTAMATE FORMATION AT GLN-23, AND VARIANT EDSARTH2 76-ASN--MET-93 DEL.
RX PubMed=2394758; DOI=10.1016/s0021-9258(18)55498-3;
RA Weil D., D'Alessio M., Ramirez F., Eyre D.R.;
RT "Structural and functional characterization of a splicing mutation in the
RT pro-alpha 2(I) collagen gene of an Ehlers-Danlos type VII patient.";
RL J. Biol. Chem. 265:16007-16011(1990).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-93, AND VARIANT EDSARTH2
RP 76-ASN--MET-93 DEL.
RX PubMed=1577745; DOI=10.1016/s0021-9258(19)50393-3;
RA Watson R.B., Wallis G.A., Holmes D.F., Viljoen D., Byers P.H., Kadler K.E.;
RT "Ehlers Danlos syndrome type VIIB. Incomplete cleavage of abnormal type I
RT procollagen by N-proteinase in vitro results in the formation of copolymers
RT of collagen and partially cleaved pNcollagen that are near circular in
RT cross-section.";
RL J. Biol. Chem. 267:9093-9100(1992).
RN [11]
RP PROTEIN SEQUENCE OF 80-96, ALLYSINE AT LYS-84, AND PYROGLUTAMATE FORMATION
RP AT GLN-80.
RC TISSUE=Skin;
RX PubMed=5529814; DOI=10.1021/bi00826a012;
RA Click E.M., Bornstein P.;
RT "Isolation and characterization of the cyanogen bromide peptides from the
RT alpha 1 and alpha 2 chains of human skin collagen.";
RL Biochemistry 9:4699-4706(1970).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 145-198.
RX PubMed=3403536; DOI=10.1016/s0021-9258(18)37971-7;
RA Kuivaniemi H., Sabol C., Tromp G., Sippola-Thiele M., Prockop D.J.;
RT "A 19-base pair deletion in the pro-alpha 2(I) gene of type I procollagen
RT that causes in-frame RNA splicing from exon 10 to exon 12 in a proband with
RT atypical osteogenesis imperfecta and in his asymptomatic mother.";
RL J. Biol. Chem. 263:11407-11413(1988).
RN [13]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 163-213, AND VARIANT OI4 181-GLY--LYS-198
RP DEL.
RX PubMed=1642148; DOI=10.1002/jbmr.5650070709;
RA Chipman S.D., Shapiro J.R., McKinstry M.B., Stover M.L., Branson P.,
RA Rowe D.W.;
RT "Expression of mutant alpha (I)-procollagen in osteoblast and fibroblast
RT cultures from a proband with osteogenesis imperfecta type IV.";
RL J. Bone Miner. Res. 7:793-805(1992).
RN [14]
RP PROTEIN SEQUENCE OF 175-180, HYDROXYLATION AT LYS-177, AND GLYCOSYLATION AT
RP LYS-177.
RC TISSUE=Skin;
RX PubMed=4319110; DOI=10.1016/s0021-9258(18)62815-7;
RA Morgan P.H., Jacobs H.G., Segrest J.P., Cunningham L.W.;
RT "A comparative study of glycopeptides derived from selected vertebrate
RT collagens. A possible role of the carbohydrate in fibril formation.";
RL J. Biol. Chem. 245:5042-5048(1970).
RN [15]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 181-1366.
RA Kalicki J., Wamsley P., Gibson A.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [16]
RP PROTEIN SEQUENCE OF 417-447, AND HYDROXYLATION AT PRO-420; PRO-441 AND
RP PRO-444.
RC TISSUE=Skin;
RX PubMed=4412529; DOI=10.1111/j.1432-1033.1974.tb03689.x;
RA Fietzek P.P., Furthmayr H., Kuehn K.;
RT "Comparative sequence studies on alpha2-CB2 from calf, human, rabbit and
RT pig-skin collagen.";
RL Eur. J. Biochem. 47:257-261(1974).
RN [17]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 520-573, AND VARIANT ALA-549.
RX PubMed=2839839; DOI=10.1073/pnas.85.14.5254;
RA Tromp G., Prockop D.J.;
RT "Single base mutation in the pro alpha 2(I) collagen gene that causes
RT efficient splicing of RNA from exon 27 to exon 29 and synthesis of a
RT shortened but in-frame pro alpha 2(I) chain.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:5254-5258(1988).
RN [18]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 622-657.
RX PubMed=6321602; DOI=10.1111/1523-1747.ep12260213;
RA Tajima S., Ting J.P., Pinnell S.R., Kaufman R.E.;
RT "Isolation and characterization of a human pro alpha 2(I) collagen gene
RT segment.";
RL J. Invest. Dermatol. 82:265-269(1984).
RN [19]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 623-1366, AND VARIANTS HIS-678; PHE-1022;
RP GLU-1189; PRO-1198 AND HIS-1354.
RX PubMed=6687691; DOI=10.1021/bi00274a023;
RA Bernard M.P., Myers J.C., Chu M.-L., Ramirez F., Eikenberry E.F.,
RA Prockop D.J.;
RT "Structure of a cDNA for the pro alpha 2 chain of human type I procollagen.
RT Comparison with chick cDNA for pro alpha 2(I) identifies structurally
RT conserved features of the protein and the gene.";
RL Biochemistry 22:1139-1145(1983).
RN [20]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 631-864, AND VARIANT OI2 676-GLY--ALA-855
RP DEL.
RX PubMed=1339453; DOI=10.1016/s0021-9258(18)42578-1;
RA Chessler S.D., Byers P.H.;
RT "Defective folding and stable association with protein disulfide
RT isomerase/prolyl hydroxylase of type I procollagen with a deletion in the
RT pro alpha 2(I) chain that preserves the Gly-X-Y repeat pattern.";
RL J. Biol. Chem. 267:7751-7757(1992).
RN [21]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 663-746, AND VARIANT OI3 VAL-676.
RX PubMed=7881420; DOI=10.1093/hmg/3.12.2201;
RA Forlino A., Zolezzi F., Valli M., Pignatti P.F., Cetta G., Brunelli P.C.,
RA Mottes M.;
RT "Severe (type III) osteogenesis imperfecta due to glycine substitutions in
RT the central domain of the collagen triple helix.";
RL Hum. Mol. Genet. 3:2201-2206(1994).
RN [22]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 960-1356, AND VARIANT HIS-1354.
RC TISSUE=Skin;
RX PubMed=2364107; DOI=10.1016/0167-4781(90)90037-3;
RA Maekelae J.K., Vuorio T., Vuorio E.;
RT "Growth-dependent modulation of type I collagen production and mRNA levels
RT in cultured human skin fibroblasts.";
RL Biochim. Biophys. Acta 1049:171-176(1990).
RN [23]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 964-1019.
RX PubMed=6267597; DOI=10.1073/pnas.78.6.3516;
RA Myers J.C., Chu M.-L., Faro S.H., Clark W.J., Prockop D.J., Ramirez F.;
RT "Cloning a cDNA for the pro-alpha 2 chain of human type I collagen.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:3516-3520(1981).
RN [24]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1090-1107, AND VARIANT OI4
RP ARG-1102.
RX PubMed=2897363; DOI=10.1016/s0021-9258(18)68560-6;
RA Wenstrup R.J., Cohn D.H., Cohen T., Byers P.H.;
RT "Arginine for glycine substitution in the triple-helical domain of the
RT products of one alpha 2(I) collagen allele (COL1A2) produces the
RT osteogenesis imperfecta type IV phenotype.";
RL J. Biol. Chem. 263:7734-7740(1988).
RN [25]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1319-1366, AND VARIANT HIS-1354.
RX PubMed=6309769; DOI=10.1016/s0021-9258(17)44615-1;
RA Myers J.C., Dickson L.A., de Wet W.J., Bernard M.P., Chu M.-L.,
RA Di Liberto M., Pepe G., Sangiorgi F.O., Ramirez F.;
RT "Analysis of the 3' end of the human pro-alpha 2(I) collagen gene.
RT Utilization of multiple polyadenylation sites in cultured fibroblasts.";
RL J. Biol. Chem. 258:10128-10135(1983).
RN [26]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1319-1366, AND VARIANT HIS-1354.
RC TISSUE=Skin;
RX PubMed=6092353; DOI=10.1016/s0021-9258(18)90635-6;
RA Pihlajaniemi T., Dickson L.A., Pope F.M., Korhonen V.R., Nicholls A.,
RA Prockop D.J., Myers J.C.;
RT "Osteogenesis imperfecta: cloning of a pro-alpha 2(I) collagen gene with a
RT frameshift mutation.";
RL J. Biol. Chem. 259:12941-12944(1984).
RN [27]
RP REVIEW ON VARIANTS.
RX PubMed=2010058; DOI=10.1096/fasebj.5.7.2010058;
RA Kuivaniemi H., Tromp G., Prockop D.J.;
RT "Mutations in collagen genes: causes of rare and some common diseases in
RT humans.";
RL FASEB J. 5:2052-2060(1991).
RN [28]
RP REVIEW ON VARIANTS.
RX PubMed=9101290;
RX DOI=10.1002/(sici)1098-1004(1997)9:4<300::aid-humu2>3.0.co;2-9;
RA Kuivaniemi H., Tromp G., Prockop D.J.;
RT "Mutations in fibrillar collagens (types I, II, III, and XI), fibril-
RT associated collagen (type IX), and network-forming collagen (type X) cause
RT a spectrum of diseases of bone, cartilage, and blood vessels.";
RL Hum. Mutat. 9:300-315(1997).
RN [29]
RP REVIEW ON OI VARIANTS.
RX PubMed=1895312; DOI=10.1136/jmg.28.7.433;
RA Byers P.H., Wallis G.A., Willing M.C.;
RT "Osteogenesis imperfecta: translation of mutation to phenotype.";
RL J. Med. Genet. 28:433-442(1991).
RN [30]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22905912; DOI=10.1021/pr300539b;
RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P.,
RA Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion profile.";
RL J. Proteome Res. 11:4733-4743(2012).
RN [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [32]
RP VARIANT OI2 ASP-997.
RX PubMed=2914942; DOI=10.1016/s0021-9258(19)81713-1;
RA Baldwin C.T., Constantinou C., Dumars K.W., Prockop D.J.;
RT "A single base mutation that converts glycine 907 of the alpha 2(I) chain
RT of type I procollagen to aspartate in a lethal variant of osteogenesis
RT imperfecta. The single amino acid substitution near the carboxyl terminus
RT destabilizes the whole triple helix.";
RL J. Biol. Chem. 264:3002-3006(1989).
RN [33]
RP VARIANT OI2 SER-955.
RX PubMed=2777764; DOI=10.1016/s0021-9258(18)71548-2;
RA Lamande S.R., Dahl H.-H.M., Cole W.G., Bateman J.F.;
RT "Characterization of point mutations in the collagen COL1A1 and COL1A2
RT genes causing lethal perinatal osteogenesis imperfecta.";
RL J. Biol. Chem. 264:15809-15812(1989).
RN [34]
RP VARIANT OI2 CYS-877.
RA Fertala A., Westerhausen A., Morris G.M., Rooney J.E., Prockop D.J.;
RT "Two cysteine substitutions in the type I procollagen genes (COL1A1 and
RT COL1A2) that cause lethal osteogenesis imperfecta. The location of glycine
RT substitutions does not in any simple way predict their effects on protein
RT function or phenotype.";
RL Am. J. Hum. Genet. 47:A216-A216(1990).
RN [35]
RP VARIANT OI4 VAL-676.
RX PubMed=2064612; DOI=10.1042/bj2760765;
RA Bateman J.F., Hannagan M., Chan D., Cole W.G.;
RT "Characterization of a type I collagen alpha 2(I) glycine-586 to valine
RT substitution in osteogenesis imperfecta type IV. Detection of the mutation
RT and prenatal diagnosis by a chemical cleavage method.";
RL Biochem. J. 276:765-770(1991).
RN [36]
RP VARIANT OI3 CYS-349, AND VARIANT OI1 CYS-736.
RX PubMed=1990009; DOI=10.1016/s0021-9258(18)52286-9;
RA Wenstrup R.J., Shrago-Howe A.W., Lever L.W., Phillips C.L., Byers P.H.,
RA Cohn D.H.;
RT "The effects of different cysteine for glycine substitutions within alpha
RT 2(I) chains. Evidence of distinct structural domains within the type I
RT collagen triple helix.";
RL J. Biol. Chem. 266:2590-2594(1991).
RN [37]
RP VARIANT OI2 ARG-784.
RX PubMed=1874719; DOI=10.1016/s0021-9258(18)98449-8;
RA Tsuneyoshi T., Westerhausen A., Constantinou C.D., Prockop D.J.;
RT "Substitutions for glycine alpha 1-637 and glycine alpha 2-694 of type I
RT procollagen in lethal osteogenesis imperfecta. The conformational strain on
RT the triple helix introduced by a glycine substitution can be transmitted
RT along the helix.";
RL J. Biol. Chem. 266:15608-15613(1991).
RN [38]
RP VARIANT OI4 SER-751.
RX PubMed=2052622; DOI=10.1073/pnas.88.12.5423;
RA Spotila L.D., Constantinou C.D., Sereda L., Ganguly A., Riggs B.L.,
RA Prockop D.J.;
RT "Mutation in a gene for type I procollagen (COL1A2) in a woman with
RT postmenopausal osteoporosis: evidence for phenotypic and genotypic overlap
RT with mild osteogenesis imperfecta.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:5423-5427(1991).
RN [39]
RP VARIANT OI2 ARG-547.
RX PubMed=1284475; DOI=10.1002/humu.1380010109;
RA Bateman J.F., Moeller I., Hannagan M., Chan D., Cole W.G.;
RT "Lethal perinatal osteogenesis imperfecta due to a type I collagen alpha
RT 2(I) Gly to Arg substitution detected by chemical cleavage of an mRNA:cDNA
RT sequence mismatch.";
RL Hum. Mutat. 1:55-62(1992).
RN [40]
RP VARIANT OI2 ASP-670.
RX PubMed=1385413; DOI=10.1016/s0021-9258(18)50063-6;
RA Niyibizi C., Bonadio J., Byers P.H., Eyre D.R.;
RT "Incorporation of type I collagen molecules that contain a mutant alpha
RT 2(I) chain (Gly580-->Asp) into bone matrix in a lethal case of osteogenesis
RT imperfecta.";
RL J. Biol. Chem. 267:23108-23112(1992).
RN [41]
RP VARIANT OI3 CYS-349, AND VARIANT OI1 CYS-736.
RX PubMed=8456807; DOI=10.1002/ajmg.1320450215;
RA Wenstrup R.J., Lever L.W., Phillips C.L., Quarles L.D.;
RT "Mutations in the COL1A2 gene of type I collagen that result in nonlethal
RT forms of osteogenesis imperfecta.";
RL Am. J. Med. Genet. 45:228-232(1993).
RN [42]
RP VARIANT ALA-549.
RX PubMed=8456808; DOI=10.1002/ajmg.1320450216;
RA Bateman J.F., Lamande S.R., Hannagan M., Moeller I., Dahl H.-H.M.,
RA Cole W.G.;
RT "Chemical cleavage method for the detection of RNA base changes: experience
RT in the application to collagen mutations in osteogenesis imperfecta.";
RL Am. J. Med. Genet. 45:233-240(1993).
RN [43]
RP VARIANT OI3 VAL-345 DEL.
RX PubMed=8444468; DOI=10.1007/bf00202479;
RA Molyneux K., Starman B.J., Byers P.H., Dalgleish R.;
RT "A single amino acid deletion in the alpha 2(I) chain of type I collagen
RT produces osteogenesis imperfecta type III.";
RL Hum. Genet. 90:621-628(1993).
RN [44]
RP VARIANT OI4 VAL-634.
RX PubMed=8401517; DOI=10.1093/hmg/2.8.1319;
RA Sztrolovics R., Glorieux F.H., van der Rest M., Roughley P.J.;
RT "Identification of type I collagen gene (COL1A2) mutations in nonlethal
RT osteogenesis imperfecta.";
RL Hum. Mol. Genet. 2:1319-1321(1993).
RN [45]
RP VARIANT OI2 GLU-433.
RX PubMed=7906591; DOI=10.1093/hmg/2.12.2175;
RA Rose N.J., Mackay K., Byers P.H., Dalgleish R.;
RT "A novel glycine to glutamic acid substitution at position 343 in the alpha
RT 2 chain of type I collagen in an individual with lethal osteogenesis
RT imperfecta.";
RL Hum. Mol. Genet. 2:2175-2177(1993).
RN [46]
RP VARIANT OI4 SER-1012.
RX PubMed=8094076; DOI=10.1016/s0021-9258(18)53826-6;
RA Marini J.C., Lewis M.B., Wang Q., Chen K.J., Orrison B.M.;
RT "Serine for glycine substitutions in type I collagen in two cases of type
RT IV osteogenesis imperfecta (OI). Additional evidence for a regional model
RT of OI pathophysiology.";
RL J. Biol. Chem. 268:2667-2673(1993).
RN [47]
RP VARIANT OI4 VAL-766, AND VARIANT OI2 SER-796.
RX PubMed=7693712; DOI=10.1016/s0021-9258(19)74583-9;
RA Wang Q., Orrison B.M., Marini J.C.;
RT "Two additional cases of osteogenesis imperfecta with substitutions for
RT glycine in the alpha 2(I) collagen chain. A regional model relating
RT mutation location with phenotype.";
RL J. Biol. Chem. 268:25162-25167(1993).
RN [48]
RP VARIANT OI3 ARG-517.
RX PubMed=7520724; DOI=10.1016/8756-3282(94)90295-x;
RA Sztrolovics R., Glorieux F.H., Travers R., van der Rest M., Roughley P.J.;
RT "Osteogenesis imperfecta: comparison of molecular defects with bone
RT histological changes.";
RL Bone 15:321-328(1994).
RN [49]
RP VARIANT OI2 SER-592.
RX PubMed=7959683; DOI=10.1007/bf00211014;
RA Rose N.J., Mackay K., de Paepe A., Steinmann B., Punnett H.H.,
RA Dalgleish R.;
RT "Three unrelated individuals with perinatally lethal osteogenesis
RT imperfecta resulting from identical Gly502Ser substitutions in the alpha 2-
RT chain of type I collagen.";
RL Hum. Genet. 94:497-503(1994).
RN [50]
RP VARIANT OI3 SER-949.
RX PubMed=8081394; DOI=10.1002/humu.1380030411;
RA Rose N.J., Mackay K., Byers P.H., Dalgleish R.;
RT "A Gly859Ser substitution in the triple helical domain of the alpha 2 chain
RT of type I collagen resulting in osteogenesis imperfecta type III in two
RT unrelated individuals.";
RL Hum. Mutat. 3:391-394(1994).
RN [51]
RP VARIANT OI2 ASP-790.
RX PubMed=8182080; DOI=10.1016/s0021-9258(17)36689-9;
RA Cohen-Solal L., Zylberberg L., Sangalli A., Gomez Lira M., Mottes M.;
RT "Substitution of an aspartic acid for glycine 700 in the alpha 2(I) chain
RT of type I collagen in a recurrent lethal type II osteogenesis imperfecta
RT dramatically affects the mineralization of bone.";
RL J. Biol. Chem. 269:14751-14758(1994).
RN [52]
RP VARIANT OI2 CYS-730.
RX PubMed=7891382; DOI=10.1136/jmg.31.12.965;
RA Gomez Lira M., Sangalli A., Pignatti P.F., Digilio M.C., Giannotti A.,
RA Carnevale E., Mottes M.;
RT "Determination of a new collagen type I alpha 2 gene point mutation which
RT causes a Gly640 Cys substitution in osteogenesis imperfecta and prenatal
RT diagnosis by DNA hybridisation.";
RL J. Med. Genet. 31:965-968(1994).
RN [53]
RP VARIANT OI3 SER-778.
RX PubMed=7720740; DOI=10.1007/bf01991915;
RA Raghunath M., Mackay K., Dalgleish R., Steinmann B.;
RT "Genetic counselling on brittle grounds: recurring osteogenesis imperfecta
RT due to parental mosaicism for a dominant mutation.";
RL Eur. J. Pediatr. 154:123-129(1995).
RN [54]
RP VARIANT OI3 SER-328.
RX PubMed=7860070; DOI=10.1007/bf00209405;
RA Rose N.J., Mackay K., Byers P.H., Dalgleish R.;
RT "A Gly238Ser substitution in the alpha 2 chain of type I collagen results
RT in osteogenesis imperfecta type III.";
RL Hum. Genet. 95:215-218(1995).
RN [55]
RP VARIANT OI3 ALA-1096.
RX PubMed=7749416; DOI=10.1002/humu.1380050212;
RA Lu J., Costa T., Cole W.G.;
RT "A novel G1006A substitution in the alpha 2(I) chain of type I collagen
RT produces osteogenesis imperfecta type III.";
RL Hum. Mutat. 5:175-178(1995).
RN [56]
RP VARIANT OI3 ASP-892, AND VARIANT OI4 ASP-892.
RX PubMed=8800927; DOI=10.1159/000472168;
RA Lund A.M., Schwartz M., Raghunath M., Steinmann B., Skovby F.;
RT "Gly802Asp substitution in the pro alpha 2(I) collagen chain in a family
RT with recurrent osteogenesis imperfecta due to paternal mosaicism.";
RL Eur. J. Hum. Genet. 4:39-45(1996).
RN [57]
RP VARIANTS OI1 ASP-211 AND SER-835, VARIANTS OI3 SER-337 AND SER-460, AND
RP VARIANT HIS-822.
RX PubMed=8829649;
RX DOI=10.1002/(sici)1098-1004(1996)7:2<89::aid-humu1>3.0.co;2-k;
RA Zhuang J., Tromp G., Kuivaniemi H., Castells S., Bugge M., Prockop D.J.;
RT "Direct sequencing of PCR products derived from cDNAs for the pro alpha 1
RT and pro alpha 2 chains of type I procollagen as a screening method to
RT detect mutations in patients with osteogenesis imperfecta.";
RL Hum. Mutat. 7:89-99(1996).
RN [58]
RP VARIANT OI3 PRO-1148.
RX PubMed=8723681;
RX DOI=10.1002/(sici)1098-1004(1996)7:4<318::aid-humu5>3.0.co;2-4;
RA Oliver J.E., Thompson E.M., Pope F.M., Nicholls A.C.;
RT "Mutation in the carboxy-terminal propeptide of the Pro alpha 1(I) chain of
RT type I collagen in a child with severe osteogenesis imperfecta (OI type
RT III): possible implications for protein folding.";
RL Hum. Mutat. 7:318-326(1996).
RN [59]
RP VARIANTS OI2 VAL-409 AND CYS-787.
RX PubMed=10627137;
RA Mottes M., Gomez Lira M., Zolezzi F., Valli M., Lisi V., Freising P.;
RT "Four new cases of lethal osteogenesis imperfecta due to glycine
RT substitutions in COL1A1 and genes.";
RL Hum. Mutat. 12:71-72(1998).
RN [60]
RP VARIANTS OI3 ASP-331; CYS-337 AND VAL-973.
RX PubMed=10408781;
RX DOI=10.1002/(sici)1098-1004(1999)13:6<503::aid-humu12>3.0.co;2-i;
RA Lund A.M., Astroem E., Soederhaell S., Schwartz M., Skovby F.;
RT "Osteogenesis imperfecta: mosaicism and refinement of the genotype-
RT phenotype map in OI type III.";
RL Hum. Mutat. 13:503-503(1999).
RN [61]
RP CHROMOSOMAL REARRANGEMENT WITH PLAG1.
RX PubMed=10987300;
RA Hibbard M.K., Kozakewich H.P., Dal Cin P., Sciot R., Tan X., Xiao S.,
RA Fletcher J.A.;
RT "PLAG1 fusion oncogenes in lipoblastoma.";
RL Cancer Res. 60:4869-4872(2000).
RN [62]
RP INVOLVEMENT IN CARDIAC VALVULAR EDS.
RX PubMed=15077201; DOI=10.1086/420794;
RA Schwarze U., Hata R., McKusick V.A., Shinkai H., Hoyme H.E., Pyeritz R.E.,
RA Byers P.H.;
RT "Rare autosomal recessive cardiac valvular form of Ehlers-Danlos syndrome
RT results from mutations in the COL1A2 gene that activate the nonsense-
RT mediated RNA decay pathway.";
RL Am. J. Hum. Genet. 74:917-930(2004).
RN [63]
RP INVOLVEMENT IN EDSCV.
RX PubMed=16816023; DOI=10.1136/jmg.2005.038224;
RA Malfait F., Symoens S., Coucke P., Nunes L., De Almeida S., De Paepe A.;
RT "Total absence of the alpha2(I) chain of collagen type I causes a rare form
RT of Ehlers-Danlos syndrome with hypermobility and propensity to cardiac
RT valvular problems.";
RL J. Med. Genet. 43:E36-E36(2006).
RN [64]
RP VARIANTS OI4 SER-193 AND CYS-754, VARIANT OI2 ASP-625, AND VARIANTS OI3
RP CYS-835 AND VAL-991.
RX PubMed=16879195; DOI=10.1111/j.1399-0004.2006.00646.x;
RA Venturi G., Tedeschi E., Mottes M., Valli M., Camilot M., Viglio S.,
RA Antoniazzi F., Tato L.;
RT "Osteogenesis imperfecta: clinical, biochemical and molecular findings.";
RL Clin. Genet. 70:131-139(2006).
RN [65]
RP VARIANTS OI1/OI3/OI4 GLU-325; SER-328; SER-358; SER-601; ASP-676; SER-820;
RP ARG-856; SER-1012; PRO-PRO-GLY-811 INS; VAL-GLY-PRO-989 INS AND
RP 1094-PRO--GLY-1096 DEL.
RX PubMed=16705691; DOI=10.1002/humu.9423;
RA Lee K.S., Song H.R., Cho T.J., Kim H.J., Lee T.M., Jin H.S., Park H.Y.,
RA Kang S., Jung S.C., Koo S.K.;
RT "Mutational spectrum of type I collagen genes in Korean patients with
RT osteogenesis imperfecta.";
RL Hum. Mutat. 27:599-599(2006).
RN [66]
RP VARIANTS OI4 ARG-202 AND VAL-256, VARIANTS OI1 ARG-247; ARG-319; CYS-733
RP AND TYR-1195, VARIANTS OI2 ASP-253; ASP-982 AND ASP-1003, AND VARIANT OI3
RP ASP-1087.
RX PubMed=16786509; DOI=10.1002/humu.9430;
RA Pollitt R., McMahon R., Nunn J., Bamford R., Afifi A., Bishop N.,
RA Dalton A.;
RT "Mutation analysis of COL1A1 and COL1A2 in patients diagnosed with
RT osteogenesis imperfecta type I-IV.";
RL Hum. Mutat. 27:716-716(2006).
RN [67]
RP VARIANTS SER-528; ALA-549 AND THR-564.
RX PubMed=18272325; DOI=10.1016/j.ygeno.2007.12.008;
RA Chan T.F., Poon A., Basu A., Addleman N.R., Chen J., Phong A., Byers P.H.,
RA Klein T.E., Kwok P.Y.;
RT "Natural variation in four human collagen genes across an ethnically
RT diverse population.";
RL Genomics 91:307-314(2008).
RN [68]
RP VARIANTS OI2 CYS-234; ARG-283; GLU-397; CYS-454; LEU-457; 461-PRO--GLY-466
RP DEL; GLU-526; VAL-562; 705-ALA--PRO-707 DEL; ARG-739; VAL-748; ASP-790;
RP PRO-798 INS; 806-PRO--GLY-811 DEL; VAL-856; SER-949; ASP-955; GLU-1027 AND
RP 1058-PRO--ALA-1062 DEL, AND VARIANT ALA-549.
RX PubMed=18996919; DOI=10.1093/hmg/ddn374;
RA Bodian D.L., Chan T.F., Poon A., Schwarze U., Yang K., Byers P.H.,
RA Kwok P.Y., Klein T.E.;
RT "Mutation and polymorphism spectrum in osteogenesis imperfecta type II:
RT implications for genotype-phenotype relationships.";
RL Hum. Mol. Genet. 18:463-471(2009).
RN [69]
RP VARIANT THR-1119, AND CHARACTERIZATION OF VARIANT THR-1119.
RX PubMed=21344539; DOI=10.1002/humu.21475;
RA Lindahl K., Barnes A.M., Fratzl-Zelman N., Whyte M.P., Hefferan T.E.,
RA Makareeva E., Brusel M., Yaszemski M.J., Rubin C.J., Kindmark A.,
RA Roschger P., Klaushofer K., McAlister W.H., Mumm S., Leikin S., Kessler E.,
RA Boskey A.L., Ljunggren O., Marini J.C.;
RT "COL1 C-propeptide cleavage site mutations cause high bone mass
RT osteogenesis imperfecta.";
RL Hum. Mutat. 32:598-609(2011).
RN [70]
RP VARIANT HIS-1067.
RX PubMed=23656646; DOI=10.1056/nejmoa1215458;
RA Laine C.M., Joeng K.S., Campeau P.M., Kiviranta R., Tarkkonen K.,
RA Grover M., Lu J.T., Pekkinen M., Wessman M., Heino T.J.,
RA Nieminen-Pihala V., Aronen M., Laine T., Kroeger H., Cole W.G.,
RA Lehesjoki A.E., Nevarez L., Krakow D., Curry C.J., Cohn D.H., Gibbs R.A.,
RA Lee B.H., Maekitie O.;
RT "WNT1 mutations in early-onset osteoporosis and osteogenesis imperfecta.";
RL N. Engl. J. Med. 368:1809-1816(2013).
RN [71]
RP VARIANTS OIEDS2 ASP-109 AND VAL-196, CHARACTERIZATION OF VARIANT OIEDS2
RP ASP-109, AND INVOLVEMENT IN OIEDS2.
RX PubMed=23692737; DOI=10.1186/1750-1172-8-78;
RA Malfait F., Symoens S., Goemans N., Gyftodimou Y., Holmberg E.,
RA Lopez-Gonzalez V., Mortier G., Nampoothiri S., Petersen M.B., De Paepe A.;
RT "Helical mutations in type I collagen that affect the processing of the
RT amino-propeptide result in an Osteogenesis Imperfecta/Ehlers-Danlos
RT Syndrome overlap syndrome.";
RL Orphanet J. Rare Dis. 8:78-78(2013).
CC -!- FUNCTION: Type I collagen is a member of group I collagen (fibrillar
CC forming collagen).
CC -!- SUBUNIT: Trimers of one alpha 2(I) and two alpha 1(I) chains.
CC -!- INTERACTION:
CC P08123; P02452: COL1A1; NbExp=5; IntAct=EBI-983038, EBI-982999;
CC P08123; O00303: EIF3F; NbExp=3; IntAct=EBI-983038, EBI-711990;
CC P08123; Q6PIL6: KCNIP4; NbExp=9; IntAct=EBI-983038, EBI-1051469;
CC P08123; Q14696: MESD; NbExp=3; IntAct=EBI-983038, EBI-6165891;
CC P08123; O43765: SGTA; NbExp=11; IntAct=EBI-983038, EBI-347996;
CC P08123; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-983038, EBI-744081;
CC P08123; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-983038, EBI-358489;
CC P08123; Q9UMX0: UBQLN1; NbExp=6; IntAct=EBI-983038, EBI-741480;
CC P08123; Q9UMX0-2: UBQLN1; NbExp=6; IntAct=EBI-983038, EBI-10173939;
CC P08123; Q9UHD9: UBQLN2; NbExp=5; IntAct=EBI-983038, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC -!- TISSUE SPECIFICITY: Forms the fibrils of tendon, ligaments and bones.
CC In bones the fibrils are mineralized with calcium hydroxyapatite.
CC -!- DOMAIN: The C-terminal propeptide, also known as COLFI domain, have
CC crucial roles in tissue growth and repair by controlling both the
CC intracellular assembly of procollagen molecules and the extracellular
CC assembly of collagen fibrils. It binds a calcium ion which is essential
CC for its function. {ECO:0000250}.
CC -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC (G-X-Y) are hydroxylated in some or all of the chains.
CC {ECO:0000269|PubMed:4412529}.
CC -!- DISEASE: Ehlers-Danlos syndrome, arthrochalasia type, 2 (EDSARTH2)
CC [MIM:617821]: A form of Ehlers-Danlos syndrome, a connective tissue
CC disorder characterized by hyperextensible skin, atrophic cutaneous
CC scars due to tissue fragility and joint hyperlaxity. EDSARTH2 is an
CC autosomal dominant condition characterized by frequent congenital hip
CC dislocation and extreme joint laxity with recurrent joint subluxations
CC and minimal skin involvement. {ECO:0000269|PubMed:1577745,
CC ECO:0000269|PubMed:2394758, ECO:0000269|PubMed:3680255}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Osteogenesis imperfecta 1 (OI1) [MIM:166200]: An autosomal
CC dominant form of osteogenesis imperfecta, a connective tissue disorder
CC characterized by low bone mass, bone fragility and susceptibility to
CC fractures after minimal trauma. Disease severity ranges from very mild
CC forms without fractures to intrauterine fractures and perinatal
CC lethality. Extraskeletal manifestations, which affect a variable number
CC of patients, are dentinogenesis imperfecta, hearing loss, and blue
CC sclerae. OI1 is a non-deforming form with normal height or mild short
CC stature, and no dentinogenesis imperfecta.
CC {ECO:0000269|PubMed:16705691, ECO:0000269|PubMed:16786509,
CC ECO:0000269|PubMed:1990009, ECO:0000269|PubMed:8456807,
CC ECO:0000269|PubMed:8829649}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Osteogenesis imperfecta 2 (OI2) [MIM:166210]: An autosomal
CC dominant form of osteogenesis imperfecta, a connective tissue disorder
CC characterized by low bone mass, bone fragility and susceptibility to
CC fractures after minimal trauma. Disease severity ranges from very mild
CC forms without fractures to intrauterine fractures and perinatal
CC lethality. Extraskeletal manifestations, which affect a variable number
CC of patients, are dentinogenesis imperfecta, hearing loss, and blue
CC sclerae. OI2 is characterized by bone fragility, with many perinatal
CC fractures, severe bowing of long bones, undermineralization, and death
CC in the perinatal period due to respiratory insufficiency.
CC {ECO:0000269|PubMed:10627137, ECO:0000269|PubMed:1284475,
CC ECO:0000269|PubMed:1339453, ECO:0000269|PubMed:1385413,
CC ECO:0000269|PubMed:16786509, ECO:0000269|PubMed:16879195,
CC ECO:0000269|PubMed:1874719, ECO:0000269|PubMed:18996919,
CC ECO:0000269|PubMed:2777764, ECO:0000269|PubMed:2914942,
CC ECO:0000269|PubMed:7693712, ECO:0000269|PubMed:7891382,
CC ECO:0000269|PubMed:7906591, ECO:0000269|PubMed:7959683,
CC ECO:0000269|PubMed:8182080, ECO:0000269|Ref.34}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Ehlers-Danlos syndrome, cardiac valvular type (EDSCV)
CC [MIM:225320]: A form of Ehlers-Danlos syndrome, a group of connective
CC tissue disorders characterized by skin hyperextensibility, articular
CC hypermobility, and tissue fragility. EDSCV is an autosomal recessive
CC disease characterized by mitral valve prolapse and insufficiency,
CC mitral regurgitation, and aortic insufficiency, in addition to joint
CC laxity, skin hyperextensibility and friability, and abnormal scar
CC formation. {ECO:0000269|PubMed:16816023}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Osteogenesis imperfecta 3 (OI3) [MIM:259420]: An autosomal
CC dominant form of osteogenesis imperfecta, a connective tissue disorder
CC characterized by low bone mass, bone fragility and susceptibility to
CC fractures after minimal trauma. Disease severity ranges from very mild
CC forms without fractures to intrauterine fractures and perinatal
CC lethality. Extraskeletal manifestations, which affect a variable number
CC of patients, are dentinogenesis imperfecta, hearing loss, and blue
CC sclerae. OI3 is characterized by progressively deforming bones, very
CC short stature, a triangular face, severe scoliosis, grayish sclera and
CC dentinogenesis imperfecta. {ECO:0000269|PubMed:10408781,
CC ECO:0000269|PubMed:16786509, ECO:0000269|PubMed:16879195,
CC ECO:0000269|PubMed:1990009, ECO:0000269|PubMed:7520724,
CC ECO:0000269|PubMed:7720740, ECO:0000269|PubMed:7749416,
CC ECO:0000269|PubMed:7860070, ECO:0000269|PubMed:7881420,
CC ECO:0000269|PubMed:8081394, ECO:0000269|PubMed:8444468,
CC ECO:0000269|PubMed:8456807, ECO:0000269|PubMed:8723681,
CC ECO:0000269|PubMed:8800927, ECO:0000269|PubMed:8829649}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Osteogenesis imperfecta 4 (OI4) [MIM:166220]: An autosomal
CC dominant form of osteogenesis imperfecta, a connective tissue disorder
CC characterized by low bone mass, bone fragility and susceptibility to
CC fractures after minimal trauma. Disease severity ranges from very mild
CC forms without fractures to intrauterine fractures and perinatal
CC lethality. Extraskeletal manifestations, which affect a variable number
CC of patients, are dentinogenesis imperfecta, hearing loss, and blue
CC sclerae. OI4 is characterized by moderately short stature, mild to
CC moderate scoliosis, grayish or white sclera and dentinogenesis
CC imperfecta. {ECO:0000269|PubMed:1642148, ECO:0000269|PubMed:16786509,
CC ECO:0000269|PubMed:16879195, ECO:0000269|PubMed:2052622,
CC ECO:0000269|PubMed:2064612, ECO:0000269|PubMed:2897363,
CC ECO:0000269|PubMed:7693712, ECO:0000269|PubMed:8094076,
CC ECO:0000269|PubMed:8401517, ECO:0000269|PubMed:8800927}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Combined osteogenesis imperfecta and Ehlers-Danlos syndrome 2
CC (OIEDS2) [MIM:619120]: An autosomal dominant connective tissue disorder
CC characterized by osteopenia, bone fragility, long bone fractures, blue
CC sclerae, joint hyperextensibility, soft and hyperextensible skin,
CC abnormal wound healing, easy bruising, and vascular fragility.
CC {ECO:0000269|PubMed:23692737}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Note=A chromosomal aberration involving COL1A2 may be a cause
CC of lipoblastomas, which are benign tumors resulting from transformation
CC of adipocytes, usually diagnosed in children. Translocation
CC t(7;8)(p22;q13) with PLAG1.
CC -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/COL1A2ID411ch7q22.html";
CC -!- WEB RESOURCE: Name=Osteogenesis imperfecta variant database;
CC Note=Collagen type I alpha 2 (COL1A2);
CC URL="http://oi.gene.le.ac.uk/home.php?select_db=COL1A2";
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DR EMBL; J03464; AAB59374.1; -; mRNA.
DR EMBL; Z74616; CAA98969.1; -; mRNA.
DR EMBL; AF004877; AAB93981.1; -; Genomic_DNA.
DR EMBL; BC042586; AAH42586.1; -; mRNA.
DR EMBL; BC054498; AAH54498.1; -; mRNA.
DR EMBL; Y00724; CAA68709.1; -; mRNA.
DR EMBL; X02488; CAA26320.1; -; mRNA.
DR EMBL; AB004317; BAA25383.1; -; Genomic_DNA.
DR EMBL; M35391; AAA60041.1; -; Genomic_DNA.
DR EMBL; S98904; AAB22126.1; -; Genomic_DNA.
DR EMBL; M21671; AAA59994.1; -; Genomic_DNA.
DR EMBL; S41099; AAB22761.1; -; mRNA.
DR EMBL; AC002528; AAB69977.1; -; Genomic_DNA.
DR EMBL; M21353; AAA52053.1; -; Genomic_DNA.
DR EMBL; M28985; AAA60356.1; -; Genomic_DNA.
DR EMBL; V00503; CAA23761.1; -; mRNA.
DR EMBL; S96821; AAB22020.2; -; mRNA.
DR EMBL; L47668; AAB59577.1; -; mRNA.
DR EMBL; X55525; CAA39142.1; -; mRNA.
DR EMBL; J00114; AAA51996.1; -; mRNA.
DR EMBL; M22816; AAA51844.1; -; mRNA.
DR EMBL; M22817; AAA51846.1; -; Genomic_DNA.
DR EMBL; K01078; AAA51887.1; -; Genomic_DNA.
DR EMBL; K02568; AAA51850.1; -; Genomic_DNA.
DR CCDS; CCDS34682.1; -.
DR PIR; A28500; CGHU2S.
DR RefSeq; NP_000080.2; NM_000089.3.
DR PDB; 5CTD; X-ray; 1.60 A; B=484-495.
DR PDB; 5CTI; X-ray; 1.90 A; B=484-495.
DR PDB; 5CVA; X-ray; 2.10 A; A/D=484-495.
DR PDB; 6JEC; X-ray; 2.05 A; A/B/C=45-72.
DR PDBsum; 5CTD; -.
DR PDBsum; 5CTI; -.
DR PDBsum; 5CVA; -.
DR PDBsum; 6JEC; -.
DR AlphaFoldDB; P08123; -.
DR SMR; P08123; -.
DR BioGRID; 107675; 49.
DR ComplexPortal; CPX-1650; Collagen type I trimer.
DR DIP; DIP-36079N; -.
DR IntAct; P08123; 34.
DR MINT; P08123; -.
DR STRING; 9606.ENSP00000297268; -.
DR ChEMBL; CHEMBL2685; -.
DR GlyConnect; 1135; 7 N-Linked glycans (1 site).
DR GlyGen; P08123; 5 sites, 7 N-linked glycans (1 site), 2 O-linked glycans (3 sites).
DR iPTMnet; P08123; -.
DR MetOSite; P08123; -.
DR PhosphoSitePlus; P08123; -.
DR BioMuta; COL1A2; -.
DR DMDM; 296439507; -.
DR EPD; P08123; -.
DR jPOST; P08123; -.
DR MassIVE; P08123; -.
DR MaxQB; P08123; -.
DR PaxDb; P08123; -.
DR PeptideAtlas; P08123; -.
DR PRIDE; P08123; -.
DR ProteomicsDB; 52070; -.
DR ABCD; P08123; 1 sequenced antibody.
DR Antibodypedia; 15754; 448 antibodies from 35 providers.
DR DNASU; 1278; -.
DR Ensembl; ENST00000297268.11; ENSP00000297268.6; ENSG00000164692.19.
DR GeneID; 1278; -.
DR KEGG; hsa:1278; -.
DR MANE-Select; ENST00000297268.11; ENSP00000297268.6; NM_000089.4; NP_000080.2.
DR UCSC; uc003ung.1; human.
DR CTD; 1278; -.
DR DisGeNET; 1278; -.
DR GeneCards; COL1A2; -.
DR GeneReviews; COL1A2; -.
DR HGNC; HGNC:2198; COL1A2.
DR HPA; ENSG00000164692; Tissue enhanced (cervix, gallbladder, smooth muscle).
DR MalaCards; COL1A2; -.
DR MIM; 120160; gene.
DR MIM; 166200; phenotype.
DR MIM; 166210; phenotype.
DR MIM; 166220; phenotype.
DR MIM; 225320; phenotype.
DR MIM; 259420; phenotype.
DR MIM; 617821; phenotype.
DR MIM; 619120; phenotype.
DR neXtProt; NX_P08123; -.
DR OpenTargets; ENSG00000164692; -.
DR Orphanet; 1899; Arthrochalasia Ehlers-Danlos syndrome.
DR Orphanet; 230851; Cardiac-valvular Ehlers-Danlos syndrome.
DR Orphanet; 230857; Ehlers-Danlos/osteogenesis imperfecta syndrome.
DR Orphanet; 314029; High bone mass osteogenesis imperfecta.
DR Orphanet; 216796; Osteogenesis imperfecta type 1.
DR Orphanet; 216804; Osteogenesis imperfecta type 2.
DR Orphanet; 216812; Osteogenesis imperfecta type 3.
DR Orphanet; 216820; Osteogenesis imperfecta type 4.
DR PharmGKB; PA35042; -.
DR VEuPathDB; HostDB:ENSG00000164692; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000155639; -.
DR InParanoid; P08123; -.
DR OMA; SFYWIDP; -.
DR OrthoDB; 1406711at2759; -.
DR PhylomeDB; P08123; -.
DR TreeFam; TF344135; -.
DR PathwayCommons; P08123; -.
DR Reactome; R-HSA-114604; GPVI-mediated activation cascade.
DR Reactome; R-HSA-1442490; Collagen degradation.
DR Reactome; R-HSA-1474244; Extracellular matrix organization.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-2214320; Anchoring fibril formation.
DR Reactome; R-HSA-2243919; Crosslinking of collagen fibrils.
DR Reactome; R-HSA-3000170; Syndecan interactions.
DR Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR Reactome; R-HSA-3000480; Scavenging by Class A Receptors.
DR Reactome; R-HSA-430116; GP1b-IX-V activation signalling.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-75892; Platelet Adhesion to exposed collagen.
DR Reactome; R-HSA-76009; Platelet Aggregation (Plug Formation).
DR Reactome; R-HSA-8874081; MET activates PTK2 signaling.
DR Reactome; R-HSA-8948216; Collagen chain trimerization.
DR SignaLink; P08123; -.
DR SIGNOR; P08123; -.
DR BioGRID-ORCS; 1278; 12 hits in 1079 CRISPR screens.
DR ChiTaRS; COL1A2; human.
DR GeneWiki; COL1A2; -.
DR GenomeRNAi; 1278; -.
DR Pharos; P08123; Tbio.
DR PRO; PR:P08123; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P08123; protein.
DR Bgee; ENSG00000164692; Expressed in periodontal ligament and 211 other tissues.
DR ExpressionAtlas; P08123; baseline and differential.
DR Genevisible; P08123; HS.
DR GO; GO:0005584; C:collagen type I trimer; IDA:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; HDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048407; F:platelet-derived growth factor binding; IDA:MGI.
DR GO; GO:0002020; F:protease binding; IPI:CAFA.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IMP:UniProtKB.
DR GO; GO:0046332; F:SMAD binding; IEA:Ensembl.
DR GO; GO:0001568; P:blood vessel development; IMP:UniProtKB.
DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR GO; GO:0030199; P:collagen fibril organization; IMP:UniProtKB.
DR GO; GO:0032963; P:collagen metabolic process; IEA:Ensembl.
DR GO; GO:0085029; P:extracellular matrix assembly; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0042476; P:odontogenesis; NAS:UniProtKB.
DR GO; GO:0070208; P:protein heterotrimerization; IEA:Ensembl.
DR GO; GO:0008217; P:regulation of blood pressure; IMP:UniProtKB.
DR GO; GO:0007266; P:Rho protein signal transduction; IDA:UniProtKB.
DR GO; GO:0001501; P:skeletal system development; IMP:UniProtKB.
DR GO; GO:0043589; P:skin morphogenesis; IMP:UniProtKB.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR000885; Fib_collagen_C.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 6.
DR SMART; SM00038; COLFI; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Chromosomal rearrangement; Collagen;
KW Direct protein sequencing; Disease variant; Disulfide bond; Dwarfism;
KW Ehlers-Danlos syndrome; Extracellular matrix; Glycoprotein; Hydroxylation;
KW Metal-binding; Osteogenesis imperfecta; Pyrrolidone carboxylic acid;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000250|UniProtKB:P02466"
FT PROPEP 23..79
FT /note="N-terminal propeptide"
FT /evidence="ECO:0000269|PubMed:5529814"
FT /id="PRO_0000005804"
FT CHAIN 80..1119
FT /note="Collagen alpha-2(I) chain"
FT /id="PRO_0000005805"
FT PROPEP 1120..1366
FT /note="C-terminal propeptide"
FT /id="PRO_0000005806"
FT DOMAIN 1133..1366
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT REGION 28..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..72
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..814
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1102
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1181
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 1183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 1184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 1186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 1189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT MOD_RES 23
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:2394758"
FT MOD_RES 47
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2394758,
FT ECO:0000269|PubMed:3680255"
FT MOD_RES 50
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2394758,
FT ECO:0000269|PubMed:3680255"
FT MOD_RES 62
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2394758,
FT ECO:0000269|PubMed:3680255"
FT MOD_RES 65
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2394758,
FT ECO:0000269|PubMed:3680255"
FT MOD_RES 68
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2394758,
FT ECO:0000269|PubMed:3680255"
FT MOD_RES 71
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2394758,
FT ECO:0000269|PubMed:3680255"
FT MOD_RES 80
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:5529814"
FT MOD_RES 84
FT /note="Allysine"
FT /evidence="ECO:0000269|PubMed:5529814"
FT MOD_RES 102
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3680255"
FT MOD_RES 108
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3680255"
FT MOD_RES 177
FT /note="5-hydroxylysine; alternate"
FT /evidence="ECO:0000269|PubMed:4319110"
FT MOD_RES 420
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:4412529"
FT MOD_RES 441
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:4412529"
FT MOD_RES 444
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:4412529"
FT CARBOHYD 177
FT /note="O-linked (Gal...) hydroxylysine; alternate"
FT /evidence="ECO:0000269|PubMed:4319110"
FT CARBOHYD 1267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1163..1195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1203..1364
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1272..1317
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT VARIANT 59
FT /note="T -> P (in dbSNP:rs1800221)"
FT /evidence="ECO:0000269|PubMed:4011429"
FT /id="VAR_030116"
FT VARIANT 76..93
FT /note="Missing (in EDSARTH2)"
FT /evidence="ECO:0000269|PubMed:1577745,
FT ECO:0000269|PubMed:2394758, ECO:0000269|PubMed:3680255"
FT /id="VAR_001851"
FT VARIANT 109
FT /note="G -> D (in OIEDS2; decreased N-terminal propeptide
FT processing; dbSNP:rs1114167416)"
FT /evidence="ECO:0000269|PubMed:23692737"
FT /id="VAR_085153"
FT VARIANT 181..198
FT /note="Missing (in OI4)"
FT /evidence="ECO:0000269|PubMed:1642148"
FT /id="VAR_030117"
FT VARIANT 193
FT /note="G -> S (in OI4; dbSNP:rs72656370)"
FT /evidence="ECO:0000269|PubMed:16879195"
FT /id="VAR_063343"
FT VARIANT 196
FT /note="G -> V (in OIEDS2)"
FT /evidence="ECO:0000269|PubMed:23692737"
FT /id="VAR_085154"
FT VARIANT 202
FT /note="G -> R (in OI4; dbSNP:rs72656376)"
FT /evidence="ECO:0000269|PubMed:16786509"
FT /id="VAR_063344"
FT VARIANT 211
FT /note="G -> D (in OI1; dbSNP:rs72656378)"
FT /evidence="ECO:0000269|PubMed:8829649"
FT /id="VAR_001852"
FT VARIANT 234
FT /note="R -> C (in OI2; dbSNP:rs1206388800)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063345"
FT VARIANT 247
FT /note="G -> R (in OI1)"
FT /evidence="ECO:0000269|PubMed:16786509"
FT /id="VAR_063346"
FT VARIANT 249
FT /note="I -> N (in dbSNP:rs1800228)"
FT /evidence="ECO:0000269|PubMed:2824475"
FT /id="VAR_001853"
FT VARIANT 253
FT /note="G -> D (in OI2; dbSNP:rs72656385)"
FT /evidence="ECO:0000269|PubMed:16786509"
FT /id="VAR_063347"
FT VARIANT 256
FT /note="G -> V (in OI4; dbSNP:rs67525025)"
FT /evidence="ECO:0000269|PubMed:16786509"
FT /id="VAR_063348"
FT VARIANT 270
FT /note="V -> I (in dbSNP:rs368468)"
FT /evidence="ECO:0000269|PubMed:9443882"
FT /id="VAR_030118"
FT VARIANT 276
FT /note="A -> T (in dbSNP:rs1800231)"
FT /evidence="ECO:0000269|PubMed:2824475"
FT /id="VAR_001854"
FT VARIANT 283
FT /note="G -> R (in OI2)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063349"
FT VARIANT 319
FT /note="G -> R (in OI1; dbSNP:rs72656393)"
FT /evidence="ECO:0000269|PubMed:16786509"
FT /id="VAR_063350"
FT VARIANT 325
FT /note="G -> E (in OI4; dbSNP:rs72656395)"
FT /evidence="ECO:0000269|PubMed:16705691"
FT /id="VAR_063351"
FT VARIANT 328
FT /note="G -> S (in OI1, OI3 AND OI4; dbSNP:rs66612022)"
FT /evidence="ECO:0000269|PubMed:16705691,
FT ECO:0000269|PubMed:7860070"
FT /id="VAR_001855"
FT VARIANT 331
FT /note="G -> D (in OI3; dbSNP:rs67729041)"
FT /evidence="ECO:0000269|PubMed:10408781"
FT /id="VAR_008119"
FT VARIANT 334
FT /note="G -> C (in OI2)"
FT /id="VAR_001856"
FT VARIANT 337
FT /note="G -> C (in OI3; dbSNP:rs67865220)"
FT /evidence="ECO:0000269|PubMed:10408781"
FT /id="VAR_001857"
FT VARIANT 337
FT /note="G -> S (in OI3; dbSNP:rs67865220)"
FT /evidence="ECO:0000269|PubMed:8829649"
FT /id="VAR_001858"
FT VARIANT 344
FT /note="L -> V (in dbSNP:rs16868573)"
FT /id="VAR_055677"
FT VARIANT 345
FT /note="Missing (in OI3)"
FT /evidence="ECO:0000269|PubMed:8444468"
FT /id="VAR_001859"
FT VARIANT 349
FT /note="G -> C (in OI3; dbSNP:rs66773001)"
FT /evidence="ECO:0000269|PubMed:1990009,
FT ECO:0000269|PubMed:8456807"
FT /id="VAR_001860"
FT VARIANT 358
FT /note="G -> S (in OI3; dbSNP:rs66619856)"
FT /evidence="ECO:0000269|PubMed:16705691"
FT /id="VAR_063352"
FT VARIANT 397
FT /note="G -> E (in OI2)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063353"
FT VARIANT 409
FT /note="G -> V (in OI2; dbSNP:rs72658109)"
FT /evidence="ECO:0000269|PubMed:10627137"
FT /id="VAR_001861"
FT VARIANT 433
FT /note="G -> E (in OI2; dbSNP:rs72658114)"
FT /evidence="ECO:0000269|PubMed:7906591"
FT /id="VAR_001862"
FT VARIANT 454
FT /note="G -> C (in OI2; dbSNP:rs72658117)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063354"
FT VARIANT 457
FT /note="G -> L (in OI2; requires 2 nucleotide
FT substitutions)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063355"
FT VARIANT 460
FT /note="G -> S (in OI3; dbSNP:rs72658118)"
FT /evidence="ECO:0000269|PubMed:8829649"
FT /id="VAR_001863"
FT VARIANT 461..466
FT /note="Missing (in OI2)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063356"
FT VARIANT 483
FT /note="A -> V (in dbSNP:rs414408)"
FT /evidence="ECO:0000269|PubMed:2824475,
FT ECO:0000269|PubMed:9443882"
FT /id="VAR_030119"
FT VARIANT 511
FT /note="G -> D (in OI2; dbSNP:rs66999265)"
FT /id="VAR_001864"
FT VARIANT 517
FT /note="G -> R (in OI3; dbSNP:rs72658126)"
FT /evidence="ECO:0000269|PubMed:7520724"
FT /id="VAR_001865"
FT VARIANT 526
FT /note="G -> E (in OI2; dbSNP:rs72658130)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063357"
FT VARIANT 528
FT /note="N -> S (in dbSNP:rs41317144)"
FT /evidence="ECO:0000269|PubMed:18272325"
FT /id="VAR_033040"
FT VARIANT 547
FT /note="G -> R (in OI2; dbSNP:rs72658136)"
FT /evidence="ECO:0000269|PubMed:1284475"
FT /id="VAR_001866"
FT VARIANT 549
FT /note="P -> A (in dbSNP:rs42524)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:18272325, ECO:0000269|PubMed:18996919,
FT ECO:0000269|PubMed:2824475, ECO:0000269|PubMed:2839839,
FT ECO:0000269|PubMed:8456808, ECO:0000269|PubMed:9016532"
FT /id="VAR_001867"
FT VARIANT 562
FT /note="G -> C (in OI2; dbSNP:rs72658138)"
FT /id="VAR_001868"
FT VARIANT 562
FT /note="G -> V (in OI2)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063358"
FT VARIANT 564
FT /note="A -> T (in dbSNP:rs41317153)"
FT /evidence="ECO:0000269|PubMed:18272325"
FT /id="VAR_033041"
FT VARIANT 586
FT /note="G -> R (in OI2; dbSNP:rs72658139)"
FT /id="VAR_001869"
FT VARIANT 592
FT /note="G -> S (in OI2; dbSNP:rs72658141)"
FT /evidence="ECO:0000269|PubMed:7959683"
FT /id="VAR_001870"
FT VARIANT 601
FT /note="G -> S (in OI; dbSNP:rs72658143)"
FT /evidence="ECO:0000269|PubMed:16705691"
FT /id="VAR_063359"
FT VARIANT 625
FT /note="G -> D (in OI2; dbSNP:rs72658145)"
FT /evidence="ECO:0000269|PubMed:16879195"
FT /id="VAR_063360"
FT VARIANT 634
FT /note="G -> V (in OI4; dbSNP:rs72658147)"
FT /evidence="ECO:0000269|PubMed:8401517"
FT /id="VAR_001871"
FT VARIANT 637
FT /note="G -> D (in OI2; dbSNP:rs72658148)"
FT /id="VAR_001872"
FT VARIANT 640
FT /note="G -> S (in OI2)"
FT /id="VAR_001873"
FT VARIANT 670
FT /note="G -> D (in OI2; dbSNP:rs72658155)"
FT /evidence="ECO:0000269|PubMed:1385413"
FT /id="VAR_001874"
FT VARIANT 676..855
FT /note="Missing (in OI2)"
FT /evidence="ECO:0000269|PubMed:1339453"
FT /id="VAR_030120"
FT VARIANT 676
FT /note="G -> D (in OI3; dbSNP:rs66883877)"
FT /evidence="ECO:0000269|PubMed:16705691"
FT /id="VAR_063361"
FT VARIANT 676
FT /note="G -> V (in OI3 and OI4; dbSNP:rs66883877)"
FT /evidence="ECO:0000269|PubMed:2064612,
FT ECO:0000269|PubMed:7881420"
FT /id="VAR_001875"
FT VARIANT 678
FT /note="P -> H (in dbSNP:rs409108)"
FT /evidence="ECO:0000269|PubMed:2824475,
FT ECO:0000269|PubMed:3421913, ECO:0000269|PubMed:6687691,
FT ECO:0000269|PubMed:9016532, ECO:0000269|PubMed:9443882"
FT /id="VAR_030121"
FT VARIANT 705..707
FT /note="Missing (in OI2)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063362"
FT VARIANT 708
FT /note="R -> Q (found in a patient with a variant form of
FT Marfan syndrome; unknown pathological significance;
FT dbSNP:rs72658163)"
FT /id="VAR_001876"
FT VARIANT 715
FT /note="G -> D (in OI2; dbSNP:rs72658167)"
FT /id="VAR_001877"
FT VARIANT 730
FT /note="G -> C (in OI2; dbSNP:rs72658171)"
FT /evidence="ECO:0000269|PubMed:7891382"
FT /id="VAR_001878"
FT VARIANT 733
FT /note="G -> C (in OI1; dbSNP:rs72658172)"
FT /evidence="ECO:0000269|PubMed:16786509"
FT /id="VAR_063363"
FT VARIANT 736
FT /note="G -> C (in OI1; mild; dbSNP:rs72658173)"
FT /evidence="ECO:0000269|PubMed:1990009,
FT ECO:0000269|PubMed:8456807"
FT /id="VAR_001879"
FT VARIANT 739
FT /note="G -> R (in OI2; dbSNP:rs72658174)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063364"
FT VARIANT 743
FT /note="A -> G (in dbSNP:rs408535)"
FT /evidence="ECO:0000269|PubMed:2824475,
FT ECO:0000269|PubMed:3421913, ECO:0000269|PubMed:9443882"
FT /id="VAR_001880"
FT VARIANT 748
FT /note="G -> V (in OI2)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063365"
FT VARIANT 751
FT /note="G -> S (in OI4; dbSNP:rs72658176)"
FT /evidence="ECO:0000269|PubMed:2052622"
FT /id="VAR_001881"
FT VARIANT 754
FT /note="G -> C (in OI4; dbSNP:rs72658177)"
FT /evidence="ECO:0000269|PubMed:16879195"
FT /id="VAR_063366"
FT VARIANT 754
FT /note="G -> R (in OI2)"
FT /id="VAR_001882"
FT VARIANT 766
FT /note="G -> V (in OI4; dbSNP:rs72658183)"
FT /evidence="ECO:0000269|PubMed:7693712"
FT /id="VAR_001883"
FT VARIANT 778
FT /note="G -> S (in OI3; dbSNP:rs72658186)"
FT /evidence="ECO:0000269|PubMed:7720740"
FT /id="VAR_001884"
FT VARIANT 784
FT /note="G -> R (in OI2; dbSNP:rs66592844)"
FT /evidence="ECO:0000269|PubMed:1874719"
FT /id="VAR_001885"
FT VARIANT 787
FT /note="G -> C (in OI2; dbSNP:rs72658187)"
FT /evidence="ECO:0000269|PubMed:10627137"
FT /id="VAR_001886"
FT VARIANT 790
FT /note="G -> D (in OI2; dbSNP:rs72658188)"
FT /evidence="ECO:0000269|PubMed:18996919,
FT ECO:0000269|PubMed:8182080"
FT /id="VAR_001887"
FT VARIANT 796
FT /note="G -> S (in OI2; dbSNP:rs66716547)"
FT /evidence="ECO:0000269|PubMed:7693712"
FT /id="VAR_001888"
FT VARIANT 798
FT /note="P -> PP (in OI2)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063367"
FT VARIANT 806..811
FT /note="Missing (in OI2)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063368"
FT VARIANT 811
FT /note="G -> GPPG (in OI4)"
FT /id="VAR_063369"
FT VARIANT 820
FT /note="G -> S (in OI3; dbSNP:rs72658191)"
FT /evidence="ECO:0000269|PubMed:16705691"
FT /id="VAR_063370"
FT VARIANT 822
FT /note="R -> H (in dbSNP:rs1800240)"
FT /evidence="ECO:0000269|PubMed:8829649"
FT /id="VAR_001889"
FT VARIANT 835
FT /note="G -> C (in OI3)"
FT /evidence="ECO:0000269|PubMed:16879195"
FT /id="VAR_063371"
FT VARIANT 835
FT /note="G -> S (in OI1; dbSNP:rs72658193)"
FT /evidence="ECO:0000269|PubMed:8829649"
FT /id="VAR_001890"
FT VARIANT 856
FT /note="G -> R (in OI3)"
FT /evidence="ECO:0000269|PubMed:16705691"
FT /id="VAR_063372"
FT VARIANT 856
FT /note="G -> V (in OI2)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063373"
FT VARIANT 877
FT /note="G -> C (in OI2; dbSNP:rs72658201)"
FT /evidence="ECO:0000269|Ref.34"
FT /id="VAR_001891"
FT VARIANT 892
FT /note="G -> D (in OI3 and OI4; dbSNP:rs72659304)"
FT /evidence="ECO:0000269|PubMed:8800927"
FT /id="VAR_001892"
FT VARIANT 895
FT /note="G -> D (in OI2; dbSNP:rs72659305)"
FT /id="VAR_001893"
FT VARIANT 949
FT /note="G -> S (in OI3; moderate; dbSNP:rs72659312)"
FT /evidence="ECO:0000269|PubMed:18996919,
FT ECO:0000269|PubMed:8081394"
FT /id="VAR_001894"
FT VARIANT 955
FT /note="G -> D (in OI2)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063374"
FT VARIANT 955
FT /note="G -> S (in OI2; dbSNP:rs66507857)"
FT /evidence="ECO:0000269|PubMed:2777764"
FT /id="VAR_001895"
FT VARIANT 973
FT /note="G -> V (in OI3; dbSNP:rs67609234)"
FT /evidence="ECO:0000269|PubMed:10408781"
FT /id="VAR_008120"
FT VARIANT 982
FT /note="G -> D (in OI2; dbSNP:rs67422093)"
FT /evidence="ECO:0000269|PubMed:16786509"
FT /id="VAR_063375"
FT VARIANT 989
FT /note="P -> PVGP (in OI4)"
FT /id="VAR_063376"
FT VARIANT 991
FT /note="G -> V (in OI3; dbSNP:rs72659316)"
FT /evidence="ECO:0000269|PubMed:16879195"
FT /id="VAR_063377"
FT VARIANT 997
FT /note="G -> D (in OI2; dbSNP:rs72659317)"
FT /evidence="ECO:0000269|PubMed:2914942"
FT /id="VAR_001896"
FT VARIANT 1003
FT /note="G -> D (in OI2; dbSNP:rs1114167414)"
FT /evidence="ECO:0000269|PubMed:16786509"
FT /id="VAR_063378"
FT VARIANT 1012
FT /note="G -> S (in OI3 and OI4; moderate; dbSNP:rs72659319)"
FT /evidence="ECO:0000269|PubMed:16705691,
FT ECO:0000269|PubMed:8094076"
FT /id="VAR_001897"
FT VARIANT 1022
FT /note="L -> F (in dbSNP:rs392609)"
FT /evidence="ECO:0000269|PubMed:2824475,
FT ECO:0000269|PubMed:6687691, ECO:0000269|PubMed:9443882"
FT /id="VAR_001898"
FT VARIANT 1027
FT /note="G -> E (in OI2; dbSNP:rs72659323)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063379"
FT VARIANT 1058..1062
FT /note="Missing (in OI2)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063380"
FT VARIANT 1066
FT /note="G -> D (in OI2; dbSNP:rs72659331)"
FT /id="VAR_001899"
FT VARIANT 1067
FT /note="R -> H (in dbSNP:rs530026906)"
FT /evidence="ECO:0000269|PubMed:23656646"
FT /id="VAR_069633"
FT VARIANT 1078
FT /note="G -> C (in OI2)"
FT /id="VAR_001900"
FT VARIANT 1087
FT /note="G -> D (in OI3; dbSNP:rs72659335)"
FT /evidence="ECO:0000269|PubMed:16786509"
FT /id="VAR_063381"
FT VARIANT 1094..1096
FT /note="Missing (in OI4)"
FT /evidence="ECO:0000269|PubMed:16705691"
FT /id="VAR_063382"
FT VARIANT 1096
FT /note="G -> A (in OI3; dbSNP:rs72659337)"
FT /evidence="ECO:0000269|PubMed:7749416"
FT /id="VAR_001901"
FT VARIANT 1101
FT /note="P -> L"
FT /id="VAR_001903"
FT VARIANT 1102
FT /note="G -> R (in OI4; dbSNP:rs67768540)"
FT /evidence="ECO:0000269|PubMed:2897363"
FT /id="VAR_001902"
FT VARIANT 1119
FT /note="A -> T (found in a patient with mild osteogenesis
FT imperfecta associated with increased bone mineral density;
FT results in defective type I procollagen processing;
FT incorporation of the immature procollagen into the matrix
FT leads to increased bone matrix mineralization and altered
FT collagen fibril structure)"
FT /evidence="ECO:0000269|PubMed:21344539"
FT /id="VAR_066386"
FT VARIANT 1148
FT /note="T -> P (in OI3; dbSNP:rs1800250)"
FT /evidence="ECO:0000269|PubMed:8723681"
FT /id="VAR_001904"
FT VARIANT 1189
FT /note="D -> E (in dbSNP:rs422361)"
FT /evidence="ECO:0000269|PubMed:2824475,
FT ECO:0000269|PubMed:6687691, ECO:0000269|PubMed:9443882"
FT /id="VAR_001905"
FT VARIANT 1195
FT /note="C -> Y (in OI1; dbSNP:rs72659342)"
FT /evidence="ECO:0000269|PubMed:16786509"
FT /id="VAR_063383"
FT VARIANT 1198
FT /note="S -> P (in dbSNP:rs384487)"
FT /evidence="ECO:0000269|PubMed:2824475,
FT ECO:0000269|PubMed:6687691, ECO:0000269|PubMed:9443882"
FT /id="VAR_001906"
FT VARIANT 1354
FT /note="Q -> H (in dbSNP:rs418570)"
FT /evidence="ECO:0000269|PubMed:2364107,
FT ECO:0000269|PubMed:2824475, ECO:0000269|PubMed:6092353,
FT ECO:0000269|PubMed:6309769, ECO:0000269|PubMed:6687691,
FT ECO:0000269|PubMed:9016532, ECO:0000269|PubMed:9443882"
FT /id="VAR_030122"
FT CONFLICT 55
FT /note="E -> G (in Ref. 6; CAA26320)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="V -> P (in Ref. 1; AAB59374)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="A -> T (in Ref. 1; AAB59374)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="P -> D (in Ref. 5; CAA68709)"
FT /evidence="ECO:0000305"
FT CONFLICT 828
FT /note="V -> A (in Ref. 19; CAA23761)"
FT /evidence="ECO:0000305"
FT CONFLICT 831
FT /note="T -> P (in Ref. 19; CAA23761)"
FT /evidence="ECO:0000305"
FT CONFLICT 837
FT /note="V -> P (in Ref. 19; CAA23761)"
FT /evidence="ECO:0000305"
FT CONFLICT 980
FT /note="E -> V (in Ref. 23; AAA51996)"
FT /evidence="ECO:0000305"
FT CONFLICT 1098
FT /note="P -> L (in Ref. 19; CAA23761)"
FT /evidence="ECO:0000305"
FT CONFLICT 1122..1125
FT /note="Missing (in Ref. 19; CAA23761)"
FT /evidence="ECO:0000305"
FT CONFLICT 1338
FT /note="R -> A (in Ref. 25; AAA51887)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1366 AA; 129314 MW; 1E68A5970FB4210A CRC64;
MLSFVDTRTL LLLAVTLCLA TCQSLQEETV RKGPAGDRGP RGERGPPGPP GRDGEDGPTG
PPGPPGPPGP PGLGGNFAAQ YDGKGVGLGP GPMGLMGPRG PPGAAGAPGP QGFQGPAGEP
GEPGQTGPAG ARGPAGPPGK AGEDGHPGKP GRPGERGVVG PQGARGFPGT PGLPGFKGIR
GHNGLDGLKG QPGAPGVKGE PGAPGENGTP GQTGARGLPG ERGRVGAPGP AGARGSDGSV
GPVGPAGPIG SAGPPGFPGA PGPKGEIGAV GNAGPAGPAG PRGEVGLPGL SGPVGPPGNP
GANGLTGAKG AAGLPGVAGA PGLPGPRGIP GPVGAAGATG ARGLVGEPGP AGSKGESGNK
GEPGSAGPQG PPGPSGEEGK RGPNGEAGSA GPPGPPGLRG SPGSRGLPGA DGRAGVMGPP
GSRGASGPAG VRGPNGDAGR PGEPGLMGPR GLPGSPGNIG PAGKEGPVGL PGIDGRPGPI
GPAGARGEPG NIGFPGPKGP TGDPGKNGDK GHAGLAGARG APGPDGNNGA QGPPGPQGVQ
GGKGEQGPPG PPGFQGLPGP SGPAGEVGKP GERGLHGEFG LPGPAGPRGE RGPPGESGAA
GPTGPIGSRG PSGPPGPDGN KGEPGVVGAV GTAGPSGPSG LPGERGAAGI PGGKGEKGEP
GLRGEIGNPG RDGARGAPGA VGAPGPAGAT GDRGEAGAAG PAGPAGPRGS PGERGEVGPA
GPNGFAGPAG AAGQPGAKGE RGAKGPKGEN GVVGPTGPVG AAGPAGPNGP PGPAGSRGDG
GPPGMTGFPG AAGRTGPPGP SGISGPPGPP GPAGKEGLRG PRGDQGPVGR TGEVGAVGPP
GFAGEKGPSG EAGTAGPPGT PGPQGLLGAP GILGLPGSRG ERGLPGVAGA VGEPGPLGIA
GPPGARGPPG AVGSPGVNGA PGEAGRDGNP GNDGPPGRDG QPGHKGERGY PGNIGPVGAA
GAPGPHGPVG PAGKHGNRGE TGPSGPVGPA GAVGPRGPSG PQGIRGDKGE PGEKGPRGLP
GLKGHNGLQG LPGIAGHHGD QGAPGSVGPA GPRGPAGPSG PAGKDGRTGH PGTVGPAGIR
GPQGHQGPAG PPGPPGPPGP PGVSGGGYDF GYDGDFYRAD QPRSAPSLRP KDYEVDATLK
SLNNQIETLL TPEGSRKNPA RTCRDLRLSH PEWSSGYYWI DPNQGCTMDA IKVYCDFSTG
ETCIRAQPEN IPAKNWYRSS KDKKHVWLGE TINAGSQFEY NVEGVTSKEM ATQLAFMRLL
ANYASQNITY HCKNSIAYMD EETGNLKKAV ILQGSNDVEL VAEGNSRFTY TVLVDGCSKK
TNEWGKTIIE YKTNKPSRLP FLDIAPLDIG GADQEFFVDI GPVCFK
