ID CO4A6_HUMAN Reviewed; 1691 AA. AC Q14031; Q12823; Q14053; Q5JYH6; Q5JYH8; Q9NQM5; Q9NTX3; Q9UJ76; Q9UMG6; AC Q9Y4L4; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 3. DT 27-MAR-2024, entry version 222. DE RecName: Full=Collagen alpha-6(IV) chain; DE Flags: Precursor; GN Name=COL4A6; 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] (ISOFORM B). RC TISSUE=Eye, and Kidney; RX PubMed=8125972; DOI=10.1016/s0021-9258(17)37317-9; RA Oohashi T., Sugimoto M., Mattei M.-G., Ninomiya Y.; RT "Identification of a new collagen IV chain, alpha 6(IV), by cDNA isolation RT and assignment of the gene to chromosome Xq22, which is the same locus for RT COL4A5."; RL J. Biol. Chem. 269:7520-7526(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A). RX PubMed=8175748; DOI=10.1016/s0021-9258(17)36818-7; RA Zhou J., Ding M., Zhao Z., Reeders S.T.; RT "Complete primary structure of the sixth chain of human basement membrane RT collagen, alpha 6(IV). Isolation of the cDNAs for alpha 6(IV) and RT comparison with five other type IV collagen chains."; RL J. Biol. Chem. 269:13193-13199(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS A AND B), AND VARIANTS ALA-455 RP AND LYS-1110. RX PubMed=8661006; DOI=10.1006/geno.1996.0222; RA Zhang X., Zhou J., Reeders S.T., Tryggvason K.; RT "Structure of the human type IV collagen COL4A6 gene, which is mutated in RT Alport syndrome-associated leiomyomatosis."; RL Genomics 33:473-479(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [5] 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-542 (ISOFORM A), AND INVOLVEMENT IN DL-ATS. RX PubMed=8356449; DOI=10.1126/science.8356449; RA Zhou J., Mochizuki T., Smeets H., Antignac C., Laurila P., de Paepe A., RA Tryggvason K., Reeders S.T.; RT "Deletion of the paired alpha 5(IV) and alpha 6(IV) collagen genes in RT inherited smooth muscle tumors."; RL Science 261:1167-1169(1993). RN [7] RP INVOLVEMENT IN DL-ATS. RX PubMed=12784310; DOI=10.1002/ajmg.a.20019; RA Anker M.C., Arnemann J., Neumann K., Ahrens P., Schmidt H., Koenig R.; RT "Alport syndrome with diffuse leiomyomatosis."; RL Am. J. Med. Genet. A 119:381-385(2003). RN [8] RP VARIANT [LARGE SCALE ANALYSIS] GLU-1130. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [9] RP VARIANT DFNX6 SER-591. RX PubMed=23714752; DOI=10.1038/ejhg.2013.108; RA Rost S., Bach E., Neuner C., Nanda I., Dysek S., Bittner R.E., Keller A., RA Bartsch O., Mlynski R., Haaf T., Mueller C.R., Kunstmann E.; RT "Novel form of X-linked nonsyndromic hearing loss with cochlear RT malformation caused by a mutation in the type IV collagen gene COL4A6."; RL Eur. J. Hum. Genet. 22:208-215(2014). CC -!- FUNCTION: Type IV collagen is the major structural component of CC glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork CC together with laminins, proteoglycans and entactin/nidogen. CC -!- SUBUNIT: There are six type IV collagen isoforms, alpha 1(IV)-alpha CC 6(IV), each of which can form a triple helix structure with 2 other CC chains to generate type IV collagen network. CC -!- INTERACTION: CC Q14031; P05067: APP; NbExp=3; IntAct=EBI-2432407, EBI-77613; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix, basement membrane. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=A; CC IsoId=Q14031-1; Sequence=Displayed; CC Name=B; CC IsoId=Q14031-2; Sequence=VSP_001174; CC -!- DOMAIN: Alpha chains of type IV collagen have a non-collagenous domain CC (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats CC in the long central triple-helical domain (which may cause flexibility CC in the triple helix), and a short N-terminal triple-helical 7S domain. 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 -!- PTM: Type IV collagens contain numerous cysteine residues which are CC involved in inter- and intramolecular disulfide bonding. 12 of these, CC located in the NC1 domain, are conserved in all known type IV CC collagens. CC -!- PTM: The trimeric structure of the NC1 domains is stabilized by CC covalent bonds between Lys and Met residues. {ECO:0000250}. CC -!- DISEASE: Note=Deletions covering the N-terminal regions of COL4A5 and CC COL4A6, which are localized in a head-to-head manner, are found in the CC chromosome Xq22.3 centromeric deletion syndrome. This results in a CC phenotype with features of diffuse leiomyomatosis and Alport syndrome CC (DL-ATS). CC -!- DISEASE: Deafness, X-linked, 6 (DFNX6) [MIM:300914]: A non-syndromic CC form of sensorineural hearing loss with prelingual onset. Sensorineural CC deafness results from damage to the neural receptors of the inner ear, CC the nerve pathways to the brain, or the area of the brain that receives CC sound information. {ECO:0000269|PubMed:23714752}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the type IV collagen family. CC {ECO:0000255|PROSITE-ProRule:PRU00736}. 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; D21337; BAA04809.1; -; mRNA. DR EMBL; U04845; AAA19569.2; -; mRNA. DR EMBL; U47004; AAB19038.1; -; Genomic_DNA. DR EMBL; U46959; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46961; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46962; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46963; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46964; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46965; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46966; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46967; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46968; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46969; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46970; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46971; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46972; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46973; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46974; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46975; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46976; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46977; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46978; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46979; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46980; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46981; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46982; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46983; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46984; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46985; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46986; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46987; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46988; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46989; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46990; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46991; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46992; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46993; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46994; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46995; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46996; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46997; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46998; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U46999; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U47000; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U47001; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U47002; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U47003; AAB19038.1; JOINED; Genomic_DNA. DR EMBL; U47004; AAB19039.1; -; Genomic_DNA. DR EMBL; U46960; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46961; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46962; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46963; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46964; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46965; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46966; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46967; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46968; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46969; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46970; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46971; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46972; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46973; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46974; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46975; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46976; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46977; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46978; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46979; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46980; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46981; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46982; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46983; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46984; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46985; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46986; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46987; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46988; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46989; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46990; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46991; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46992; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46993; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46994; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46995; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46996; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46997; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46998; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U46999; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U47000; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U47001; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U47002; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; U47003; AAB19039.1; JOINED; Genomic_DNA. DR EMBL; AL136080; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL034369; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL109943; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL031177; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471120; EAX02688.1; -; Genomic_DNA. DR EMBL; L22763; AAA16338.1; -; mRNA. DR CCDS; CCDS14541.1; -. [Q14031-1] DR CCDS; CCDS14542.1; -. [Q14031-2] DR PIR; A54122; CGHU6B. DR RefSeq; NP_001274689.1; NM_001287760.1. DR RefSeq; NP_001838.2; NM_001847.3. [Q14031-1] DR RefSeq; NP_378667.1; NM_033641.3. [Q14031-2] DR AlphaFoldDB; Q14031; -. DR SMR; Q14031; -. DR BioGRID; 107685; 16. DR ComplexPortal; CPX-1724; Collagen type IV trimer variant 2. DR IntAct; Q14031; 9. DR MINT; Q14031; -. DR STRING; 9606.ENSP00000378340; -. DR ChEMBL; CHEMBL2364188; -. DR GlyCosmos; Q14031; 2 sites, 1 glycan. DR GlyGen; Q14031; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q14031; -. DR PhosphoSitePlus; Q14031; -. DR BioMuta; COL4A6; -. DR DMDM; 116241307; -. DR EPD; Q14031; -. DR jPOST; Q14031; -. DR MassIVE; Q14031; -. DR MaxQB; Q14031; -. DR PaxDb; 9606-ENSP00000378340; -. DR PeptideAtlas; Q14031; -. DR ProteomicsDB; 59800; -. [Q14031-1] DR ProteomicsDB; 59801; -. [Q14031-2] DR Pumba; Q14031; -. DR Antibodypedia; 29421; 192 antibodies from 28 providers. DR DNASU; 1288; -. DR Ensembl; ENST00000334504.12; ENSP00000334733.7; ENSG00000197565.17. [Q14031-2] DR Ensembl; ENST00000372216.8; ENSP00000361290.4; ENSG00000197565.17. [Q14031-1] DR GeneID; 1288; -. DR KEGG; hsa:1288; -. DR MANE-Select; ENST00000334504.12; ENSP00000334733.7; NM_033641.4; NP_378667.1. [Q14031-2] DR UCSC; uc004env.5; human. [Q14031-1] DR AGR; HGNC:2208; -. DR CTD; 1288; -. DR DisGeNET; 1288; -. DR GeneCards; COL4A6; -. DR HGNC; HGNC:2208; COL4A6. DR HPA; ENSG00000197565; Tissue enhanced (endometrium, urinary bladder). DR MalaCards; COL4A6; -. DR MIM; 300914; phenotype. DR MIM; 303631; gene. DR neXtProt; NX_Q14031; -. DR OpenTargets; ENSG00000197565; -. DR Orphanet; 90625; Rare X-linked non-syndromic sensorineural deafness type DFN. DR Orphanet; 1018; X-linked Alport syndrome-diffuse leiomyomatosis. DR PharmGKB; PA26723; -. DR VEuPathDB; HostDB:ENSG00000197565; -. DR eggNOG; KOG3544; Eukaryota. DR GeneTree; ENSGT00940000153991; -. DR HOGENOM; CLU_002023_1_0_1; -. DR InParanoid; Q14031; -. DR OMA; GDQGQTF; -. DR OrthoDB; 2882192at2759; -. DR PhylomeDB; Q14031; -. DR TreeFam; TF344135; -. DR PathwayCommons; Q14031; -. 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-2022090; Assembly of collagen fibrils and other multimeric structures. 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-3000157; Laminin interactions. DR Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions. DR Reactome; R-HSA-3000178; ECM proteoglycans. DR Reactome; R-HSA-8948216; Collagen chain trimerization. DR SignaLink; Q14031; -. DR SIGNOR; Q14031; -. DR BioGRID-ORCS; 1288; 16 hits in 774 CRISPR screens. DR ChiTaRS; COL4A6; human. DR GeneWiki; COL4A6; -. DR GenomeRNAi; 1288; -. DR Pharos; Q14031; Tbio. DR PRO; PR:Q14031; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q14031; Protein. DR Bgee; ENSG00000197565; Expressed in mucosa of stomach and 130 other cell types or tissues. DR ExpressionAtlas; Q14031; baseline and differential. DR GO; GO:0005604; C:basement membrane; IBA:GO_Central. DR GO; GO:0005587; C:collagen type IV trimer; IBA:GO_Central. 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:0030020; F:extracellular matrix structural constituent conferring tensile strength; HDA:BHF-UCL. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl. DR GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IBA:GO_Central. DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central. DR Gene3D; 2.170.240.10; Collagen IV, non-collagenous; 1. DR InterPro; IPR008160; Collagen. DR InterPro; IPR001442; Collagen_IV_NC. DR InterPro; IPR036954; Collagen_IV_NC_sf. DR InterPro; IPR016187; CTDL_fold. DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1. DR PANTHER; PTHR24023:SF533; COLLAGEN ALPHA-6(IV) CHAIN; 1. DR Pfam; PF01413; C4; 2. DR Pfam; PF01391; Collagen; 19. DR SMART; SM00111; C4; 2. DR SUPFAM; SSF56436; C-type lectin-like; 2. DR PROSITE; PS51403; NC1_IV; 1. DR Genevisible; Q14031; HS. PE 1: Evidence at protein level; KW Alternative splicing; Basement membrane; Cell adhesion; KW Chromosomal rearrangement; Collagen; Deafness; Disease variant; KW Disulfide bond; Extracellular matrix; Glycoprotein; Hydroxylation; KW Non-syndromic deafness; Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT CHAIN 23..1691 FT /note="Collagen alpha-6(IV) chain" FT /id="PRO_0000005853" FT DOMAIN 1467..1691 FT /note="Collagen IV NC1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736" FT REGION 23..46 FT /note="7S domain" FT REGION 47..1463 FT /note="Triple-helical region" FT REGION 108..338 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 404..473 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 486..881 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 915..1099 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1185..1459 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 515..517 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT MOTIF 560..562 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT MOTIF 986..988 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT COMPBIAS 194..214 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 430..444 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 609..623 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 127 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 1482..1571 FT /note="Or C-1482 with C-1568" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736" FT DISULFID 1515..1568 FT /note="Or C-1515 with C-1571" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736" FT DISULFID 1527..1533 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736" FT DISULFID 1590..1687 FT /note="Or C-1590 with C-1684" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736" FT DISULFID 1624..1684 FT /note="Or C-1624 with C-1687" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736" FT DISULFID 1636..1643 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736" FT VAR_SEQ 1..5 FT /note="MLINK -> MHPG (in isoform B)" FT /evidence="ECO:0000303|PubMed:8125972" FT /id="VSP_001174" FT VARIANT 455 FT /note="S -> A (in dbSNP:rs1042065)" FT /evidence="ECO:0000269|PubMed:8661006" FT /id="VAR_015216" FT VARIANT 455 FT /note="S -> P (in dbSNP:rs1042065)" FT /id="VAR_059242" FT VARIANT 591 FT /note="G -> S (in DFNX6; dbSNP:rs779748859)" FT /evidence="ECO:0000269|PubMed:23714752" FT /id="VAR_070936" FT VARIANT 1110 FT /note="N -> K (in dbSNP:rs1042067)" FT /evidence="ECO:0000269|PubMed:8661006" FT /id="VAR_015217" FT VARIANT 1126 FT /note="P -> S (in dbSNP:rs35179844)" FT /id="VAR_032972" FT VARIANT 1130 FT /note="G -> E (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035748" FT VARIANT 1162 FT /note="I -> V (in dbSNP:rs34466065)" FT /id="VAR_032973" FT VARIANT 1362 FT /note="L -> P (in dbSNP:rs35363062)" FT /id="VAR_032974" FT CONFLICT 170 FT /note="M -> I (in Ref. 2; AAA19569 and 5; AAA16338)" FT /evidence="ECO:0000305" FT CONFLICT 272..273 FT /note="IS -> LR (in Ref. 3; AAB19038/AAB19039)" FT /evidence="ECO:0000305" FT CONFLICT 366 FT /note="V -> D (in Ref. 3; AAB19038/AAB19039)" FT /evidence="ECO:0000305" FT CONFLICT 518 FT /note="R -> Q (in Ref. 3; AAB19038/AAB19039)" FT /evidence="ECO:0000305" FT CONFLICT 917 FT /note="P -> S (in Ref. 1; BAA04809 and 3; FT AAB19038/AAB19039)" FT /evidence="ECO:0000305" FT CONFLICT 1302..1313 FT /note="Missing (in Ref. 1; BAA04809)" FT /evidence="ECO:0000305" FT CONFLICT 1356 FT /note="P -> A (in Ref. 1; BAA04809)" FT /evidence="ECO:0000305" FT CONFLICT 1365 FT /note="D -> H (in Ref. 3; AAB19038/AAB19039)" FT /evidence="ECO:0000305" SQ SEQUENCE 1691 AA; 163807 MW; 9313294D4CE63067 CRC64; MLINKLWLLL VTLCLTEELA AAGEKSYGKP CGGQDCSGSC QCFPEKGARG RPGPIGIQGP TGPQGFTGST GLSGLKGERG FPGLLGPYGP KGDKGPMGVP GFLGINGIPG HPGQPGPRGP PGLDGCNGTQ GAVGFPGPDG YPGLLGPPGL PGQKGSKGDP VLAPGSFKGM KGDPGLPGLD GITGPQGAPG FPGAVGPAGP PGLQGPPGPP GPLGPDGNMG LGFQGEKGVK GDVGLPGPAG PPPSTGELEF MGFPKGKKGS KGEPGPKGFP GISGPPGFPG LGTTGEKGEK GEKGIPGLPG PRGPMGSEGV QGPPGQQGKK GTLGFPGLNG FQGIEGQKGD IGLPGPDVFI DIDGAVISGN PGDPGVPGLP GLKGDEGIQG LRGPSGVPGL PALSGVPGAL GPQGFPGLKG DQGNPGRTTI GAAGLPGRDG LPGPPGPPGP PSPEFETETL HNKESGFPGL RGEQGPKGNL GLKGIKGDSG FCACDGGVPN TGPPGEPGPP GPWGLIGLPG LKGARGDRGS GGAQGPAGAP GLVGPLGPSG PKGKKGEPIL STIQGMPGDR GDSGSQGFRG VIGEPGKDGV PGLPGLPGLP GDGGQGFPGE KGLPGLPGEK GHPGPPGLPG NGLPGLPGPR GLPGDKGKDG LPGQQGLPGS KGITLPCIIP GSYGPSGFPG TPGFPGPKGS RGLPGTPGQP GSSGSKGEPG SPGLVHLPEL PGFPGPRGEK GLPGFPGLPG KDGLPGMIGS PGLPGSKGAT GDIFGAENGA PGEQGLQGLT GHKGFLGDSG LPGLKGVHGK PGLLGPKGER GSPGTPGQVG QPGTPGSSGP YGIKGKSGLP GAPGFPGISG HPGKKGTRGK KGPPGSIVKK GLPGLKGLPG NPGLVGLKGS PGSPGVAGLP ALSGPKGEKG SVGFVGFPGI PGLPGIPGTR GLKGIPGSTG KMGPSGRAGT PGEKGDRGNP GPVGIPSPRR PMSNLWLKGD KGSQGSAGSN GFPGPRGDKG EAGRPGPPGL PGAPGLPGII KGVSGKPGPP GFMGIRGLPG LKGSSGITGF PGMPGESGSQ GIRGSPGLPG ASGLPGLKGD NGQTVEISGS PGPKGQPGES GFKGTKGRDG LIGNIGFPGN KGEDGKVGVS GDVGLPGAPG FPGVAGMRGE PGLPGSSGHQ GAIGPLGSPG LIGPKGFPGF PGLHGLNGLP GTKGTHGTPG PSITGVPGPA GLPGPKGEKG YPGIGIGAPG KPGLRGQKGD RGFPGLQGPA GLPGAPGISL PSLIAGQPGD PGRPGLDGER GRPGPAGPPG PPGPSSNQGD TGDPGFPGIP GPKGPKGDQG IPGFSGLPGE LGLKGMRGEP GFMGTPGKVG PPGDPGFPGM KGKAGPRGSS GLQGDPGQTP TAEAVQVPPG PLGLPGIDGI PGLTGDPGAQ GPVGLQGSKG LPGIPGKDGP SGLPGPPGAL GDPGLPGLQG PPGFEGAPGQ QGPFGMPGMP GQSMRVGYTL VKHSQSEQVP PCPIGMSQLW VGYSLLFVEG QEKAHNQDLG FAGSCLPRFS TMPFIYCNIN EVCHYARRND KSYWLSTTAP IPMMPVSQTQ IPQYISRCSV CEAPSQAIAV HSQDITIPQC PLGWRSLWIG YSFLMHTAAG AEGGGQSLVS PGSCLEDFRA TPFIECSGAR GTCHYFANKY SFWLTTVEER QQFGELPVSE TLKAGQLHTR VSRCQVCMKS L //