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 02-OCT-2024, entry version 245. 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 BTHLM1B 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 BTHLM1B 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 UCMD1B PRO-837 AND ASN-897 DEL, CHARACTERIZATION OF VARIANTS RP UCMD1B 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 BTHLM1B SER-700 AND ARG-777, VARIANTS UCMD1B 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 BTHLM1B LEU-932, AND VARIANTS ASN-227; ASN-399; HIS-680 AND RP 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 1B (BTHLM1B) [MIM:620725]: A form of Bethlem CC myopathy, a slowly progressive muscular dystrophy characterized by CC joint contractures, most frequently affecting the elbows and ankles, CC and muscle weakness and wasting involving the proximal and extensor CC muscles more than the distal and flexor ones. The clinical onset more CC often occurs in childhood or adulthood, but it can be prenatal with CC decreased fetal movements or neonatal with hypotonia. The hallmark of CC Bethlem myopathy is long finger flexion contractures. Inheritance can CC be autosomal dominant or autosomal recessive. 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 1B (UCMD1B) CC [MIM:620727]: A form of Ullrich congenital muscular dystrophy, a CC disease characterized by generalized muscle weakness and striking CC hypermobility of distal joints in conjunction with variable CC contractures of more proximal joints and normal intelligence. CC Additional findings may include kyphoscoliosis, protruded calcanei, and CC follicular hyperkeratosis (rough skin). More severely affected patients CC manifest at birth and never achieve independent ambulation, while CC patients with milder phenotypes might maintain ambulation into CC adulthood. Inheritance can be autosomal dominant or autosomal CC recessive. {ECO:0000269|PubMed:15563506, ECO:0000269|PubMed:15689448}. CC Note=The disease is caused by variants affecting the gene represented CC in this 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}. 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; 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. DR AlphaFoldDB; P12110; -. DR SMR; P12110; -. DR BioGRID; 107689; 130. DR ComplexPortal; CPX-1736; Collagen type VI trimer. DR IntAct; P12110; 81. DR MINT; P12110; -. DR STRING; 9606.ENSP00000300527; -. DR ChEMBL; CHEMBL2364188; -. DR GlyConnect; 1137; 52 N-Linked glycans (4 sites). DR GlyCosmos; P12110; 9 sites, 67 glycans. DR GlyGen; P12110; 9 sites, 65 N-linked glycans (4 sites), 2 O-linked glycans (3 sites). DR iPTMnet; P12110; -. DR PhosphoSitePlus; P12110; -. DR SwissPalm; P12110; -. DR BioMuta; COL6A2; -. DR DMDM; 125987812; -. DR REPRODUCTION-2DPAGE; P12110; -. DR jPOST; P12110; -. DR MassIVE; P12110; -. DR PaxDb; 9606-ENSP00000300527; -. DR PeptideAtlas; P12110; -. DR ProteomicsDB; 52830; -. [P12110-1] DR ProteomicsDB; 52831; -. [P12110-2] DR ProteomicsDB; 52832; -. [P12110-3] DR Pumba; P12110; -. DR TopDownProteomics; P12110-3; -. [P12110-3] DR Antibodypedia; 1646; 265 antibodies from 31 providers. DR DNASU; 1292; -. DR Ensembl; ENST00000300527.9; ENSP00000300527.4; ENSG00000142173.17. [P12110-1] DR Ensembl; ENST00000397763.6; ENSP00000380870.1; ENSG00000142173.17. [P12110-2] DR Ensembl; ENST00000409416.6; ENSP00000387115.1; ENSG00000142173.17. [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 AGR; HGNC:2212; -. 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; 255600; phenotype. DR MIM; 620725; phenotype. DR MIM; 620727; phenotype. DR neXtProt; NX_P12110; -. DR OpenTargets; ENSG00000142173; -. DR Orphanet; 610; Bethlem muscular dystrophy. DR Orphanet; 646098; Collagen VI-related congenital muscular dystrophy. DR Orphanet; 646113; Intermediate collagen VI-related muscular dystrophy. DR Orphanet; 289380; Myosclerosis. DR Orphanet; 75840; Ullrich congenital muscular dystrophy. 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; MEHELCP; -. DR OrthoDB; 2906665at2759; -. 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 1146 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 179 other cell types or tissues. DR ExpressionAtlas; P12110; baseline and differential. 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:0051402; P:neuron apoptotic process; IEA:Ensembl. DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl. DR GO; GO:0009749; P:response to glucose; IEA:Ensembl. DR GO; GO:0009411; P:response to UV; IEA:Ensembl. DR CDD; cd01480; vWA_collagen_alpha_1-VI-type; 2. DR CDD; cd00198; vWFA; 1. DR Gene3D; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1. DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 3. DR InterPro; IPR008160; Collagen. DR InterPro; IPR050525; ECM_Assembly_Org. DR InterPro; IPR002035; VWF_A. DR InterPro; IPR036465; vWFA_dom_sf. DR PANTHER; PTHR24020; COLLAGEN ALPHA; 1. DR PANTHER; PTHR24020:SF70; PH DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF01391; Collagen; 4. DR Pfam; PF00092; VWA; 3. DR PRINTS; PR00453; VWFADOMAIN. DR SMART; SM00327; VWA; 3. DR SUPFAM; SSF53300; vWA-like; 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; Membrane; KW Phosphoprotein; Proteomics identification; Reference proteome; Repeat; KW 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 BTHLM1B; dbSNP:rs121912940)" FT /evidence="ECO:0000269|PubMed:8782832" FT /id="VAR_013589" FT VARIANT 283 FT /note="G -> R (in UCMD1B; 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 UCMD1B; 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 UCMD1B)" FT /evidence="ECO:0000269|PubMed:15689448" FT /id="VAR_058230" FT VARIANT 621 FT /note="D -> N (in BTHLM1B; 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 BTHLM1B; 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 BTHLM1B; 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 UCMD1B; 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 UCMD1B; 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 UCMD1B; results in severe collagen VI FT matrix deficiencies; dbSNP:rs2078769555)" FT /evidence="ECO:0000269|PubMed:15563506" FT /id="VAR_058240" FT VARIANT 932 FT /note="P -> L (in BTHLM1B; 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 //