CHAD_HUMAN
ID CHAD_HUMAN Reviewed; 359 AA.
AC O15335; A8K812; Q6GTU0; Q96RJ5;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Chondroadherin;
DE AltName: Full=Cartilage leucine-rich protein;
DE Flags: Precursor;
GN Name=CHAD; Synonyms=SLRR4A;
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 [GENOMIC DNA].
RX PubMed=9344663; DOI=10.1006/geno.1997.4951;
RA Grover J., Chen X.-N., Korenberg J.R., Roughley P.J.;
RT "The structure and chromosome location of the human chondroadherin gene
RT (CHAD).";
RL Genomics 45:379-385(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11445564; DOI=10.1074/jbc.m101680200;
RA Maansson B., Wenglen C., Moergelin M., Saxne T., Heinegaard D.;
RT "Association of chondroadherin with collagen type II.";
RL J. Biol. Chem. 276:32883-32888(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Promotes attachment of chondrocytes, fibroblasts, and
CC osteoblasts. This binding is mediated (at least for chondrocytes and
CC fibroblasts) by the integrin alpha(2)beta(1). May play an important
CC role in the regulation of chondrocyte growth and proliferation (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Mostly monomeric (By similarity). Interacts with collagen type
CC II. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Present in chondrocytes at all ages.
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class IV subfamily. {ECO:0000305}.
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DR EMBL; U96769; AAC13410.1; -; Genomic_DNA.
DR EMBL; U96767; AAC13410.1; JOINED; Genomic_DNA.
DR EMBL; U96768; AAC13410.1; JOINED; Genomic_DNA.
DR EMBL; AF371328; AAK51556.1; -; mRNA.
DR EMBL; AK292177; BAF84866.1; -; mRNA.
DR EMBL; CH471109; EAW94613.1; -; Genomic_DNA.
DR EMBL; BC036360; AAH36360.1; -; mRNA.
DR EMBL; BC073974; AAH73974.1; -; mRNA.
DR CCDS; CCDS11568.1; -.
DR RefSeq; NP_001258.2; NM_001267.2.
DR PDB; 5LFN; X-ray; 2.10 A; A/B/C/D=23-359.
DR PDB; 5MX1; X-ray; 2.17 A; A/B=20-359.
DR PDBsum; 5LFN; -.
DR PDBsum; 5MX1; -.
DR AlphaFoldDB; O15335; -.
DR SMR; O15335; -.
DR BioGRID; 107526; 3.
DR CORUM; O15335; -.
DR IntAct; O15335; 2.
DR STRING; 9606.ENSP00000423812; -.
DR GlyGen; O15335; 1 site.
DR PhosphoSitePlus; O15335; -.
DR BioMuta; CHAD; -.
DR jPOST; O15335; -.
DR MassIVE; O15335; -.
DR PaxDb; O15335; -.
DR PeptideAtlas; O15335; -.
DR PRIDE; O15335; -.
DR ProteomicsDB; 48592; -.
DR Antibodypedia; 18082; 126 antibodies from 27 providers.
DR DNASU; 1101; -.
DR Ensembl; ENST00000258969.4; ENSP00000258969.4; ENSG00000136457.10.
DR Ensembl; ENST00000508540.6; ENSP00000423812.1; ENSG00000136457.10.
DR GeneID; 1101; -.
DR KEGG; hsa:1101; -.
DR MANE-Select; ENST00000508540.6; ENSP00000423812.1; NM_001267.3; NP_001258.2.
DR UCSC; uc010dbr.4; human.
DR CTD; 1101; -.
DR DisGeNET; 1101; -.
DR GeneCards; CHAD; -.
DR HGNC; HGNC:1909; CHAD.
DR HPA; ENSG00000136457; Tissue enhanced (liver, pancreas).
DR MIM; 602178; gene.
DR neXtProt; NX_O15335; -.
DR OpenTargets; ENSG00000136457; -.
DR PharmGKB; PA26445; -.
DR VEuPathDB; HostDB:ENSG00000136457; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000154464; -.
DR HOGENOM; CLU_000288_18_6_1; -.
DR InParanoid; O15335; -.
DR OMA; FRSCKSP; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; O15335; -.
DR TreeFam; TF332659; -.
DR PathwayCommons; O15335; -.
DR SignaLink; O15335; -.
DR BioGRID-ORCS; 1101; 15 hits in 1060 CRISPR screens.
DR GenomeRNAi; 1101; -.
DR Pharos; O15335; Tbio.
DR PRO; PR:O15335; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O15335; protein.
DR Bgee; ENSG00000136457; Expressed in tibia and 113 other tissues.
DR ExpressionAtlas; O15335; baseline and differential.
DR Genevisible; O15335; HS.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0060348; P:bone development; IEA:Ensembl.
DR GO; GO:1900155; P:negative regulation of bone trabecula formation; IEA:Ensembl.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF01462; LRRNT; 1.
DR SMART; SM00369; LRR_TYP; 9.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR PROSITE; PS51450; LRR; 10.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Leucine-rich repeat; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..359
FT /note="Chondroadherin"
FT /id="PRO_0000032773"
FT DOMAIN 23..52
FT /note="LRRNT"
FT REPEAT 76..97
FT /note="LRR 1"
FT REPEAT 100..121
FT /note="LRR 2"
FT REPEAT 124..145
FT /note="LRR 3"
FT REPEAT 148..169
FT /note="LRR 4"
FT REPEAT 172..193
FT /note="LRR 5"
FT REPEAT 196..217
FT /note="LRR 6"
FT REPEAT 220..241
FT /note="LRR 7"
FT REPEAT 245..266
FT /note="LRR 8"
FT REPEAT 269..290
FT /note="LRR 9"
FT DOMAIN 300..348
FT /note="LRRCT"
FT CARBOHYD 144
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT DISULFID 23..38
FT /evidence="ECO:0000250"
FT DISULFID 304..346
FT /evidence="ECO:0000250"
FT DISULFID 306..326
FT /evidence="ECO:0000250"
FT VARIANT 312
FT /note="R -> Q (in dbSNP:rs35218093)"
FT /id="VAR_052019"
FT VARIANT 350
FT /note="T -> I (in dbSNP:rs2231510)"
FT /id="VAR_030631"
FT CONFLICT 114
FT /note="L -> V (in Ref. 1; AAC13410)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="A -> P (in Ref. 1; AAC13410)"
FT /evidence="ECO:0000305"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:5LFN"
FT TURN 31..34
FT /evidence="ECO:0007829|PDB:5LFN"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:5LFN"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:5LFN"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:5LFN"
FT TURN 68..73
FT /evidence="ECO:0007829|PDB:5LFN"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:5LFN"
FT TURN 92..97
FT /evidence="ECO:0007829|PDB:5LFN"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:5LFN"
FT TURN 116..121
FT /evidence="ECO:0007829|PDB:5LFN"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:5LFN"
FT TURN 140..145
FT /evidence="ECO:0007829|PDB:5LFN"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:5LFN"
FT TURN 164..169
FT /evidence="ECO:0007829|PDB:5LFN"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:5LFN"
FT TURN 188..191
FT /evidence="ECO:0007829|PDB:5LFN"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:5LFN"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:5LFN"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:5LFN"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:5LFN"
FT TURN 236..239
FT /evidence="ECO:0007829|PDB:5LFN"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:5LFN"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:5LFN"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:5LFN"
FT TURN 261..266
FT /evidence="ECO:0007829|PDB:5LFN"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:5LFN"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:5LFN"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:5LFN"
FT HELIX 309..317
FT /evidence="ECO:0007829|PDB:5LFN"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:5MX1"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:5LFN"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:5LFN"
FT TURN 342..345
FT /evidence="ECO:0007829|PDB:5MX1"
SQ SEQUENCE 359 AA; 40476 MW; CF24D2B5A5DFCF0C CRC64;
MVRPMLLLSL GLLAGLLPAL AACPQNCHCH SDLQHVICDK VGLQKIPKVS EKTKLLNLQR
NNFPVLAANS FRAMPNLVSL HLQHCQIREV AAGAFRGLKQ LIYLYLSHND IRVLRAGAFD
DLTELTYLYL DHNKVTELPR GLLSPLVNLF ILQLNNNKIR ELRAGAFQGA KDLRWLYLSE
NALSSLQPGA LDDVENLAKF HVDRNQLSSY PSAALSKLRV VEELKLSHNP LKSIPDNAFQ
SFGRYLETLW LDNTNLEKFS DGAFLGVTTL KHVHLENNRL NQLPSNFPFD SLETLALTNN
PWKCTCQLRG LRRWLEAKAS RPDATCASPA KFKGQHIRDT DAFRSCKFPT KRSKKAGRH
