CO6A6_HUMAN
ID CO6A6_HUMAN Reviewed; 2263 AA.
AC A6NMZ7; A7DZQ0; A7DZQ1; A7DZQ2; Q69YT0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Collagen alpha-6(VI) chain;
DE Flags: Precursor;
GN Name=COL6A6;
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 1).
RX PubMed=18276594; DOI=10.1074/jbc.m709540200;
RA Gara S.K., Grumati P., Urciuolo A., Bonaldo P., Kobbe B., Koch M.,
RA Paulsson M., Wagener R.;
RT "Three novel collagen VI chains with high homology to the alpha 3 chain.";
RL J. Biol. Chem. 283:10658-10670(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1364-2263 (ISOFORM 2).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-198; ASN-275; ASN-288; ASN-930;
RP ASN-988 AND ASN-1290.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Collagen VI acts as a cell-binding protein. {ECO:0000250}.
CC -!- SUBUNIT: Trimers composed of three different chains: alpha-1(VI),
CC alpha-2(VI), and alpha-3(VI) or alpha-5(VI) or alpha-6(VI).
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}. Note=Deposed in the extracellular matrix of
CC skeletal muscle. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A6NMZ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A6NMZ7-2; Sequence=VSP_033914, VSP_033915;
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the type VI collagen family. {ECO:0000305}.
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DR EMBL; AM774225; CAO81741.1; -; mRNA.
DR EMBL; AM774226; CAO81739.1; -; mRNA.
DR EMBL; AM774227; CAO81740.1; -; mRNA.
DR EMBL; AC093006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC128683; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL713792; CAH10639.2; -; mRNA.
DR CCDS; CCDS46911.1; -. [A6NMZ7-1]
DR RefSeq; NP_001096078.1; NM_001102608.1. [A6NMZ7-1]
DR RefSeq; XP_005247178.1; XM_005247121.4. [A6NMZ7-1]
DR RefSeq; XP_011510727.1; XM_011512425.2. [A6NMZ7-1]
DR RefSeq; XP_011510728.1; XM_011512426.2. [A6NMZ7-1]
DR RefSeq; XP_011510730.1; XM_011512428.2. [A6NMZ7-1]
DR RefSeq; XP_016861200.1; XM_017005711.1. [A6NMZ7-1]
DR RefSeq; XP_016861201.1; XM_017005712.1. [A6NMZ7-1]
DR RefSeq; XP_016861202.1; XM_017005713.1. [A6NMZ7-1]
DR RefSeq; XP_016861203.1; XM_017005714.1. [A6NMZ7-1]
DR RefSeq; XP_016861204.1; XM_017005715.1. [A6NMZ7-1]
DR AlphaFoldDB; A6NMZ7; -.
DR SMR; A6NMZ7; -.
DR BioGRID; 126296; 2.
DR IntAct; A6NMZ7; 2.
DR STRING; 9606.ENSP00000351310; -.
DR ChEMBL; CHEMBL2364188; -.
DR GlyConnect; 1140; 8 N-Linked glycans (4 sites).
DR GlyGen; A6NMZ7; 10 sites, 8 N-linked glycans (4 sites).
DR iPTMnet; A6NMZ7; -.
DR PhosphoSitePlus; A6NMZ7; -.
DR BioMuta; COL6A6; -.
DR EPD; A6NMZ7; -.
DR jPOST; A6NMZ7; -.
DR MassIVE; A6NMZ7; -.
DR MaxQB; A6NMZ7; -.
DR PaxDb; A6NMZ7; -.
DR PeptideAtlas; A6NMZ7; -.
DR PRIDE; A6NMZ7; -.
DR ProteomicsDB; 1573; -. [A6NMZ7-1]
DR ProteomicsDB; 1574; -. [A6NMZ7-2]
DR Antibodypedia; 56016; 62 antibodies from 11 providers.
DR DNASU; 131873; -.
DR Ensembl; ENST00000358511.11; ENSP00000351310.6; ENSG00000206384.11. [A6NMZ7-1]
DR GeneID; 131873; -.
DR KEGG; hsa:131873; -.
DR MANE-Select; ENST00000358511.11; ENSP00000351310.6; NM_001102608.3; NP_001096078.1.
DR UCSC; uc010htl.4; human. [A6NMZ7-1]
DR CTD; 131873; -.
DR DisGeNET; 131873; -.
DR GeneCards; COL6A6; -.
DR HGNC; HGNC:27023; COL6A6.
DR HPA; ENSG00000206384; Tissue enriched (parathyroid).
DR MIM; 616613; gene.
DR neXtProt; NX_A6NMZ7; -.
DR OpenTargets; ENSG00000206384; -.
DR PharmGKB; PA165697087; -.
DR VEuPathDB; HostDB:ENSG00000206384; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000155619; -.
DR HOGENOM; CLU_000182_0_0_1; -.
DR InParanoid; A6NMZ7; -.
DR OMA; NFIRNTS; -.
DR OrthoDB; 1049829at2759; -.
DR PhylomeDB; A6NMZ7; -.
DR TreeFam; TF318242; -.
DR PathwayCommons; A6NMZ7; -.
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; A6NMZ7; -.
DR SIGNOR; A6NMZ7; -.
DR BioGRID-ORCS; 131873; 9 hits in 1062 CRISPR screens.
DR ChiTaRS; COL6A6; human.
DR GenomeRNAi; 131873; -.
DR Pharos; A6NMZ7; Tbio.
DR PRO; PR:A6NMZ7; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; A6NMZ7; protein.
DR Bgee; ENSG00000206384; Expressed in buccal mucosa cell and 93 other tissues.
DR ExpressionAtlas; A6NMZ7; baseline and differential.
DR Genevisible; A6NMZ7; HS.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR Gene3D; 3.40.50.410; -; 8.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF01391; Collagen; 1.
DR Pfam; PF00092; VWA; 8.
DR SMART; SM00327; VWA; 9.
DR SUPFAM; SSF53300; SSF53300; 9.
DR PROSITE; PS50234; VWFA; 9.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Collagen; Extracellular matrix;
KW Glycoprotein; Hydroxylation; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..2263
FT /note="Collagen alpha-6(VI) chain"
FT /id="PRO_5000266306"
FT DOMAIN 27..206
FT /note="VWFA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 229..411
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 436..606
FT /note="VWFA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 622..791
FT /note="VWFA 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 809..982
FT /note="VWFA 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1000..1171
FT /note="VWFA 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1187..1371
FT /note="VWFA 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1757..1937
FT /note="VWFA 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1965..2166
FT /note="VWFA 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 20..1391
FT /note="Nonhelical region"
FT REGION 1392..1725
FT /note="Triple-helical region"
FT REGION 1397..1723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1726..2263
FT /note="Nonhelical region"
FT MOTIF 1508..1510
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 930
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 988
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 1290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT VAR_SEQ 1512..1520
FT /note="GAPGVDSSI -> VSARAANWS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_033914"
FT VAR_SEQ 1521..2263
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_033915"
FT VARIANT 345
FT /note="E -> K (in dbSNP:rs4613427)"
FT /id="VAR_043609"
FT VARIANT 370
FT /note="A -> T (in dbSNP:rs9830253)"
FT /id="VAR_043610"
FT VARIANT 461
FT /note="E -> A (in dbSNP:rs11921769)"
FT /id="VAR_043611"
FT VARIANT 556
FT /note="P -> S (in dbSNP:rs59021909)"
FT /id="VAR_061120"
FT VARIANT 1739
FT /note="R -> Q (in dbSNP:rs16830494)"
FT /id="VAR_043612"
FT VARIANT 1799
FT /note="H -> R (in dbSNP:rs7614116)"
FT /id="VAR_043613"
FT CONFLICT 1429
FT /note="A -> V (in Ref. 3; CAH10639)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2263 AA; 247173 MW; EED4F30ABAED7F30 CRC64;
MMLLILFLVI ICSHISVNQD SGPEYADVVF LVDSSDRLGS KSFPFVKMFI TKMISSLPIE
ADKYRVALAQ YSDKLHSEFH LSTFKGRSPM LNHLRKNFGF IGGSLQIGKA LQEAHRTYFS
APANGRDKKQ FPPILVVLAS SESEDNVEEA SKALRKDGVK IISVGVQKAS EENLKAMATS
QFHFNLRTVR DLSMFSQNMT HIIKDVIKYK EGAVDDIFVE ACQGPSMADV VFLLDMSING
SEENFDYLKG FLEESVSALD IKENCMRVGL VAYSNETKVI NSLSMGINKS EVLQHIQNLS
PRTGKAYTGA AIKKLRKEVF SARNGSRKNQ GVPQIAVLVT HRDSEDNVTK AAVNLRREGV
TIFTLGIEGA SDTQLEKIAS HPAEQYVSKL KTFADLAAHN QTFLKKLRNQ ITHTVSVFSE
RTETLKSGCV DTEEADIYLL IDGSGSTQAT DFHEMKTFLS EVVGMFNIAP HKVRVGAVQY
ADSWDLEFEI NKYSNKQDLG KAIENIRQMG GNTNTGAALN FTLSLLQKAK KQRGNKVPCH
LVVLTNGMSK DSILEPANRL REEHIRVYAI GIKEANQTQL REIAGEEKRV YYVHDFDALK
DIRNQVVQEI CTEEACKEMK ADIMFLVDSS GSIGPENFSK MKTFMKNLVS KSQIGPDRVQ
IGVVQFSDIN KEEFQLNRFM SQSDISNAID QMAHIGQTTL TGSALSFVSQ YFSPTKGARP
NIRKFLILIT DGEAQDIVKE PAVVLRQEGV IIYSVGVFGS NVTQLEEISG RPEMVFYVEN
FDILQRIEDD LVFGICSPRE ECKRIEVLDV VFVIDSSGSI DYDEYNIMKD FMIGLVKKAD
VGKNQVRFGA LKYADDPEVL FYLDDFGTKL EVISVLQNDQ AMGGSTYTAE ALGFSDHMFT
EARGSRLNKG VPQVLIVITD GESHDADKLN ATAKALRDKG ILVLAVGIDG ANPVELLAMA
GSSDKYFFVE TFGGLKGIFS DVTASVCNSS KVDCEIDKVD LVFLMDGSTS IQPNDFKKMK
EFLASVVQDF DVSLNRVRIG AAQFSDTYHP EFPLGTFIGE KEISFQIENI KQIFGNTHIG
AALREVEHYF RPDMGSRINT GTPQVLLVLT DGQSQDEVAQ AAEALRHRGI DIYSVGIGDV
DDQQLIQITG TAEKKLTVHN FDELKKVNKR IVRNICTTAG ESNCFVDVVV GFDVSTQEKG
QTLLEGQPWM ETYLQDILRA ISSLNGVSCE VGTETQVSVA FQVTNAMEKY SPKFEIYSEN
ILNSLKDITV KGPSLLNANL LDSLWDTFQN KSAARGKVVL LFSDGLDDDV EKLEQKSDEL
RKEGLNALIT VALDGPADSS DLADLPYIEF GKGFEYRTQL SIGMRELGSR LSKQLVNVAE
RTCCCLFCKC IGGDGTMGDP GPPGKRGPPG FKGSEGYLGE EGIAGERGAP GPVGEQGTKG
CYGTKGPKGN RGLNGQEGEV GENGIDGLNG EQGDNGLPGR KGEKGDEGSQ GSPGKRGTPG
DRGAKGLRGD PGAPGVDSSI EGPTGLKGER GRQGRRGWPG PPGTPGSRRK TAAHGRRGHT
GPQGTAGIPG PDGLEGSLGL KGPQGPRGEA GVKGEKGGVG SKGPQGPPGP GGEAGNQGRL
GSQGNKGEPG DLGEKGAVGF PGPRGLQGND GSPGYGSVGR KGAKGQEGFP GESGPKGEIG
DPGGPGETGL KGARGKMISA GLPGEMGSPG EPGPPGRKGV KGAKGLASFS TCELIQYVRD
RSPGRHGKPE CPVHPTELVF ALDHSRDVTE QEFERMKEMM AFLVRDIKVR ENSCPVGAHI
AILSYNSHAR HLVRFSDAYK KSQLLREIET IPYERSSASR EIGRAMRFIS RNVFKRTLPG
AHTRKIATFF SSGQSADAHS ITTAAMEFGA LEIIPVVITF SNVPSVRRAF AIDDTGTFQV
IVVPSGADYI PALERLQRCT FCYDVCKPDA SCDQARPPPV QSYMDAAFLL DASRNMGSAE
FEDIRAFLGA LLDHFEITPE PETSVTGDRV ALLSHAPPDF LPNTQKSPVR AEFNLTTYRS
KRLMKRHVHE SVKQLNGDAF IGHALQWTLD NVFLSTPNLR RNKVIFVISA GETSHLDGEI
LKKESLRAKC QGYALFVFSL GPIWDDKELE DLASHPLDHH LVQLGRIHKP DHSYGVKFVK
SFINSIRRAI NKYPPINLKI KCNRLNSIDP KQPPRPFRSF VPGPLKATLK EDVLQKAKFF
QDKKYLSRVA RSGRDDAIQN FMRSTSHTFK NGRMIESAPK QHD
