CO6A2_HUMAN
ID CO6A2_HUMAN Reviewed; 1019 AA.
AC P12110; Q13909; Q13910; Q13911; Q14048; Q14049; Q16259; Q16597; Q6P0Q1;
AC Q9UML3; Q9Y4S8;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 4.
DT 03-AUG-2022, entry version 233.
DE RecName: Full=Collagen alpha-2(VI) chain;
DE Flags: Precursor;
GN Name=COL6A2;
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 2C2), SEQUENCE REVISION, AND VARIANTS
RP ASN-227; ASN-399 AND HIS-680.
RC TISSUE=Fibroblast, and Placenta;
RA Chu M.-L.;
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2C2), AND VARIANT ASN-399.
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-266, AND ALTERNATIVE SPLICING.
RX PubMed=1556127; DOI=10.1016/s0021-9258(18)42680-4;
RA Saitta B., Timpl R., Chu M.-L.;
RT "Human alpha 2(VI) collagen gene. Heterogeneity at the 5'-untranslated
RT region generated by an alternate exon.";
RL J. Biol. Chem. 267:6188-6196(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-255 AND 591-1019, AND NUCLEOTIDE SEQUENCE
RP [MRNA] OF 821-1019 (ISOFORM 2C2A).
RC TISSUE=Fibroblast, and Placenta;
RX PubMed=2551668; DOI=10.1002/j.1460-2075.1989.tb03598.x;
RA Chu M.-L., Pan T.-C., Conway D., Kuo H.J., Glanville R.W., Timpl R.,
RA Mann K., Deutzmann R.;
RT "Sequence analysis of alpha 1(VI) and alpha 2(VI) chains of human type VI
RT collagen reveals internal triplication of globular domains similar to the A
RT domains of von Willebrand factor and two alpha 2(VI) chain variants that
RT differ in the carboxy terminus.";
RL EMBO J. 8:1939-1946(1989).
RN [5]
RP PROTEIN SEQUENCE OF 179-185 AND 581-594.
RX PubMed=8168508; DOI=10.1111/j.1432-1033.1994.tb18727.x;
RA Tillet E., Wiedemann H., Golbik R., Pan T.-C., Zhang R.Z., Mann K.,
RA Chu M.-L., Timpl R.;
RT "Recombinant expression and structural and binding properties of alpha
RT 1(VI) and alpha 2(VI) chains of human collagen type VI.";
RL Eur. J. Biochem. 221:177-185(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 238-299.
RX PubMed=3665927; DOI=10.1111/j.1432-1033.1987.tb13422.x;
RA Chu M.-L., Mann K., Deutzmann R., Pribula-Conway D., Hsu-Chen C.-C.,
RA Bernard M.P., Timpl R.;
RT "Characterization of three constituent chains of collagen type VI by
RT peptide sequences and cDNA clones.";
RL Eur. J. Biochem. 168:309-317(1987).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 246-590, AND VARIANT ASN-399.
RX PubMed=1765372; DOI=10.1016/0888-7543(91)90111-q;
RA Saitta B., Wang Y.-M., Renkart L., Zhang R.-Z., Pan T.-C., Timpl R.,
RA Chu M.-L.;
RT "The exon organization of the triple-helical coding regions of the human
RT alpha 1(VI) and alpha 2(VI) collagen genes is highly similar.";
RL Genomics 11:145-153(1991).
RN [8]
RP PROTEIN SEQUENCE OF 251-264.
RX PubMed=6852033; DOI=10.1111/j.1432-1033.1983.tb07427.x;
RA Jander R., Rauterberg J., Glanville R.W.;
RT "Further characterization of the three polypeptide chains of bovine and
RT human short-chain collagen (intima collagen).";
RL Eur. J. Biochem. 133:39-46(1983).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 256-590.
RX PubMed=3198591; DOI=10.1016/s0021-9258(18)37327-7;
RA Chu M.-L., Conway D., Pan T.-C., Baldwin C., Mann K., Deutzmann R.,
RA Timpl R.;
RT "Amino acid sequence of the triple-helical domain of human collagen type
RT VI.";
RL J. Biol. Chem. 263:18601-18606(1988).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 316-359.
RC TISSUE=Placenta;
RX PubMed=3348212;
RA Weil D., Mattei M.-G., Passage E., N'Guyen V.C., Pribula-Conway D.,
RA Mann K., Deutzmann R., Timpl R., Chu M.-L.;
RT "Cloning and chromosomal localization of human genes encoding the three
RT chains of type VI collagen.";
RL Am. J. Hum. Genet. 42:435-445(1988).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 591-1019, ALTERNATIVE SPLICING, AND VARIANT
RP HIS-680.
RX PubMed=1690728; DOI=10.1016/s0021-9258(19)39351-2;
RA Saitta B., Stokes D.G., Vissing H., Timpl R., Chu M.-L.;
RT "Alternative splicing of the human alpha 2(VI) collagen gene generates
RT multiple mRNA transcripts which predict three protein variants with
RT distinct carboxyl termini.";
RL J. Biol. Chem. 265:6473-6480(1990).
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 820-1019 (ISOFORM 2C2).
RC TISSUE=Uterus;
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 [13]
RP SUBCELLULAR LOCATION.
RX PubMed=8305732; DOI=10.1091/mbc.4.11.1097;
RA Nishiyama A., Stallcup W.B.;
RT "Expression of NG2 proteoglycan causes retention of type VI collagen on the
RT cell surface.";
RL Mol. Biol. Cell 4:1097-1108(1993).
RN [14]
RP INTERACTION WITH CSPG4.
RX PubMed=9099729; DOI=10.1074/jbc.272.16.10769;
RA Tillet E., Ruggiero F., Nishiyama A., Stallcup W.B.;
RT "The membrane-spanning proteoglycan NG2 binds to collagens V and VI through
RT the central nonglobular domain of its core protein.";
RL J. Biol. Chem. 272:10769-10776(1997).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-140; ASN-785; ASN-897 AND
RP ASN-954.
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-701, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22905912; DOI=10.1021/pr300539b;
RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P.,
RA Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion profile.";
RL J. Proteome Res. 11:4733-4743(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-705, AND IDENTIFICATION BY
RP 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).
RN [19]
RP VARIANT BTHLM1 SER-271.
RX PubMed=8782832; DOI=10.1038/ng0996-113;
RA Joebsis G.J., Keizers H., Vreijling J.P., de Visser M., Speer M.C.,
RA Wolterman R.A., Baas F., Bohlhuis P.A.;
RT "Type VI collagen mutations in Bethlem myopathy, an autosomal dominant
RT myopathy with contractures.";
RL Nat. Genet. 14:113-115(1996).
RN [20]
RP VARIANT BTHLM1 ASN-621.
RX PubMed=11865138; DOI=10.1212/wnl.58.4.593;
RA Scacheri P.C., Gillanders E.M., Subramony S.H., Vedanarayanan V.,
RA Crowe C.A., Thakore N., Bingler M., Hoffman E.P.;
RT "Novel mutations in collagen VI genes: expansion of the Bethlem myopathy
RT phenotype.";
RL Neurology 58:593-602(2002).
RN [21]
RP VARIANTS UCMD1 PRO-837 AND ASN-897 DEL, CHARACTERIZATION OF VARIANTS UCMD1
RP PRO-837 AND ASN-897 DEL, AND VARIANTS ASN-227; ASN-399 AND HIS-680.
RX PubMed=15563506; DOI=10.1093/hmg/ddi025;
RA Baker N.L., Moergelin M., Peat R., Goemans N., North K.N., Bateman J.F.,
RA Lamande S.R.;
RT "Dominant collagen VI mutations are a common cause of Ullrich congenital
RT muscular dystrophy.";
RL Hum. Mol. Genet. 14:279-293(2005).
RN [22]
RP VARIANTS BTHLM1 SER-700 AND ARG-777, VARIANTS UCMD1 ARG-283; HIS-498;
RP ARG-531; ARG-777 AND SER-876, AND VARIANTS LYS-106; ASN-227; ASN-399;
RP GLN-489; SER-518; HIS-680; CYS-724; HIS-784; GLY-804; GLN-853 AND ARG-935.
RX PubMed=15689448; DOI=10.1136/jmg.2004.023754;
RA Lampe A.K., Dunn D.M., von Niederhausern A.C., Hamil C., Aoyagi A.,
RA Laval S.H., Marie S.K., Chu M.-L., Swoboda K., Muntoni F., Bonnemann C.G.,
RA Flanigan K.M., Bushby K.M.D., Weiss R.B.;
RT "Automated genomic sequence analysis of the three collagen VI genes:
RT applications to Ullrich congenital muscular dystrophy and Bethlem
RT myopathy.";
RL J. Med. Genet. 42:108-120(2005).
RN [23]
RP VARIANT BTHLM1 LEU-932, AND VARIANTS ASN-227; ASN-399; HIS-680 AND ARG-895.
RX PubMed=17886299; DOI=10.1002/ana.21213;
RA Baker N.L., Moergelin M., Pace R.A., Peat R.A., Adams N.E., Gardner R.J.,
RA Rowland L.P., Miller G., De Jonghe P., Ceulemans B., Hannibal M.C.,
RA Edwards M., Thompson E.M., Jacobson R., Quinlivan R.C.M., Aftimos S.,
RA Kornberg A.J., North K.N., Bateman J.F., Lamande S.R.;
RT "Molecular consequences of dominant Bethlem myopathy collagen VI
RT mutations.";
RL Ann. Neurol. 62:390-405(2007).
RN [24]
RP INVOLVEMENT IN MYOSCLEROSIS.
RX PubMed=18852439; DOI=10.1212/01.wnl.0000327611.01687.5e;
RA Merlini L., Martoni E., Grumati P., Sabatelli P., Squarzoni S.,
RA Urciuolo A., Ferlini A., Gualandi F., Bonaldo P.;
RT "Autosomal recessive myosclerosis myopathy is a collagen VI disorder.";
RL Neurology 71:1245-1253(2008).
RN [25]
RP VARIANTS LYS-106; CYS-377; ASN-446; MET-728; GLN-843; GLN-853 AND CYS-1010.
RX PubMed=23040494; DOI=10.1016/j.ajhg.2012.08.017;
RA Ackerman C., Locke A.E., Feingold E., Reshey B., Espana K., Thusberg J.,
RA Mooney S., Bean L.J., Dooley K.J., Cua C.L., Reeves R.H., Sherman S.L.,
RA Maslen C.L.;
RT "An excess of deleterious variants in VEGF-A pathway genes in Down-
RT syndrome-associated atrioventricular septal defects.";
RL Am. J. Hum. Genet. 91:646-659(2012).
RN [26]
RP VARIANT GLN-853.
RX PubMed=27535533; DOI=10.1038/nature19057;
RG Exome Aggregation Consortium;
RA Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E., Fennell T.,
RA O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B., Tukiainen T.,
RA Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K., Zhao F., Zou J.,
RA Pierce-Hoffman E., Berghout J., Cooper D.N., Deflaux N., DePristo M.,
RA Do R., Flannick J., Fromer M., Gauthier L., Goldstein J., Gupta N.,
RA Howrigan D., Kiezun A., Kurki M.I., Moonshine A.L., Natarajan P.,
RA Orozco L., Peloso G.M., Poplin R., Rivas M.A., Ruano-Rubio V., Rose S.A.,
RA Ruderfer D.M., Shakir K., Stenson P.D., Stevens C., Thomas B.P., Tiao G.,
RA Tusie-Luna M.T., Weisburd B., Won H.H., Yu D., Altshuler D.M.,
RA Ardissino D., Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
RA Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S., Laakso M.,
RA McCarroll S., McCarthy M.I., McGovern D., McPherson R., Neale B.M.,
RA Palotie A., Purcell S.M., Saleheen D., Scharf J.M., Sklar P.,
RA Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C., Wilson J.G.,
RA Daly M.J., MacArthur D.G.;
RT "Analysis of protein-coding genetic variation in 60,706 humans.";
RL Nature 536:285-291(2016).
CC -!- FUNCTION: Collagen VI acts as a cell-binding protein.
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). Interacts
CC with CSPG4. {ECO:0000269|PubMed:9099729}.
CC -!- INTERACTION:
CC P12110; Q9NRI5: DISC1; NbExp=3; IntAct=EBI-928749, EBI-529989;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:8305732}. Membrane
CC {ECO:0000269|PubMed:8305732}; Peripheral membrane protein
CC {ECO:0000269|PubMed:8305732}. Note=Recruited on membranes by CSPG4.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=2C2;
CC IsoId=P12110-1; Sequence=Displayed;
CC Name=2C2A;
CC IsoId=P12110-2; Sequence=VSP_001163, VSP_001164;
CC Name=2C2A';
CC IsoId=P12110-3; Sequence=VSP_001161, VSP_001162;
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 -!- DISEASE: Bethlem myopathy 1 (BTHLM1) [MIM:158810]: A benign proximal
CC myopathy characterized by early childhood onset and joint contractures
CC most frequently affecting the elbows and ankles.
CC {ECO:0000269|PubMed:11865138, ECO:0000269|PubMed:15689448,
CC ECO:0000269|PubMed:17886299, ECO:0000269|PubMed:8782832}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Ullrich congenital muscular dystrophy 1 (UCMD1) [MIM:254090]:
CC A congenital myopathy characterized by muscle weakness and multiple
CC joint contractures, generally noted at birth or early infancy. The
CC clinical course is more severe than in Bethlem myopathy.
CC {ECO:0000269|PubMed:15563506, ECO:0000269|PubMed:15689448}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Myosclerosis autosomal recessive (MYOSAR) [MIM:255600]: A
CC condition characterized by chronic inflammation of skeletal muscle with
CC hyperplasia of the interstitial connective tissue. The clinical picture
CC includes slender muscles with firm 'woody' consistency and restriction
CC of movement of many joints because of muscle contractures. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the type VI collagen family. {ECO:0000305}.
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DR EMBL; AY029208; AAA52056.2; -; mRNA.
DR EMBL; BC065509; AAH65509.1; -; mRNA.
DR EMBL; M81835; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X15977; CAA34099.1; -; mRNA.
DR EMBL; X06195; CAA29556.1; -; mRNA.
DR EMBL; S75462; AAB20836.1; -; Genomic_DNA.
DR EMBL; S75425; AAB20836.1; JOINED; Genomic_DNA.
DR EMBL; S75428; AAB20836.1; JOINED; Genomic_DNA.
DR EMBL; S75430; AAB20836.1; JOINED; Genomic_DNA.
DR EMBL; S75432; AAB20836.1; JOINED; Genomic_DNA.
DR EMBL; S75434; AAB20836.1; JOINED; Genomic_DNA.
DR EMBL; S75436; AAB20836.1; JOINED; Genomic_DNA.
DR EMBL; S75438; AAB20836.1; JOINED; Genomic_DNA.
DR EMBL; S75440; AAB20836.1; JOINED; Genomic_DNA.
DR EMBL; S75442; AAB20836.1; JOINED; Genomic_DNA.
DR EMBL; S75444; AAB20836.1; JOINED; Genomic_DNA.
DR EMBL; S75446; AAB20836.1; JOINED; Genomic_DNA.
DR EMBL; S75448; AAB20836.1; JOINED; Genomic_DNA.
DR EMBL; S75450; AAB20836.1; JOINED; Genomic_DNA.
DR EMBL; S75452; AAB20836.1; JOINED; Genomic_DNA.
DR EMBL; S75454; AAB20836.1; JOINED; Genomic_DNA.
DR EMBL; S75456; AAB20836.1; JOINED; Genomic_DNA.
DR EMBL; S75458; AAB20836.1; JOINED; Genomic_DNA.
DR EMBL; S75460; AAB20836.1; JOINED; Genomic_DNA.
DR EMBL; M34572; AAA35618.1; -; mRNA.
DR EMBL; M34571; AAA35618.1; JOINED; mRNA.
DR EMBL; M34572; AAA35619.1; -; mRNA.
DR EMBL; M34571; AAA35619.1; JOINED; mRNA.
DR EMBL; M34573; AAA35620.1; -; mRNA.
DR EMBL; M34571; AAA35620.1; JOINED; mRNA.
DR EMBL; M34570; AAA35621.1; -; mRNA.
DR EMBL; AL096746; CAB46421.2; -; mRNA.
DR CCDS; CCDS13728.1; -. [P12110-1]
DR CCDS; CCDS13729.1; -. [P12110-2]
DR CCDS; CCDS13730.1; -. [P12110-3]
DR PIR; S05378; CGHU2A.
DR PIR; S09646; S09646.
DR PIR; T12549; T12549.
DR RefSeq; NP_001840.3; NM_001849.3. [P12110-1]
DR RefSeq; NP_478054.2; NM_058174.2. [P12110-2]
DR RefSeq; NP_478055.2; NM_058175.2. [P12110-3]
DR RefSeq; XP_011527753.1; XM_011529451.1. [P12110-1]
DR AlphaFoldDB; P12110; -.
DR SMR; P12110; -.
DR BioGRID; 107689; 128.
DR ComplexPortal; CPX-1736; Collagen type VI trimer.
DR IntAct; P12110; 31.
DR MINT; P12110; -.
DR STRING; 9606.ENSP00000300527; -.
DR ChEMBL; CHEMBL2364188; -.
DR GlyConnect; 1137; 52 N-Linked glycans (4 sites).
DR GlyGen; P12110; 9 sites, 65 N-linked glycans (4 sites), 2 O-linked glycans (3 sites).
DR iPTMnet; P12110; -.
DR PhosphoSitePlus; P12110; -.
DR BioMuta; COL6A2; -.
DR DMDM; 125987812; -.
DR REPRODUCTION-2DPAGE; P12110; -.
DR EPD; P12110; -.
DR jPOST; P12110; -.
DR MassIVE; P12110; -.
DR MaxQB; P12110; -.
DR PaxDb; P12110; -.
DR PeptideAtlas; P12110; -.
DR PRIDE; P12110; -.
DR ProteomicsDB; 52830; -. [P12110-1]
DR ProteomicsDB; 52831; -. [P12110-2]
DR ProteomicsDB; 52832; -. [P12110-3]
DR TopDownProteomics; P12110-3; -. [P12110-3]
DR Antibodypedia; 1646; 251 antibodies from 31 providers.
DR DNASU; 1292; -.
DR Ensembl; ENST00000300527.9; ENSP00000300527.4; ENSG00000142173.16. [P12110-1]
DR Ensembl; ENST00000310645.9; ENSP00000312529.5; ENSG00000142173.16. [P12110-3]
DR Ensembl; ENST00000397763.5; ENSP00000380870.1; ENSG00000142173.16. [P12110-2]
DR Ensembl; ENST00000409416.6; ENSP00000387115.1; ENSG00000142173.16. [P12110-3]
DR GeneID; 1292; -.
DR KEGG; hsa:1292; -.
DR MANE-Select; ENST00000300527.9; ENSP00000300527.4; NM_001849.4; NP_001840.3.
DR UCSC; uc002zhy.1; human. [P12110-1]
DR CTD; 1292; -.
DR DisGeNET; 1292; -.
DR GeneCards; COL6A2; -.
DR GeneReviews; COL6A2; -.
DR HGNC; HGNC:2212; COL6A2.
DR HPA; ENSG00000142173; Low tissue specificity.
DR MalaCards; COL6A2; -.
DR MIM; 120240; gene.
DR MIM; 158810; phenotype.
DR MIM; 254090; phenotype.
DR MIM; 255600; phenotype.
DR neXtProt; NX_P12110; -.
DR OpenTargets; ENSG00000142173; -.
DR Orphanet; 610; Bethlem myopathy.
DR Orphanet; 75840; Congenital muscular dystrophy, Ullrich type.
DR Orphanet; 289380; Myosclerosis.
DR PharmGKB; PA26728; -.
DR VEuPathDB; HostDB:ENSG00000142173; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000155682; -.
DR HOGENOM; CLU_009158_2_0_1; -.
DR InParanoid; P12110; -.
DR OMA; GNERQEW; -.
DR OrthoDB; 140989at2759; -.
DR PhylomeDB; P12110; -.
DR TreeFam; TF331207; -.
DR PathwayCommons; P12110; -.
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; P12110; -.
DR SIGNOR; P12110; -.
DR BioGRID-ORCS; 1292; 9 hits in 1066 CRISPR screens.
DR ChiTaRS; COL6A2; human.
DR GeneWiki; COL6A2; -.
DR GenomeRNAi; 1292; -.
DR Pharos; P12110; Tbio.
DR PRO; PR:P12110; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; P12110; protein.
DR Bgee; ENSG00000142173; Expressed in stromal cell of endometrium and 177 other tissues.
DR ExpressionAtlas; P12110; baseline and differential.
DR Genevisible; P12110; HS.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IPI:MGI.
DR GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
DR GO; GO:0005518; F:collagen binding; IPI:MGI.
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:0009749; P:response to glucose; IEA:Ensembl.
DR Gene3D; 3.40.50.410; -; 3.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF00092; VWA; 3.
DR SMART; SM00327; VWA; 3.
DR SUPFAM; SSF53300; SSF53300; 3.
DR PROSITE; PS50234; VWFA; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Collagen;
KW Congenital muscular dystrophy; Direct protein sequencing; Disease variant;
KW Extracellular matrix; Glycoprotein; Hydroxylation;
KW Limb-girdle muscular dystrophy; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1019
FT /note="Collagen alpha-2(VI) chain"
FT /id="PRO_0000005832"
FT DOMAIN 46..234
FT /note="VWFA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 615..805
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 833..1014
FT /note="VWFA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 21..256
FT /note="Nonhelical region"
FT REGION 257..590
FT /note="Triple-helical region"
FT REGION 257..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..1019
FT /note="Nonhelical region"
FT MOTIF 366..368
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 426..428
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 489..491
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 498..500
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 539..541
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 543..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..584
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 701
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 705
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 785
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 897
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 954
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT VAR_SEQ 821..991
FT /note="ELSVAQCTQRPVDIVFLLDGSERLGEQNFHKARRFVEQVARRLTLARRDDDP
FT LNARVALLQFGGPGEQQVAFPLSHNLTAIHEALETTQYLNSFSHVGAGVVHAINAIVRS
FT PRGGARRHAELSFVFLTDGVTGNDSLHESAHSMRKQNVVPTVLALGSDVDMDVLTTLSL
FT G -> DAPWPGGEPPVTFLRTEEGPDATFPRTIPLIQQLLNATELTQDPAAYSQLVAVL
FT VYTAERAKFATGVERQDWMELFIDTFKLVHRDIVGDPETALALC (in isoform
FT 2C2A)"
FT /evidence="ECO:0000303|PubMed:2551668"
FT /id="VSP_001163"
FT VAR_SEQ 821..828
FT /note="ELSVAQCT -> GLDGAVLC (in isoform 2C2A')"
FT /evidence="ECO:0000305"
FT /id="VSP_001161"
FT VAR_SEQ 829..1019
FT /note="Missing (in isoform 2C2A')"
FT /evidence="ECO:0000305"
FT /id="VSP_001162"
FT VAR_SEQ 992..1019
FT /note="Missing (in isoform 2C2A)"
FT /evidence="ECO:0000303|PubMed:2551668"
FT /id="VSP_001164"
FT VARIANT 106
FT /note="E -> K (in dbSNP:rs141703710)"
FT /evidence="ECO:0000269|PubMed:15689448,
FT ECO:0000269|PubMed:23040494"
FT /id="VAR_058225"
FT VARIANT 227
FT /note="D -> N (in dbSNP:rs35881321)"
FT /evidence="ECO:0000269|PubMed:15563506,
FT ECO:0000269|PubMed:15689448, ECO:0000269|PubMed:17886299,
FT ECO:0000269|Ref.1"
FT /id="VAR_048801"
FT VARIANT 271
FT /note="G -> S (in BTHLM1; dbSNP:rs121912940)"
FT /evidence="ECO:0000269|PubMed:8782832"
FT /id="VAR_013589"
FT VARIANT 283
FT /note="G -> R (in UCMD1; dbSNP:rs267606748)"
FT /evidence="ECO:0000269|PubMed:15689448"
FT /id="VAR_058226"
FT VARIANT 377
FT /note="R -> C (in dbSNP:rs144801620)"
FT /evidence="ECO:0000269|PubMed:23040494"
FT /id="VAR_076959"
FT VARIANT 399
FT /note="S -> N (in dbSNP:rs2839110)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15563506, ECO:0000269|PubMed:15689448,
FT ECO:0000269|PubMed:1765372, ECO:0000269|PubMed:17886299,
FT ECO:0000269|Ref.1"
FT /id="VAR_030315"
FT VARIANT 446
FT /note="D -> N (in dbSNP:rs535007570)"
FT /evidence="ECO:0000269|PubMed:23040494"
FT /id="VAR_076960"
FT VARIANT 489
FT /note="R -> Q (in dbSNP:rs61735828)"
FT /evidence="ECO:0000269|PubMed:15689448"
FT /id="VAR_058227"
FT VARIANT 498
FT /note="R -> H (in UCMD1; dbSNP:rs267606749)"
FT /evidence="ECO:0000269|PubMed:15689448"
FT /id="VAR_058228"
FT VARIANT 518
FT /note="P -> S (in dbSNP:rs141166141)"
FT /evidence="ECO:0000269|PubMed:15689448"
FT /id="VAR_058229"
FT VARIANT 531
FT /note="G -> R (in UCMD1)"
FT /evidence="ECO:0000269|PubMed:15689448"
FT /id="VAR_058230"
FT VARIANT 621
FT /note="D -> N (in BTHLM1; dbSNP:rs267606750)"
FT /evidence="ECO:0000269|PubMed:11865138"
FT /id="VAR_013590"
FT VARIANT 680
FT /note="R -> H (in dbSNP:rs1042917)"
FT /evidence="ECO:0000269|PubMed:15563506,
FT ECO:0000269|PubMed:15689448, ECO:0000269|PubMed:1690728,
FT ECO:0000269|PubMed:17886299, ECO:0000269|Ref.1"
FT /id="VAR_030316"
FT VARIANT 700
FT /note="G -> S (in BTHLM1; dbSNP:rs794727418)"
FT /evidence="ECO:0000269|PubMed:15689448"
FT /id="VAR_058231"
FT VARIANT 724
FT /note="R -> C (in dbSNP:rs150098077)"
FT /evidence="ECO:0000269|PubMed:15689448"
FT /id="VAR_058232"
FT VARIANT 728
FT /note="V -> M (in dbSNP:rs200585528)"
FT /evidence="ECO:0000269|PubMed:23040494"
FT /id="VAR_076961"
FT VARIANT 777
FT /note="C -> R (in BTHLM1; dbSNP:rs267606747)"
FT /evidence="ECO:0000269|PubMed:15689448"
FT /id="VAR_058233"
FT VARIANT 784
FT /note="R -> H (in dbSNP:rs75120695)"
FT /evidence="ECO:0000269|PubMed:15689448"
FT /id="VAR_058234"
FT VARIANT 804
FT /note="V -> G (in dbSNP:rs779847082)"
FT /evidence="ECO:0000269|PubMed:15689448"
FT /id="VAR_058235"
FT VARIANT 837
FT /note="L -> P (in UCMD1; prevents collagen VI assembly;
FT dbSNP:rs1255514828)"
FT /evidence="ECO:0000269|PubMed:15563506"
FT /id="VAR_058236"
FT VARIANT 843
FT /note="R -> Q (in dbSNP:rs201736323)"
FT /evidence="ECO:0000269|PubMed:23040494"
FT /id="VAR_076962"
FT VARIANT 853
FT /note="R -> Q (in dbSNP:rs144830948)"
FT /evidence="ECO:0000269|PubMed:15689448,
FT ECO:0000269|PubMed:23040494, ECO:0000269|PubMed:27535533"
FT /id="VAR_058237"
FT VARIANT 876
FT /note="R -> S (in UCMD1; dbSNP:rs387906608)"
FT /evidence="ECO:0000269|PubMed:15689448"
FT /id="VAR_058238"
FT VARIANT 895
FT /note="S -> R (in dbSNP:rs141233891)"
FT /evidence="ECO:0000269|PubMed:17886299"
FT /id="VAR_058239"
FT VARIANT 897
FT /note="Missing (in UCMD1; results in severe collagen VI
FT matrix deficiencies)"
FT /evidence="ECO:0000269|PubMed:15563506"
FT /id="VAR_058240"
FT VARIANT 932
FT /note="P -> L (in BTHLM1; results in reduced intracellular
FT collagen VI assembly and secretion; dbSNP:rs117725825)"
FT /evidence="ECO:0000269|PubMed:17886299"
FT /id="VAR_058241"
FT VARIANT 935
FT /note="G -> R (in dbSNP:rs35548026)"
FT /evidence="ECO:0000269|PubMed:15689448"
FT /id="VAR_048802"
FT VARIANT 1010
FT /note="F -> C (in dbSNP:rs1051148162)"
FT /evidence="ECO:0000269|PubMed:23040494"
FT /id="VAR_076963"
FT VARIANT 1015
FT /note="I -> L (in dbSNP:rs11910483)"
FT /id="VAR_048803"
FT CONFLICT 507
FT /note="K -> S (in Ref. 7; AAB20836)"
FT /evidence="ECO:0000305"
FT CONFLICT 966..967
FT /note="KQ -> NE (in Ref. 1; AAA52056 and 11; AAA35620)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1019 AA; 108579 MW; 6C513ADE46C1D111 CRC64;
MLQGTCSVLL LWGILGAIQA QQQEVISPDT TERNNNCPEK TDCPIHVYFV LDTSESVTMQ
SPTDILLFHM KQFVPQFISQ LQNEFYLDQV ALSWRYGGLH FSDQVEVFSP PGSDRASFIK
NLQGISSFRR GTFTDCALAN MTEQIRQDRS KGTVHFAVVI TDGHVTGSPC GGIKLQAERA
REEGIRLFAV APNQNLKEQG LRDIASTPHE LYRNDYATML PDSTEIDQDT INRIIKVMKH
EAYGECYKVS CLEIPGPSGP KGYRGQKGAK GNMGEPGEPG QKGRQGDPGI EGPIGFPGPK
GVPGFKGEKG EFGADGRKGA PGLAGKNGTD GQKGKLGRIG PPGCKGDPGN RGPDGYPGEA
GSPGERGDQG GKGDPGRPGR RGPPGEIGAK GSKGYQGNSG APGSPGVKGA KGGPGPRGPK
GEPGRRGDPG TKGSPGSDGP KGEKGDPGPE GPRGLAGEVG NKGAKGDRGL PGPRGPQGAL
GEPGKQGSRG DPGDAGPRGD SGQPGPKGDP GRPGFSYPGP RGAPGEKGEP GPRGPEGGRG
DFGLKGEPGR KGEKGEPADP GPPGEPGPRG PRGVPGPEGE PGPPGDPGLT ECDVMTYVRE
TCGCCDCEKR CGALDVVFVI DSSESIGYTN FTLEKNFVIN VVNRLGAIAK DPKSETGTRV
GVVQYSHEGT FEAIQLDDER IDSLSSFKEA VKNLEWIAGG TWTPSALKFA YDRLIKESRR
QKTRVFAVVI TDGRHDPRDD DLNLRALCDR DVTVTAIGIG DMFHEKHESE NLYSIACDKP
QQVRNMTLFS DLVAEKFIDD MEDVLCPDPQ IVCPDLPCQT ELSVAQCTQR PVDIVFLLDG
SERLGEQNFH KARRFVEQVA RRLTLARRDD DPLNARVALL QFGGPGEQQV AFPLSHNLTA
IHEALETTQY LNSFSHVGAG VVHAINAIVR SPRGGARRHA ELSFVFLTDG VTGNDSLHES
AHSMRKQNVV PTVLALGSDV DMDVLTTLSL GDRAAVFHEK DYDSLAQPGF FDRFIRWIC
