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   24-JAN-2024, entry version 129.
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}.
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; 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.
DR   RefSeq; XP_011510728.1; XM_011512426.2. [A6NMZ7-1]
DR   RefSeq; XP_011510730.1; XM_011512428.2.
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.
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   GlyCosmos; A6NMZ7; 10 sites, 8 glycans.
DR   GlyGen; A6NMZ7; 10 sites, 8 N-linked glycans (4 sites).
DR   iPTMnet; A6NMZ7; -.
DR   PhosphoSitePlus; A6NMZ7; -.
DR   SwissPalm; A6NMZ7; -.
DR   BioMuta; COL6A6; -.
DR   EPD; A6NMZ7; -.
DR   jPOST; A6NMZ7; -.
DR   MassIVE; A6NMZ7; -.
DR   MaxQB; A6NMZ7; -.
DR   PaxDb; 9606-ENSP00000351310; -.
DR   PeptideAtlas; 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   AGR; HGNC:27023; -.
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; 5359724at2759; -.
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 1139 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 94 other cell types or tissues.
DR   ExpressionAtlas; A6NMZ7; baseline and differential.
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   CDD; cd01472; vWA_collagen; 3.
DR   CDD; cd01450; vWFA_subfamily_ECM; 3.
DR   Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 8.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR22588:SF5; COLLAGEN ALPHA-6(VI) CHAIN; 1.
DR   PANTHER; PTHR22588; UNCHARACTERIZED; 1.
DR   Pfam; PF01391; Collagen; 1.
DR   Pfam; PF00092; VWA; 8.
DR   PRINTS; PR00453; VWFADOMAIN.
DR   SMART; SM00327; VWA; 9.
DR   SUPFAM; SSF53300; vWA-like; 9.
DR   PROSITE; PS50234; VWFA; 9.
DR   Genevisible; A6NMZ7; HS.
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
//