CO9A1_HUMAN
ID CO9A1_HUMAN Reviewed; 921 AA.
AC P20849; Q13699; Q13700; Q5TF52; Q6P467; Q96BM8; Q99225; Q9H151; Q9H152;
AC Q9Y6P2; Q9Y6P3;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=Collagen alpha-1(IX) chain;
DE Flags: Precursor;
GN Name=COL9A1;
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], ALTERNATIVE SPLICING, AND VARIANTS
RP LYS-870 AND LEU-882.
RX PubMed=2209617; DOI=10.1111/j.1432-1033.1990.tb19279.x;
RA Muragaki Y., Kimura T., Ninomiya Y., Olsen B.R.;
RT "The complete primary structure of two distinct forms of human alpha 1 (IX)
RT collagen chains.";
RL Eur. J. Biochem. 192:703-708(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, AND
RP VARIANTS ARG-621; LYS-870 AND LEU-882.
RX PubMed=9707347; DOI=10.1016/s0945-053x(98)90063-4;
RA Pihlajamaa T., Vuoristo M.M., Annunen S., Peraelae M., Prockop D.J.,
RA Ala-Kokko L.;
RT "Human COL9A1 and COL9A2 genes. Two genes of 90 and 15 kb code for similar
RT polypeptides of the same collagen molecule.";
RL Matrix Biol. 17:237-241(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain, and Mammary gland;
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 PROTEIN SEQUENCE OF 405-417 (ISOFORMS 1/2).
RX PubMed=8660302; DOI=10.1042/bj3140327;
RA Diab M., Wu J.J., Eyre D.R.;
RT "Collagen type IX from human cartilage: a structural profile of
RT intermolecular cross-linking sites.";
RL Biochem. J. 314:327-332(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 580-820 AND 835-884, AND VARIANTS
RP LYS-870 AND LEU-882.
RX PubMed=2465149; DOI=10.1111/j.1432-1033.1989.tb14522.x;
RA Kimura T., Mattei M.-G., Stevens J.W., Goldring M.B., Ninomiya Y.,
RA Olsen B.R.;
RT "Molecular cloning of rat and human type IX collagen cDNA and localization
RT of the alpha 1(IX) gene on the human chromosome 6.";
RL Eur. J. Biochem. 179:71-78(1989).
RN [7]
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=1690886; DOI=10.1073/pnas.87.7.2400;
RA Muragaki Y., Nishimura I., Henney A., Ninomiya Y., Olsen B.R.;
RT "The alpha 1 (IX) collagen gene gives rise to two different transcripts in
RT both mouse embryonic and human fetal RNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:2400-2404(1990).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 24-268, DISULFIDE BONDS, AND
RP ZINC-BINDING SITES.
RX PubMed=17553797; DOI=10.1074/jbc.m702514200;
RA Leppanen V.M., Tossavainen H., Permi P., Lehtio L., Ronnholm G.,
RA Goldman A., Kilpelainen I., Pihlajamaa T.;
RT "Crystal structure of the N-terminal NC4 domain of collagen IX, a zinc
RT binding member of the laminin-neurexin-sex hormone binding globulin (LNS)
RT domain family.";
RL J. Biol. Chem. 282:23219-23230(2007).
RN [9]
RP VARIANTS PRO-339 AND ARG-621, AND INVOLVEMENT IN EDM6.
RX PubMed=11565064; DOI=10.1086/324023;
RA Czarny-Ratajczak M., Lohiniva J., Rogala P., Kozlowski K., Peraelae M.,
RA Carter L., Spector T.D., Kolodziej L., Seppaenen U., Glazar R.,
RA Krolewski J., Latos-Bielenska A., Ala-Kokko L.;
RT "A mutation in COL9A1 causes multiple epiphyseal dysplasia: further
RT evidence for locus heterogeneity.";
RL Am. J. Hum. Genet. 69:969-980(2001).
RN [10]
RP INVOLVEMENT IN STL4.
RX PubMed=16909383; DOI=10.1086/506478;
RA Van Camp G., Snoeckx R.L., Hilgert N., van den Ende J., Fukuoka H.,
RA Wagatsuma M., Suzuki H., Smets R.M., Vanhoenacker F., Declau F.,
RA Van de Heyning P., Usami S.;
RT "A new autosomal recessive form of Stickler syndrome is caused by a
RT mutation in the COL9A1 gene.";
RL Am. J. Hum. Genet. 79:449-457(2006).
CC -!- FUNCTION: Structural component of hyaline cartilage and vitreous of the
CC eye.
CC -!- SUBUNIT: Heterotrimer of an alpha 1(IX), an alpha 2(IX) and an alpha
CC 3(IX) chain.
CC -!- INTERACTION:
CC P20849; P02489: CRYAA; NbExp=3; IntAct=EBI-2528238, EBI-6875961;
CC P20849; O14908-2: GIPC1; NbExp=3; IntAct=EBI-2528238, EBI-25913156;
CC P20849; Q92876: KLK6; NbExp=3; IntAct=EBI-2528238, EBI-2432309;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=Long;
CC IsoId=P20849-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=P20849-2; Sequence=VSP_001141, VSP_001142;
CC Name=3;
CC IsoId=P20849-3; Sequence=VSP_015250, VSP_015251;
CC -!- DOMAIN: Each subunit is composed of three triple-helical domains
CC interspersed with non-collagenous domains. The globular domain at the
CC N-terminus of type IX collagen molecules represents the NC4 domain
CC which may participate in electrostatic interactions with polyanionic
CC glycosaminoglycans in cartilage.
CC -!- PTM: Covalently linked to the telopeptides of type II collagen by
CC lysine-derived cross-links.
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 -!- DISEASE: Multiple epiphyseal dysplasia 6 (EDM6) [MIM:614135]: A
CC generalized skeletal dysplasia associated with significant morbidity.
CC Joint pain, joint deformity, waddling gait, and short stature are the
CC main clinical signs and symptoms. Radiological examination of the
CC skeleton shows delayed, irregular mineralization of the epiphyseal
CC ossification centers and of the centers of the carpal and tarsal bones.
CC Multiple epiphyseal dysplasia is broadly categorized into the more
CC severe Fairbank and the milder Ribbing types. The Fairbank type is
CC characterized by shortness of stature, short and stubby fingers, small
CC epiphyses in several joints, including the knee, ankle, hand, and hip.
CC The Ribbing type is confined predominantly to the hip joints and is
CC characterized by hands that are normal and stature that is normal or
CC near-normal. {ECO:0000269|PubMed:11565064}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- DISEASE: Stickler syndrome 4 (STL4) [MIM:614134]: An autosomal
CC recessive form of Stickler syndrome, an inherited disorder that
CC associates ocular signs with more or less complete forms of Pierre
CC Robin sequence, bone disorders and sensorineural deafness. Ocular
CC disorders may include juvenile cataract, myopia, strabismus,
CC vitreoretinal or chorioretinal degeneration, retinal detachment, and
CC chronic uveitis. Pierre Robin sequence includes an opening in the roof
CC of the mouth (a cleft palate), a large tongue (macroglossia), and a
CC small lower jaw (micrognathia). Bones are affected by slight
CC platyspondylisis and large, often defective epiphyses. Juvenile joint
CC laxity is followed by early signs of arthrosis. The degree of hearing
CC loss varies among affected individuals and may become more severe over
CC time. Syndrome expressivity is variable. {ECO:0000269|PubMed:16909383}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the fibril-associated collagens with interrupted
CC helices (FACIT) family. {ECO:0000305}.
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DR EMBL; X54412; CAA38276.1; -; mRNA.
DR EMBL; X54413; CAA38277.1; -; mRNA.
DR EMBL; AF036130; AAC33527.1; -; Genomic_DNA.
DR EMBL; AF036110; AAC33527.1; JOINED; Genomic_DNA.
DR EMBL; AF036111; AAC33527.1; JOINED; Genomic_DNA.
DR EMBL; AF036112; AAC33527.1; JOINED; Genomic_DNA.
DR EMBL; AF036113; AAC33527.1; JOINED; Genomic_DNA.
DR EMBL; AF036114; AAC33527.1; JOINED; Genomic_DNA.
DR EMBL; AF036115; AAC33527.1; JOINED; Genomic_DNA.
DR EMBL; AF036116; AAC33527.1; JOINED; Genomic_DNA.
DR EMBL; AF036117; AAC33527.1; JOINED; Genomic_DNA.
DR EMBL; AF036118; AAC33527.1; JOINED; Genomic_DNA.
DR EMBL; AF036119; AAC33527.1; JOINED; Genomic_DNA.
DR EMBL; AF036120; AAC33527.1; JOINED; Genomic_DNA.
DR EMBL; AF036121; AAC33527.1; JOINED; Genomic_DNA.
DR EMBL; AF036122; AAC33527.1; JOINED; Genomic_DNA.
DR EMBL; AF036123; AAC33527.1; JOINED; Genomic_DNA.
DR EMBL; AF036124; AAC33527.1; JOINED; Genomic_DNA.
DR EMBL; AF036125; AAC33527.1; JOINED; Genomic_DNA.
DR EMBL; AF036126; AAC33527.1; JOINED; Genomic_DNA.
DR EMBL; AF036127; AAC33527.1; JOINED; Genomic_DNA.
DR EMBL; AF036128; AAC33527.1; JOINED; Genomic_DNA.
DR EMBL; AF036129; AAC33527.1; JOINED; Genomic_DNA.
DR EMBL; AF036130; AAC33528.1; -; Genomic_DNA.
DR EMBL; AF036112; AAC33528.1; JOINED; Genomic_DNA.
DR EMBL; AF036113; AAC33528.1; JOINED; Genomic_DNA.
DR EMBL; AF036114; AAC33528.1; JOINED; Genomic_DNA.
DR EMBL; AF036115; AAC33528.1; JOINED; Genomic_DNA.
DR EMBL; AF036116; AAC33528.1; JOINED; Genomic_DNA.
DR EMBL; AF036117; AAC33528.1; JOINED; Genomic_DNA.
DR EMBL; AF036118; AAC33528.1; JOINED; Genomic_DNA.
DR EMBL; AF036119; AAC33528.1; JOINED; Genomic_DNA.
DR EMBL; AF036120; AAC33528.1; JOINED; Genomic_DNA.
DR EMBL; AF036121; AAC33528.1; JOINED; Genomic_DNA.
DR EMBL; AF036122; AAC33528.1; JOINED; Genomic_DNA.
DR EMBL; AF036123; AAC33528.1; JOINED; Genomic_DNA.
DR EMBL; AF036124; AAC33528.1; JOINED; Genomic_DNA.
DR EMBL; AF036125; AAC33528.1; JOINED; Genomic_DNA.
DR EMBL; AF036126; AAC33528.1; JOINED; Genomic_DNA.
DR EMBL; AF036127; AAC33528.1; JOINED; Genomic_DNA.
DR EMBL; AF036128; AAC33528.1; JOINED; Genomic_DNA.
DR EMBL; AF036129; AAC33528.1; JOINED; Genomic_DNA.
DR EMBL; AL080275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL160262; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015409; AAH15409.1; -; mRNA.
DR EMBL; BC063646; AAH63646.1; -; mRNA.
DR EMBL; M32137; AAA53474.1; -; Genomic_DNA.
DR EMBL; M32133; AAA53474.1; JOINED; Genomic_DNA.
DR EMBL; M32137; AAA53475.1; -; Genomic_DNA.
DR EMBL; M32135; AAA53475.1; JOINED; Genomic_DNA.
DR CCDS; CCDS47447.1; -. [P20849-2]
DR CCDS; CCDS4971.1; -. [P20849-1]
DR PIR; S13580; S13580.
DR PIR; S13581; S13581.
DR RefSeq; NP_001842.3; NM_001851.4. [P20849-1]
DR RefSeq; NP_511040.2; NM_078485.3. [P20849-2]
DR PDB; 2UUR; X-ray; 1.80 A; A=24-268.
DR PDB; 5CTD; X-ray; 1.60 A; A=754-789.
DR PDB; 5CTI; X-ray; 1.90 A; A=754-789.
DR PDB; 5CVA; X-ray; 2.10 A; A/D=754-789.
DR PDB; 5CVB; X-ray; 2.25 A; A/D=754-789.
DR PDBsum; 2UUR; -.
DR PDBsum; 5CTD; -.
DR PDBsum; 5CTI; -.
DR PDBsum; 5CVA; -.
DR PDBsum; 5CVB; -.
DR AlphaFoldDB; P20849; -.
DR SMR; P20849; -.
DR BioGRID; 107694; 9.
DR ComplexPortal; CPX-1748; Collagen type IX trimer.
DR IntAct; P20849; 9.
DR STRING; 9606.ENSP00000349790; -.
DR GlyGen; P20849; 1 site.
DR iPTMnet; P20849; -.
DR PhosphoSitePlus; P20849; -.
DR BioMuta; COL9A1; -.
DR DMDM; 296439373; -.
DR MassIVE; P20849; -.
DR PaxDb; P20849; -.
DR PeptideAtlas; P20849; -.
DR PRIDE; P20849; -.
DR ProteomicsDB; 53816; -. [P20849-1]
DR ProteomicsDB; 53817; -. [P20849-2]
DR ProteomicsDB; 53818; -. [P20849-3]
DR Antibodypedia; 17698; 195 antibodies from 32 providers.
DR DNASU; 1297; -.
DR Ensembl; ENST00000320755.12; ENSP00000315252.7; ENSG00000112280.18. [P20849-2]
DR Ensembl; ENST00000357250.11; ENSP00000349790.6; ENSG00000112280.18. [P20849-1]
DR Ensembl; ENST00000370496.3; ENSP00000359527.3; ENSG00000112280.18. [P20849-3]
DR GeneID; 1297; -.
DR KEGG; hsa:1297; -.
DR MANE-Select; ENST00000357250.11; ENSP00000349790.6; NM_001851.6; NP_001842.3.
DR UCSC; uc003pff.5; human. [P20849-1]
DR CTD; 1297; -.
DR DisGeNET; 1297; -.
DR GeneCards; COL9A1; -.
DR GeneReviews; COL9A1; -.
DR HGNC; HGNC:2217; COL9A1.
DR HPA; ENSG00000112280; Tissue enhanced (choroid plexus, prostate).
DR MalaCards; COL9A1; -.
DR MIM; 120210; gene.
DR MIM; 614134; phenotype.
DR MIM; 614135; phenotype.
DR neXtProt; NX_P20849; -.
DR OpenTargets; ENSG00000112280; -.
DR Orphanet; 250984; Autosomal recessive Stickler syndrome.
DR Orphanet; 166002; Multiple epiphyseal dysplasia due to collagen 9 anomaly.
DR PharmGKB; PA26733; -.
DR VEuPathDB; HostDB:ENSG00000112280; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000157935; -.
DR HOGENOM; CLU_001074_18_1_1; -.
DR InParanoid; P20849; -.
DR OMA; CPTIRIG; -.
DR OrthoDB; 1295141at2759; -.
DR PhylomeDB; P20849; -.
DR TreeFam; TF332900; -.
DR PathwayCommons; P20849; -.
DR Reactome; R-HSA-1442490; Collagen degradation.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-HSA-186797; Signaling by PDGF.
DR Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR Reactome; R-HSA-419037; NCAM1 interactions.
DR Reactome; R-HSA-8948216; Collagen chain trimerization.
DR SignaLink; P20849; -.
DR BioGRID-ORCS; 1297; 7 hits in 1061 CRISPR screens.
DR ChiTaRS; COL9A1; human.
DR EvolutionaryTrace; P20849; -.
DR GeneWiki; Collagen,_type_IX,_alpha_1; -.
DR GenomeRNAi; 1297; -.
DR Pharos; P20849; Tbio.
DR PRO; PR:P20849; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P20849; protein.
DR Bgee; ENSG00000112280; Expressed in tibia and 112 other tissues.
DR ExpressionAtlas; P20849; baseline and differential.
DR Genevisible; P20849; HS.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0005594; C:collagen type IX trimer; IDA:BHF-UCL.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
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; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IC:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF01391; Collagen; 8.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Collagen; Deafness;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Hydroxylation; Metal-binding; Reference proteome; Repeat;
KW Secreted; Signal; Stickler syndrome; Zinc.
FT SIGNAL 1..23
FT CHAIN 24..921
FT /note="Collagen alpha-1(IX) chain"
FT /id="PRO_0000005765"
FT DOMAIN 50..244
FT /note="Laminin G-like"
FT DOMAIN 269..324
FT /note="Collagen-like 1"
FT DOMAIN 325..356
FT /note="Collagen-like 2"
FT DOMAIN 358..403
FT /note="Collagen-like 3"
FT DOMAIN 416..472
FT /note="Collagen-like 4"
FT DOMAIN 473..516
FT /note="Collagen-like 5"
FT DOMAIN 587..643
FT /note="Collagen-like 6"
FT DOMAIN 655..712
FT /note="Collagen-like 7"
FT DOMAIN 713..755
FT /note="Collagen-like 8"
FT DOMAIN 790..847
FT /note="Collagen-like 9"
FT DOMAIN 848..899
FT /note="Collagen-like 10"
FT REGION 24..268
FT /note="Nonhelical region (NC4)"
FT REGION 254..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..405
FT /note="Triple-helical region (COL3)"
FT REGION 406..417
FT /note="Nonhelical region (NC3)"
FT REGION 418..756
FT /note="Triple-helical region (COL2)"
FT REGION 757..786
FT /note="Nonhelical region (NC2)"
FT REGION 783..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..901
FT /note="Triple-helical region (COL1)"
FT REGION 902..921
FT /note="Nonhelical region (NC1)"
FT COMPBIAS 272..286
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..317
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..399
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..807
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..899
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..242
FT /evidence="ECO:0000269|PubMed:17553797"
FT DISULFID 198..252
FT /evidence="ECO:0000269|PubMed:17553797"
FT DISULFID 411
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:17553797"
FT DISULFID 415
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:17553797"
FT VAR_SEQ 1..243
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9707347"
FT /id="VSP_001141"
FT VAR_SEQ 244..267
FT /note="PLRPRRETCHELPARITPSQTTDE -> MAWTARDRGALGLLLLGLCLCAAQ
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9707347"
FT /id="VSP_001142"
FT VAR_SEQ 326..328
FT /note="GLT -> TSP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015250"
FT VAR_SEQ 329..921
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015251"
FT VARIANT 339
FT /note="S -> P (in dbSNP:rs592121)"
FT /evidence="ECO:0000269|PubMed:11565064"
FT /id="VAR_026463"
FT VARIANT 621
FT /note="Q -> R (in dbSNP:rs1135056)"
FT /evidence="ECO:0000269|PubMed:11565064,
FT ECO:0000269|PubMed:9707347"
FT /id="VAR_026464"
FT VARIANT 684
FT /note="E -> K (in dbSNP:rs35470562)"
FT /id="VAR_055668"
FT VARIANT 767
FT /note="M -> V (in dbSNP:rs6910140)"
FT /id="VAR_055669"
FT VARIANT 870
FT /note="R -> K (in dbSNP:rs1056921)"
FT /evidence="ECO:0000269|PubMed:2209617,
FT ECO:0000269|PubMed:2465149, ECO:0000269|PubMed:9707347"
FT /id="VAR_023326"
FT VARIANT 882
FT /note="V -> L (in dbSNP:rs1056923)"
FT /evidence="ECO:0000269|PubMed:2209617,
FT ECO:0000269|PubMed:2465149, ECO:0000269|PubMed:9707347"
FT /id="VAR_023327"
FT CONFLICT 279..280
FT /note="PP -> AS (in Ref. 1; CAA38276/CAA38277)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="I -> L (in Ref. 1; CAA38276)"
FT /evidence="ECO:0000305"
FT CONFLICT 570
FT /note="Q -> H (in Ref. 2; AAC33527/AAC33528)"
FT /evidence="ECO:0000305"
FT CONFLICT 910..921
FT /note="AGQRAFNKGPDP -> LVSEHLTKGLTLERLTAAWLSA (in Ref. 1;
FT AAA53475)"
FT /evidence="ECO:0000305"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:2UUR"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:2UUR"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:2UUR"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:2UUR"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:2UUR"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:2UUR"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:2UUR"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:2UUR"
FT STRAND 109..118
FT /evidence="ECO:0007829|PDB:2UUR"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:2UUR"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:2UUR"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:2UUR"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:2UUR"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:2UUR"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:2UUR"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:2UUR"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:2UUR"
FT STRAND 181..188
FT /evidence="ECO:0007829|PDB:2UUR"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:2UUR"
FT STRAND 199..205
FT /evidence="ECO:0007829|PDB:2UUR"
FT STRAND 215..225
FT /evidence="ECO:0007829|PDB:2UUR"
FT STRAND 233..242
FT /evidence="ECO:0007829|PDB:2UUR"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:2UUR"
FT HELIX 759..771
FT /evidence="ECO:0007829|PDB:5CTD"
FT HELIX 774..781
FT /evidence="ECO:0007829|PDB:5CTD"
SQ SEQUENCE 921 AA; 91869 MW; A69BF076127283D0 CRC64;
MKTCWKIPVF FFVCSFLEPW ASAAVKRRPR FPVNSNSNGG NELCPKIRIG QDDLPGFDLI
SQFQVDKAAS RRAIQRVVGS ATLQVAYKLG NNVDFRIPTR NLYPSGLPEE YSFLTTFRMT
GSTLKKNWNI WQIQDSSGKE QVGIKINGQT QSVVFSYKGL DGSLQTAAFS NLSSLFDSQW
HKIMIGVERS SATLFVDCNR IESLPIKPRG PIDIDGFAVL GKLADNPQVS VPFELQWMLI
HCDPLRPRRE TCHELPARIT PSQTTDERGP PGEQGPPGPP GPPGVPGIDG IDGDRGPKGP
PGPPGPAGEP GKPGAPGKPG TPGADGLTGP DGSPGSIGSK GQKGEPGVPG SRGFPGRGIP
GPPGPPGTAG LPGELGRVGP VGDPGRRGPP GPPGPPGPRG TIGFHDGDPL CPNACPPGRS
GYPGLPGMRG HKGAKGEIGE PGRQGHKGEE GDQGELGEVG AQGPPGAQGL RGITGIVGDK
GEKGARGLDG EPGPQGLPGA PGDQGQRGPP GEAGPKGDRG AEGARGIPGL PGPKGDTGLP
GVDGRDGIPG MPGTKGEPGK PGPPGDAGLQ GLPGVPGIPG AKGVAGEKGS TGAPGKPGQM
GNSGKPGQQG PPGEVGPRGP QGLPGSRGEL GPVGSPGLPG KLGSLGSPGL PGLPGPPGLP
GMKGDRGVVG EPGPKGEQGA SGEEGEAGER GELGDIGLPG PKGSAGNPGE PGLRGPEGSR
GLPGVEGPRG PPGPRGVQGE QGATGLPGVQ GPPGRAPTDQ HIKQVCMRVI QEHFAEMAAS
LKRPDSGATG LPGRPGPPGP PGPPGENGFP GQMGIRGLPG IKGPPGALGL RGPKGDLGEK
GERGPPGRGP NGLPGAIGLP GDPGPASYGR NGRDGERGPP GVAGIPGVPG PPGPPGLPGF
CEPASCTMQA GQRAFNKGPD P
