CO4A6_HUMAN
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 03-AUG-2022, entry version 213.
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}.
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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; 14.
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 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; Q14031; -.
DR PeptideAtlas; Q14031; -.
DR PRIDE; Q14031; -.
DR ProteomicsDB; 59800; -. [Q14031-1]
DR ProteomicsDB; 59801; -. [Q14031-2]
DR Antibodypedia; 29421; 177 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 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; 1018; X-linked Alport syndrome-diffuse leiomyomatosis.
DR Orphanet; 90625; X-linked non-syndromic sensorineural deafness type DFN.
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; HGSKGQP; -.
DR OrthoDB; 63831at2759; -.
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; 13 hits in 700 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 128 other tissues.
DR ExpressionAtlas; Q14031; baseline and differential.
DR Genevisible; Q14031; HS.
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: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; 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; -; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR001442; Collagen_IV_NC.
DR InterPro; IPR036954; Collagen_IV_NC_sf.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF01413; C4; 2.
DR Pfam; PF01391; Collagen; 19.
DR SMART; SM00111; C4; 2.
DR SUPFAM; SSF56436; SSF56436; 2.
DR PROSITE; PS51403; NC1_IV; 1.
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; AAB19038/
FT 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
