CO1A2_RAT
ID CO1A2_RAT Reviewed; 1372 AA.
AC P02466; Q9R1E8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Collagen alpha-2(I) chain;
DE AltName: Full=Alpha-2 type I collagen;
DE Flags: Precursor;
GN Name=Col1a2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Guenther D., Seibold S., Marx M.;
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 86-98, ALLYSINE AT LYS-90, AND PYROGLUTAMATE FORMATION
RP AT GLN-86.
RC TISSUE=Skin;
RX PubMed=5337886; DOI=10.1021/bi00855a019;
RA Kang A.H., Bornstein P., Piez K.A.;
RT "The amino acid sequence of peptides from the cross-linking region of rat
RT skin collagen.";
RL Biochemistry 6:788-795(1967).
RN [3]
RP PROTEIN SEQUENCE OF 99-102.
RC TISSUE=Skin;
RX PubMed=5785232; DOI=10.1021/bi00833a052;
RA Fietzek P.P., Piez K.A.;
RT "Isolation and characterization of the cyanogen bromide peptides from the
RT alpha 2 chain of rat skin collagen.";
RL Biochemistry 8:2129-2133(1969).
RN [4]
RP PROTEIN SEQUENCE OF 103-143.
RC TISSUE=Skin;
RX PubMed=4636752; DOI=10.1016/0014-5793(72)80543-x;
RA Fietzek P.P., Kell I., Kuehn K.;
RT "The covalent structure of collagen. Amino acid sequence of the N-terminal
RT region of alpha 2-CB4 from calf and rat skin collagen.";
RL FEBS Lett. 26:66-68(1972).
RN [5]
RP PROTEIN SEQUENCE OF 424-452.
RC TISSUE=Skin;
RX PubMed=5544653; DOI=10.1021/bi00780a010;
RA Highberger J.H., Kang A.H., Gross J.;
RT "Comparative studies on the amino acid sequence of the alpha 2-CB2 peptides
RT from chick and rat skin collagens.";
RL Biochemistry 10:610-616(1971).
RN [6]
RP PROTEIN SEQUENCE OF 453-501.
RC TISSUE=Skin;
RX PubMed=4435743; DOI=10.1515/bchm2.1974.355.1.647;
RA Fietzek P.P., Kuehn K.;
RT "The covalent structure of collagen: amino acid sequence of the N-terminal
RT region of alpha2-CB3 from rat skin collagen and alpha2-CB3.5 from calf skin
RT collagen.";
RL Hoppe-Seyler's Z. Physiol. Chem. 355:647-650(1974).
RN [7]
RP PROTEIN SEQUENCE OF 791-836.
RC TISSUE=Skin;
RX PubMed=4763308; DOI=10.1016/0014-5793(73)80393-x;
RA Fietzek P.P., Kuehn K.;
RT "The covalent structure of collagen: amino acid sequence of the N-terminal
RT region of alpha 2-CB5 from rat skin collagen.";
RL FEBS Lett. 36:289-291(1973).
RN [8]
RP ORDER OF CNBR PEPTIDES.
RX PubMed=5443712; DOI=10.1016/0006-291x(70)90638-8;
RA Vuust J., Lane J.M., Fietzek P.P., Miller E.J., Piez K.A.;
RT "The order of the CNBr peptides from the alpha 2 chain of collagen.";
RL Biochem. Biophys. Res. Commun. 38:703-708(1970).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION.
RA Xiong X., Ghosh R., Hiller E., Drepper F., Knapp B., Brunner H., Rupp S.;
RT "A new procedure for rapid, high yield purification of Type I collagen for
RT tissue engineering.";
RL Process Biochem. 44:1200-1212(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=19423663; DOI=10.1530/rep-09-0052;
RA Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.;
RT "Identification of novel immunodominant epididymal sperm proteins using
RT combinatorial approach.";
RL Reproduction 138:81-93(2009).
RN [11]
RP CLEAVAGE OF SIGNAL PEPTIDE AFTER CYS-22, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=26479776; DOI=10.1021/acs.jproteome.5b00820;
RA Tsuchiya T., Osaki T., Minamino N., Sasaki K.;
RT "Peptidomics for studying limited proteolysis.";
RL J. Proteome Res. 14:4921-4931(2015).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (5.16 ANGSTROMS) OF 86-1113.
RX PubMed=16751282; DOI=10.1073/pnas.0502718103;
RA Orgel J.P.R.O., Irving T.C., Miller A., Wess T.J.;
RT "Microfibrillar structure of type I collagen in situ.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9001-9005(2006).
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 -!- 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 Expressed in flagella of epididymal sperm.
CC {ECO:0000269|PubMed:19423663}.
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: Proline residues at the third position of the tripeptide repeating
CC unit (G-X-P) are hydroxylated in some or all of the chains. Proline
CC residues at the second position of the tripeptide repeating unit (G-P-
CC X) are hydroxylated in some of the chains.
CC -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF121217; AAD41775.1; -; mRNA.
DR RefSeq; NP_445808.1; NM_053356.1.
DR PDB; 3HQV; Fiber; 5.16 A; B=86-1113.
DR PDB; 3HR2; Fiber; 5.16 A; B=86-1113.
DR PDBsum; 3HQV; -.
DR PDBsum; 3HR2; -.
DR AlphaFoldDB; P02466; -.
DR SMR; P02466; -.
DR BioGRID; 249912; 2.
DR ComplexPortal; CPX-3104; Collagen type I trimer.
DR DIP; DIP-37338N; -.
DR IntAct; P02466; 2.
DR STRING; 10116.ENSRNOP00000016423; -.
DR GlyGen; P02466; 2 sites.
DR iPTMnet; P02466; -.
DR PhosphoSitePlus; P02466; -.
DR PaxDb; P02466; -.
DR PRIDE; P02466; -.
DR GeneID; 84352; -.
DR KEGG; rno:84352; -.
DR UCSC; RGD:621351; rat.
DR CTD; 1278; -.
DR RGD; 621351; Col1a2.
DR eggNOG; KOG3544; Eukaryota.
DR InParanoid; P02466; -.
DR OrthoDB; 1406711at2759; -.
DR PhylomeDB; P02466; -.
DR Reactome; R-RNO-114604; GPVI-mediated activation cascade.
DR Reactome; R-RNO-1442490; Collagen degradation.
DR Reactome; R-RNO-1474244; Extracellular matrix organization.
DR Reactome; R-RNO-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-RNO-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-RNO-216083; Integrin cell surface interactions.
DR Reactome; R-RNO-2243919; Crosslinking of collagen fibrils.
DR Reactome; R-RNO-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-RNO-3000178; ECM proteoglycans.
DR Reactome; R-RNO-430116; GP1b-IX-V activation signalling.
DR Reactome; R-RNO-75892; Platelet Adhesion to exposed collagen.
DR Reactome; R-RNO-76009; Platelet Aggregation (Plug Formation).
DR Reactome; R-RNO-8874081; MET activates PTK2 signaling.
DR Reactome; R-RNO-8948216; Collagen chain trimerization.
DR EvolutionaryTrace; P02466; -.
DR PRO; PR:P02466; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005581; C:collagen trimer; ISO:RGD.
DR GO; GO:0005584; C:collagen type I trimer; ISO:RGD.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048407; F:platelet-derived growth factor binding; ISO:RGD.
DR GO; GO:0002020; F:protease binding; ISO:RGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:RGD.
DR GO; GO:0046332; F:SMAD binding; ISO:RGD.
DR GO; GO:0001568; P:blood vessel development; ISO:RGD.
DR GO; GO:0030282; P:bone mineralization; ISO:RGD.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISO:RGD.
DR GO; GO:0071310; P:cellular response to organic substance; IEP:RGD.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEP:RGD.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; IEP:RGD.
DR GO; GO:0030199; P:collagen fibril organization; ISO:RGD.
DR GO; GO:0032963; P:collagen metabolic process; ISO:RGD.
DR GO; GO:0085029; P:extracellular matrix assembly; ISO:RGD.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0070208; P:protein heterotrimerization; ISO:RGD.
DR GO; GO:0008217; P:regulation of blood pressure; ISO:RGD.
DR GO; GO:0071873; P:response to norepinephrine; IEP:RGD.
DR GO; GO:0007266; P:Rho protein signal transduction; ISO:RGD.
DR GO; GO:0001501; P:skeletal system development; ISO:RGD.
DR GO; GO:0043589; P:skin morphogenesis; ISO:RGD.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR000885; Fib_collagen_C.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 7.
DR SMART; SM00038; COLFI; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Collagen; Direct protein sequencing; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydroxylation; Metal-binding;
KW Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:26479776"
FT PROPEP 23..85
FT /note="N-terminal propeptide"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT /id="PRO_0000005812"
FT CHAIN 86..1125
FT /note="Collagen alpha-2(I) chain"
FT /id="PRO_0000005813"
FT PROPEP 1126..1372
FT /note="C-terminal propeptide"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT /id="PRO_0000005814"
FT DOMAIN 1139..1372
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT REGION 28..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 783..785
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 828..830
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 1011..1013
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 58..78
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..268
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1108
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1187
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 BINDING 1190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 1192
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q03692"
FT BINDING 1195
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:0000250|UniProtKB:P08123"
FT MOD_RES 86
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:5337886"
FT MOD_RES 90
FT /note="Allysine"
FT /evidence="ECO:0000269|PubMed:5337886"
FT MOD_RES 183
FT /note="5-hydroxylysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT CARBOHYD 183
FT /note="O-linked (Gal...) hydroxylysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08123"
FT CARBOHYD 1273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1169..1201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1209..1370
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1278..1323
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT CONFLICT 132
FT /note="T -> P (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="S -> P (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 431..432
FT /note="ST -> TS (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="E -> Z (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="N -> A (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 825
FT /note="R -> K (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1372 AA; 129564 MW; B069371A8DB20A72 CRC64;
MLSFVDTRTL LLLAVTSCLA TCQSLQMGSV RKGPTGDRGP RGQRGPAGPR GRDGVDGPVG
PPGPPGAPGP PGPPGPPGLT GNFAAQYSDK GVSAGPGPMG LMGPRGPPGA VGAPGPQGFQ
GPAGEPGEPG QTGPAGSRGP AGPPGKAGED GHPGKPGRPG ERGVVGPQGA RGFPGTPGLP
GFKGIRGHNG LDGLKGQPGA QGVKGEPGAP GENGTPGQAG ARGLPGERGR VGAPGPAGAR
GSDGSVGPVG PAGPIGSAGP PGFPGAPGPK GELGPVGNPG PAGPAGPRGE AGLPGLSGPV
GPPGNPGANG LTGAKGATGL PGVAGAPGLP GPRGIPGPVG AAGATGPRGL VGEPGPAGSK
GETGNKGEPG SAGAQGPPGP SGEEGKRGSP GEPGSAGPAG PPGLRGSPGS RGLPGADGRA
GVMGPPGNRG STGPAGVRGP NGDAGRPGEP GLMGPRGLPG SPGNVGPAGK EGPVGLPGID
GRPGPIGPAG PRGEAGNIGF PGPKGPSGDP GKPGEKGHPG LAGARGAPGP DGNNGAQGPP
GPQGVQGGKG EQGPAGPPGF QGLPGPSGTA GEVGKPGERG LPGEFGLPGP AGPRGERGPP
GESGAAGPSG PIGIRGPSGA PGPDGNKGEA GAVGAPGSAG ASGPGGLPGE RGAAGIPGGK
GEKGETGLRG EIGNPGRDGA RGAPGAIGAP GPAGASGDRG EAGAAGPSGP AGPRGSPGER
GEVGPAGPNG FAGPAGSAGQ PGAKGEKGTK GPKGENGIVG PTGPVGAAGP SGPNGPPGPA
GSRGDGGPPG MTGFPGAAGR TGPPGPSGIT GPPGPPGAAG KEGIRGPRGD QGPVGRTGEI
GASGPPGFAG EKGPSGEPGT TGPPGTAGPQ GLLGAPGILG LPGSRGERGQ PGIAGALGEP
GPLGIAGPPG ARGPPGAVGS PGVNGAPGEA GRDGNPGSDG PPGRDGQPGH KGERGYPGNI
GPTGAAGAPG PHGSVGPAGK HGNRGEPGPA GSVGPVGAVG PRGPSGPQGI RGDKGEPGDK
GARGLPGLKG HNGLQGLPGL AGLHGDQGAP GPVGPAGPRG PAGPSGPIGK DGRSGHPGPV
GPAGVRGSQG SQGPAGPPGP PGPPGPPGVS GGGYDFGFEG GFYRADQPRS QPSLRPKDYE
VDATLKSLNN QIETLLTPEG SRKNPARTCR DLRLSHPEWK SDYYWIDPNQ GCTMDAIKVY
CDFSTGETCI QAQPVNTPAK NAYSRAQANK HVWLGETING GSQFEYNAEG VSSKEMATQL
AFMRLLANRA SQNITYHCKN SIAYLDEETG RLNKAVILQG SNDVELVAEG NSRFTYTVLV
DGCSKKTNEW DKTVIEYKTN KPSRLPFLDI APLDIGGTNQ EFRVEVGPVC FK
