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   13-FEB-2019, entry version 104.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   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.,
RA   Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA   Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA   Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA   Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA   Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA   Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA   Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA   Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA   Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA   Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA   Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA   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.,
RA   Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA   Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA   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.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., 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;
RP   ASN-930; 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
RT   multiple 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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Collagen VI acts as a cell-binding protein.
CC       {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         Note=No experimental confirmation available.;
CC   -!- PTM: Prolines at the third position of the tripeptide repeating
CC       unit (G-X-Y) are hydroxylated in some or all of the chains.
CC       {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   UniGene; Hs.591282; -.
DR   UniGene; Hs.596709; -.
DR   UniGene; Hs.596805; -.
DR   ProteinModelPortal; A6NMZ7; -.
DR   SMR; A6NMZ7; -.
DR   IntAct; A6NMZ7; 2.
DR   STRING; 9606.ENSP00000351310; -.
DR   ChEMBL; CHEMBL2364188; -.
DR   GlyConnect; 1140; -.
DR   iPTMnet; A6NMZ7; -.
DR   PhosphoSitePlus; A6NMZ7; -.
DR   BioMuta; COL6A6; -.
DR   EPD; A6NMZ7; -.
DR   jPOST; A6NMZ7; -.
DR   MaxQB; A6NMZ7; -.
DR   PaxDb; A6NMZ7; -.
DR   PRIDE; A6NMZ7; -.
DR   ProteomicsDB; 1573; -.
DR   ProteomicsDB; 1574; -. [A6NMZ7-2]
DR   Ensembl; ENST00000358511; ENSP00000351310; ENSG00000206384. [A6NMZ7-1]
DR   GeneID; 131873; -.
DR   KEGG; hsa:131873; -.
DR   UCSC; uc010htl.4; human. [A6NMZ7-1]
DR   CTD; 131873; -.
DR   EuPathDB; HostDB:ENSG00000206384.10; -.
DR   GeneCards; COL6A6; -.
DR   H-InvDB; HIX0003677; -.
DR   HGNC; HGNC:27023; COL6A6.
DR   HPA; HPA045239; -.
DR   MIM; 616613; gene.
DR   neXtProt; NX_A6NMZ7; -.
DR   OpenTargets; ENSG00000206384; -.
DR   PharmGKB; PA165697087; -.
DR   eggNOG; KOG3544; Eukaryota.
DR   eggNOG; ENOG410Y0KT; LUCA.
DR   GeneTree; ENSGT00940000155619; -.
DR   HOGENOM; HOG000111864; -.
DR   HOVERGEN; HBG107743; -.
DR   InParanoid; A6NMZ7; -.
DR   KO; K06238; -.
DR   OMA; ATDFQEM; -.
DR   OrthoDB; 1049829at2759; -.
DR   PhylomeDB; A6NMZ7; -.
DR   TreeFam; TF318242; -.
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   SIGNOR; A6NMZ7; -.
DR   ChiTaRS; COL6A6; human.
DR   GenomeRNAi; 131873; -.
DR   PRO; PR:A6NMZ7; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   Bgee; ENSG00000206384; Expressed in 97 organ(s), highest expression level in parietal pleura.
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:0030020; F:extracellular matrix structural constituent conferring tensile strength; HDA:BHF-UCL.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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; Complete proteome;
KW   Extracellular matrix; Glycoprotein; Hydroxylation; Polymorphism;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20   2263       Collagen alpha-6(VI) chain.
FT                                /FTId=PRO_5000266306.
FT   DOMAIN       27    206       VWFA 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00219}.
FT   DOMAIN      229    411       VWFA 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00219}.
FT   DOMAIN      436    606       VWFA 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00219}.
FT   DOMAIN      622    791       VWFA 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00219}.
FT   DOMAIN      809    982       VWFA 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00219}.
FT   DOMAIN     1000   1171       VWFA 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00219}.
FT   DOMAIN     1187   1371       VWFA 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00219}.
FT   DOMAIN     1757   1937       VWFA 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00219}.
FT   DOMAIN     1965   2166       VWFA 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00219}.
FT   REGION       20   1391       Nonhelical region.
FT   REGION     1392   1725       Triple-helical region.
FT   REGION     1726   2263       Nonhelical region.
FT   MOTIF      1508   1510       Cell attachment site. {ECO:0000255}.
FT   CARBOHYD    198    198       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD    275    275       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD    288    288       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD    347    347       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    520    520       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    930    930       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD    988    988       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD   1290   1290       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   VAR_SEQ    1512   1520       GAPGVDSSI -> VSARAANWS (in isoform 2).
FT                                {ECO:0000303|PubMed:17974005}.
FT                                /FTId=VSP_033914.
FT   VAR_SEQ    1521   2263       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:17974005}.
FT                                /FTId=VSP_033915.
FT   VARIANT     345    345       E -> K (in dbSNP:rs4613427).
FT                                /FTId=VAR_043609.
FT   VARIANT     370    370       A -> T (in dbSNP:rs9830253).
FT                                /FTId=VAR_043610.
FT   VARIANT     461    461       E -> A (in dbSNP:rs11921769).
FT                                /FTId=VAR_043611.
FT   VARIANT     556    556       P -> S (in dbSNP:rs59021909).
FT                                /FTId=VAR_061120.
FT   VARIANT    1739   1739       R -> Q (in dbSNP:rs16830494).
FT                                /FTId=VAR_043612.
FT   VARIANT    1799   1799       H -> R (in dbSNP:rs7614116).
FT                                /FTId=VAR_043613.
FT   CONFLICT   1429   1429       A -> V (in Ref. 3; CAH10639).
FT                                {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
//