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 27-MAR-2024, entry version 231. 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 VARIANT STL4 295-ARG--PRO-921 DEL, AND 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). RN [11] RP VARIANTS STL4 295-ARG--PRO-921 DEL AND 507-ARG--PRO-921 DEL, AND RP INVOLVEMENT IN STL4. RX PubMed=21421862; DOI=10.1167/iovs.10-7128; RA Nikopoulos K., Schrauwen I., Simon M., Collin R.W., Veckeneer M., RA Keymolen K., Van Camp G., Cremers F.P., van den Born L.I.; RT "Autosomal recessive Stickler syndrome in two families is caused by RT mutations in the COL9A1 gene."; RL Invest. Ophthalmol. Vis. Sci. 52:4774-4779(2011). RN [12] RP VARIANT STL4 507-ARG--PRO-921 DEL. RX PubMed=31090205; DOI=10.1002/ajmg.a.61191; RA Nixon T.R.W., Alexander P., Richards A., McNinch A., Bearcroft P.W.P., RA Cobben J., Snead M.P.; RT "Homozygous Type IX collagen variants (COL9A1, COL9A2, and COL9A3) causing RT recessive Stickler syndrome-Expanding the phenotype."; RL Am. J. Med. Genet. A 179:1498-1506(2019). 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 ECO:0000269|PubMed:21421862, ECO:0000269|PubMed:31090205}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the fibril-associated collagens with interrupted CC helices (FACIT) family. {ECO:0000305}. 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; 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 CCDS; CCDS93941.1; -. [P20849-3] 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; 11. DR ComplexPortal; CPX-1748; Collagen type IX trimer. DR IntAct; P20849; 10. DR MINT; P20849; -. DR STRING; 9606.ENSP00000349790; -. DR GlyCosmos; P20849; 1 site, No reported glycans. DR GlyGen; P20849; 1 site. DR iPTMnet; P20849; -. DR PhosphoSitePlus; P20849; -. DR BioMuta; COL9A1; -. DR DMDM; 296439373; -. DR MassIVE; P20849; -. DR PaxDb; 9606-ENSP00000349790; -. DR PeptideAtlas; P20849; -. DR ProteomicsDB; 53816; -. [P20849-1] DR ProteomicsDB; 53817; -. [P20849-2] DR ProteomicsDB; 53818; -. [P20849-3] DR Antibodypedia; 17698; 207 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 AGR; HGNC:2217; -. DR CTD; 1297; -. DR DisGeNET; 1297; -. DR GeneCards; COL9A1; -. DR GeneReviews; COL9A1; -. DR HGNC; HGNC:2217; COL9A1. DR HPA; ENSG00000112280; Tissue enhanced (brain, 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; KHWSIWQ; -. DR OrthoDB; 2968414at2759; -. 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 1139 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 114 other cell types or tissues. DR ExpressionAtlas; P20849; baseline and differential. 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:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0030246; F:carbohydrate binding; IMP:DisProt. DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL. DR GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc. DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central. DR Gene3D; 2.60.120.200; -; 1. DR InterPro; IPR008160; Collagen. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR048287; TSPN-like_N. DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1. DR PANTHER; PTHR24023:SF1100; FIBRILLAR COLLAGEN NC1 DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF01391; Collagen; 8. DR SMART; SM00210; TSPN; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR Genevisible; P20849; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Collagen; Deafness; KW Direct protein sequencing; Disease variant; Disulfide bond; KW Extracellular matrix; Glycoprotein; Hydroxylation; Metal-binding; KW Reference proteome; Repeat; 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 295..921 FT /note="Missing (in STL4)" FT /evidence="ECO:0000269|PubMed:16909383, FT ECO:0000269|PubMed:21421862" FT /id="VAR_087538" FT VARIANT 339 FT /note="S -> P (in dbSNP:rs592121)" FT /evidence="ECO:0000269|PubMed:11565064" FT /id="VAR_026463" FT VARIANT 507..921 FT /note="Missing (in STL4)" FT /evidence="ECO:0000269|PubMed:21421862, FT ECO:0000269|PubMed:31090205" FT /id="VAR_087539" 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 //