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Collagen alpha-2(VI) chain

 CO6A2_HUMAN             Reviewed;        1019 AA.
P12110; Q13909; Q13910; Q13911; Q14048; Q14049; Q16259; Q16597;
Q6P0Q1; Q9UML3; Q9Y4S8;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
06-FEB-2007, sequence version 4.
27-SEP-2017, entry version 198.
RecName: Full=Collagen alpha-2(VI) chain;
Flags: Precursor;
Name=COL6A2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2C2), SEQUENCE REVISION, AND
VARIANTS ASN-227; ASN-399 AND HIS-680.
TISSUE=Fibroblast, and Placenta;
Chu M.-L.;
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2C2), AND VARIANT
ASN-399.
TISSUE=Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-266, AND ALTERNATIVE SPLICING.
PubMed=1556127;
Saitta B., Timpl R., Chu M.-L.;
"Human alpha 2(VI) collagen gene. Heterogeneity at the 5'-untranslated
region generated by an alternate exon.";
J. Biol. Chem. 267:6188-6196(1992).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-255 AND 591-1019, AND NUCLEOTIDE
SEQUENCE [MRNA] OF 821-1019 (ISOFORM 2C2A).
TISSUE=Fibroblast, and Placenta;
PubMed=2551668;
Chu M.-L., Pan T.-C., Conway D., Kuo H.J., Glanville R.W., Timpl R.,
Mann K., Deutzmann R.;
"Sequence analysis of alpha 1(VI) and alpha 2(VI) chains of human type
VI collagen reveals internal triplication of globular domains similar
to the A domains of von Willebrand factor and two alpha 2(VI) chain
variants that differ in the carboxy terminus.";
EMBO J. 8:1939-1946(1989).
[5]
PROTEIN SEQUENCE OF 179-185 AND 581-594.
PubMed=8168508; DOI=10.1111/j.1432-1033.1994.tb18727.x;
Tillet E., Wiedemann H., Golbik R., Pan T.-C., Zhang R.Z., Mann K.,
Chu M.-L., Timpl R.;
"Recombinant expression and structural and binding properties of alpha
1(VI) and alpha 2(VI) chains of human collagen type VI.";
Eur. J. Biochem. 221:177-185(1994).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 238-299.
PubMed=3665927; DOI=10.1111/j.1432-1033.1987.tb13422.x;
Chu M.-L., Mann K., Deutzmann R., Pribula-Conway D., Hsu-Chen C.-C.,
Bernard M.P., Timpl R.;
"Characterization of three constituent chains of collagen type VI by
peptide sequences and cDNA clones.";
Eur. J. Biochem. 168:309-317(1987).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 246-590, AND VARIANT ASN-399.
PubMed=1765372; DOI=10.1016/0888-7543(91)90111-Q;
Saitta B., Wang Y.-M., Renkart L., Zhang R.-Z., Pan T.-C., Timpl R.,
Chu M.-L.;
"The exon organization of the triple-helical coding regions of the
human alpha 1(VI) and alpha 2(VI) collagen genes is highly similar.";
Genomics 11:145-153(1991).
[8]
PROTEIN SEQUENCE OF 251-264.
PubMed=6852033; DOI=10.1111/j.1432-1033.1983.tb07427.x;
Jander R., Rauterberg J., Glanville R.W.;
"Further characterization of the three polypeptide chains of bovine
and human short-chain collagen (intima collagen).";
Eur. J. Biochem. 133:39-46(1983).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 256-590.
PubMed=3198591;
Chu M.-L., Conway D., Pan T.-C., Baldwin C., Mann K., Deutzmann R.,
Timpl R.;
"Amino acid sequence of the triple-helical domain of human collagen
type VI.";
J. Biol. Chem. 263:18601-18606(1988).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 316-359.
TISSUE=Placenta;
PubMed=3348212;
Weil D., Mattei M.-G., Passage E., N'Guyen V.C., Pribula-Conway D.,
Mann K., Deutzmann R., Timpl R., Chu M.-L.;
"Cloning and chromosomal localization of human genes encoding the
three chains of type VI collagen.";
Am. J. Hum. Genet. 42:435-445(1988).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 591-1019, ALTERNATIVE SPLICING, AND
VARIANT HIS-680.
PubMed=1690728;
Saitta B., Stokes D.G., Vissing H., Timpl R., Chu M.-L.;
"Alternative splicing of the human alpha 2(VI) collagen gene generates
multiple mRNA transcripts which predict three protein variants with
distinct carboxyl termini.";
J. Biol. Chem. 265:6473-6480(1990).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 820-1019 (ISOFORM 2C2).
TISSUE=Uterus;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[13]
SUBCELLULAR LOCATION.
PubMed=8305732; DOI=10.1091/mbc.4.11.1097;
Nishiyama A., Stallcup W.B.;
"Expression of NG2 proteoglycan causes retention of type VI collagen
on the cell surface.";
Mol. Biol. Cell 4:1097-1108(1993).
[14]
INTERACTION WITH CSPG4.
PubMed=9099729; DOI=10.1074/jbc.272.16.10769;
Tillet E., Ruggiero F., Nishiyama A., Stallcup W.B.;
"The membrane-spanning proteoglycan NG2 binds to collagens V and VI
through the central nonglobular domain of its core protein.";
J. Biol. Chem. 272:10769-10776(1997).
[15]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-140; ASN-785; ASN-897 AND
ASN-954.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-701, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-705, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
VARIANT BTHLM1 SER-271.
PubMed=8782832; DOI=10.1038/ng0996-113;
Joebsis G.J., Keizers H., Vreijling J.P., de Visser M., Speer M.C.,
Wolterman R.A., Baas F., Bohlhuis P.A.;
"Type VI collagen mutations in Bethlem myopathy, an autosomal dominant
myopathy with contractures.";
Nat. Genet. 14:113-115(1996).
[20]
VARIANT BTHLM1 ASN-621.
PubMed=11865138; DOI=10.1212/WNL.58.4.593;
Scacheri P.C., Gillanders E.M., Subramony S.H., Vedanarayanan V.,
Crowe C.A., Thakore N., Bingler M., Hoffman E.P.;
"Novel mutations in collagen VI genes: expansion of the Bethlem
myopathy phenotype.";
Neurology 58:593-602(2002).
[21]
VARIANTS UCMD1 PRO-837 AND ASN-897 DEL, CHARACTERIZATION OF VARIANTS
UCMD1 PRO-837 AND ASN-897 DEL, AND VARIANTS ASN-227; ASN-399 AND
HIS-680.
PubMed=15563506; DOI=10.1093/hmg/ddi025;
Baker N.L., Moergelin M., Peat R., Goemans N., North K.N.,
Bateman J.F., Lamande S.R.;
"Dominant collagen VI mutations are a common cause of Ullrich
congenital muscular dystrophy.";
Hum. Mol. Genet. 14:279-293(2005).
[22]
VARIANTS BTHLM1 SER-700 AND ARG-777, VARIANTS UCMD1 ARG-283; HIS-498;
ARG-531; ARG-777; HIS-784 AND SER-876, AND VARIANTS LYS-106; ASN-227;
ASN-399; GLN-489; SER-518; HIS-680; CYS-724; GLY-804; GLN-853 AND
ARG-935.
PubMed=15689448; DOI=10.1136/jmg.2004.023754;
Lampe A.K., Dunn D.M., von Niederhausern A.C., Hamil C., Aoyagi A.,
Laval S.H., Marie S.K., Chu M.-L., Swoboda K., Muntoni F.,
Bonnemann C.G., Flanigan K.M., Bushby K.M.D., Weiss R.B.;
"Automated genomic sequence analysis of the three collagen VI genes:
applications to Ullrich congenital muscular dystrophy and Bethlem
myopathy.";
J. Med. Genet. 42:108-120(2005).
[23]
VARIANT BTHLM1 LEU-932, AND VARIANTS ASN-227; ASN-399; HIS-680 AND
ARG-895.
PubMed=17886299; DOI=10.1002/ana.21213;
Baker N.L., Moergelin M., Pace R.A., Peat R.A., Adams N.E.,
Gardner R.J., Rowland L.P., Miller G., De Jonghe P., Ceulemans B.,
Hannibal M.C., Edwards M., Thompson E.M., Jacobson R.,
Quinlivan R.C.M., Aftimos S., Kornberg A.J., North K.N., Bateman J.F.,
Lamande S.R.;
"Molecular consequences of dominant Bethlem myopathy collagen VI
mutations.";
Ann. Neurol. 62:390-405(2007).
[24]
INVOLVEMENT IN MYOSCLEROSIS.
PubMed=18852439; DOI=10.1212/01.wnl.0000327611.01687.5e;
Merlini L., Martoni E., Grumati P., Sabatelli P., Squarzoni S.,
Urciuolo A., Ferlini A., Gualandi F., Bonaldo P.;
"Autosomal recessive myosclerosis myopathy is a collagen VI
disorder.";
Neurology 71:1245-1253(2008).
[25]
VARIANTS LYS-106; CYS-377; ASN-446; MET-728; GLN-843; GLN-853 AND
CYS-1010.
PubMed=23040494; DOI=10.1016/j.ajhg.2012.08.017;
Ackerman C., Locke A.E., Feingold E., Reshey B., Espana K.,
Thusberg J., Mooney S., Bean L.J., Dooley K.J., Cua C.L., Reeves R.H.,
Sherman S.L., Maslen C.L.;
"An excess of deleterious variants in VEGF-A pathway genes in Down-
syndrome-associated atrioventricular septal defects.";
Am. J. Hum. Genet. 91:646-659(2012).
[26]
VARIANT GLN-853.
PubMed=27535533; DOI=10.1038/nature19057;
Exome Aggregation Consortium;
Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E.,
Fennell T., O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B.,
Tukiainen T., Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K.,
Zhao F., Zou J., Pierce-Hoffman E., Berghout J., Cooper D.N.,
Deflaux N., DePristo M., Do R., Flannick J., Fromer M., Gauthier L.,
Goldstein J., Gupta N., Howrigan D., Kiezun A., Kurki M.I.,
Moonshine A.L., Natarajan P., Orozco L., Peloso G.M., Poplin R.,
Rivas M.A., Ruano-Rubio V., Rose S.A., Ruderfer D.M., Shakir K.,
Stenson P.D., Stevens C., Thomas B.P., Tiao G., Tusie-Luna M.T.,
Weisburd B., Won H.H., Yu D., Altshuler D.M., Ardissino D.,
Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S.,
Laakso M., McCarroll S., McCarthy M.I., McGovern D., McPherson R.,
Neale B.M., Palotie A., Purcell S.M., Saleheen D., Scharf J.M.,
Sklar P., Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C.,
Wilson J.G., Daly M.J., MacArthur D.G.;
"Analysis of protein-coding genetic variation in 60,706 humans.";
Nature 536:285-291(2016).
-!- FUNCTION: Collagen VI acts as a cell-binding protein.
-!- SUBUNIT: Trimers composed of three different chains: alpha-1(VI),
alpha-2(VI), and alpha-3(VI) or alpha-5(VI) or alpha-6(VI).
Interacts with CSPG4. {ECO:0000269|PubMed:9099729}.
-!- INTERACTION:
Q9NRI5:DISC1; NbExp=3; IntAct=EBI-928749, EBI-529989;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000269|PubMed:8305732}. Membrane
{ECO:0000269|PubMed:8305732}; Peripheral membrane protein
{ECO:0000269|PubMed:8305732}. Note=Recruited on membranes by
CSPG4.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=2C2;
IsoId=P12110-1; Sequence=Displayed;
Name=2C2A;
IsoId=P12110-2; Sequence=VSP_001163, VSP_001164;
Name=2C2A';
IsoId=P12110-3; Sequence=VSP_001161, VSP_001162;
-!- PTM: Prolines at the third position of the tripeptide repeating
unit (G-X-Y) are hydroxylated in some or all of the chains.
-!- DISEASE: Bethlem myopathy 1 (BTHLM1) [MIM:158810]: A benign
proximal myopathy characterized by early childhood onset and joint
contractures most frequently affecting the elbows and ankles.
{ECO:0000269|PubMed:11865138, ECO:0000269|PubMed:15689448,
ECO:0000269|PubMed:17886299, ECO:0000269|PubMed:8782832}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Ullrich congenital muscular dystrophy 1 (UCMD1)
[MIM:254090]: A congenital myopathy characterized by muscle
weakness and multiple joint contractures, generally noted at birth
or early infancy. The clinical course is more severe than in
Bethlem myopathy. {ECO:0000269|PubMed:15563506,
ECO:0000269|PubMed:15689448}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Myosclerosis autosomal recessive (MYOSAR) [MIM:255600]: A
condition characterized by chronic inflammation of skeletal muscle
with hyperplasia of the interstitial connective tissue. The
clinical picture includes slender muscles with firm 'woody'
consistency and restriction of movement of many joints because of
muscle contractures. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the type VI collagen family. {ECO:0000305}.
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EMBL; AY029208; AAA52056.2; -; mRNA.
EMBL; BC065509; AAH65509.1; -; mRNA.
EMBL; M81835; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X15977; CAA34099.1; -; mRNA.
EMBL; X06195; CAA29556.1; -; mRNA.
EMBL; S75462; AAB20836.1; -; Genomic_DNA.
EMBL; S75425; AAB20836.1; JOINED; Genomic_DNA.
EMBL; S75428; AAB20836.1; JOINED; Genomic_DNA.
EMBL; S75430; AAB20836.1; JOINED; Genomic_DNA.
EMBL; S75432; AAB20836.1; JOINED; Genomic_DNA.
EMBL; S75434; AAB20836.1; JOINED; Genomic_DNA.
EMBL; S75436; AAB20836.1; JOINED; Genomic_DNA.
EMBL; S75438; AAB20836.1; JOINED; Genomic_DNA.
EMBL; S75440; AAB20836.1; JOINED; Genomic_DNA.
EMBL; S75442; AAB20836.1; JOINED; Genomic_DNA.
EMBL; S75444; AAB20836.1; JOINED; Genomic_DNA.
EMBL; S75446; AAB20836.1; JOINED; Genomic_DNA.
EMBL; S75448; AAB20836.1; JOINED; Genomic_DNA.
EMBL; S75450; AAB20836.1; JOINED; Genomic_DNA.
EMBL; S75452; AAB20836.1; JOINED; Genomic_DNA.
EMBL; S75454; AAB20836.1; JOINED; Genomic_DNA.
EMBL; S75456; AAB20836.1; JOINED; Genomic_DNA.
EMBL; S75458; AAB20836.1; JOINED; Genomic_DNA.
EMBL; S75460; AAB20836.1; JOINED; Genomic_DNA.
EMBL; M34572; AAA35618.1; -; mRNA.
EMBL; M34571; AAA35618.1; JOINED; mRNA.
EMBL; M34572; AAA35619.1; -; mRNA.
EMBL; M34571; AAA35619.1; JOINED; mRNA.
EMBL; M34573; AAA35620.1; -; mRNA.
EMBL; M34571; AAA35620.1; JOINED; mRNA.
EMBL; M34570; AAA35621.1; -; mRNA.
EMBL; AL096746; CAB46421.2; -; mRNA.
CCDS; CCDS13728.1; -. [P12110-1]
CCDS; CCDS13729.1; -. [P12110-2]
CCDS; CCDS13730.1; -. [P12110-3]
PIR; S05378; CGHU2A.
PIR; S09646; S09646.
PIR; T12549; T12549.
RefSeq; NP_001840.3; NM_001849.3. [P12110-1]
RefSeq; NP_478054.2; NM_058174.2. [P12110-2]
RefSeq; NP_478055.2; NM_058175.2. [P12110-3]
RefSeq; XP_011527753.1; XM_011529451.1. [P12110-1]
UniGene; Hs.420269; -.
ProteinModelPortal; P12110; -.
SMR; P12110; -.
BioGrid; 107689; 37.
IntAct; P12110; 6.
STRING; 9606.ENSP00000300527; -.
ChEMBL; CHEMBL2364188; -.
iPTMnet; P12110; -.
PhosphoSitePlus; P12110; -.
BioMuta; COL6A2; -.
DMDM; 125987812; -.
REPRODUCTION-2DPAGE; P12110; -.
EPD; P12110; -.
MaxQB; P12110; -.
PaxDb; P12110; -.
PeptideAtlas; P12110; -.
PRIDE; P12110; -.
TopDownProteomics; P12110-3; -. [P12110-3]
DNASU; 1292; -.
Ensembl; ENST00000300527; ENSP00000300527; ENSG00000142173. [P12110-1]
Ensembl; ENST00000310645; ENSP00000312529; ENSG00000142173. [P12110-3]
Ensembl; ENST00000397763; ENSP00000380870; ENSG00000142173. [P12110-2]
Ensembl; ENST00000409416; ENSP00000387115; ENSG00000142173. [P12110-3]
GeneID; 1292; -.
KEGG; hsa:1292; -.
UCSC; uc002zhy.1; human. [P12110-1]
CTD; 1292; -.
DisGeNET; 1292; -.
EuPathDB; HostDB:ENSG00000142173.14; -.
GeneCards; COL6A2; -.
GeneReviews; COL6A2; -.
H-InvDB; HIX0016186; -.
HGNC; HGNC:2212; COL6A2.
HPA; HPA007029; -.
HPA; HPA030920; -.
HPA; HPA038799; -.
MalaCards; COL6A2; -.
MIM; 120240; gene.
MIM; 158810; phenotype.
MIM; 254090; phenotype.
MIM; 255600; phenotype.
neXtProt; NX_P12110; -.
OpenTargets; ENSG00000142173; -.
Orphanet; 610; Bethlem myopathy.
Orphanet; 75840; Congenital muscular dystrophy, Ullrich type.
Orphanet; 289380; Myosclerosis.
PharmGKB; PA26728; -.
eggNOG; ENOG410IS7F; Eukaryota.
eggNOG; ENOG410XT53; LUCA.
GeneTree; ENSGT00820000126981; -.
HOVERGEN; HBG051051; -.
InParanoid; P12110; -.
KO; K06238; -.
OMA; RALCNHD; -.
OrthoDB; EOG091G020V; -.
PhylomeDB; P12110; -.
TreeFam; TF331207; -.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
Reactome; R-HSA-186797; Signaling by PDGF.
Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-3000178; ECM proteoglycans.
Reactome; R-HSA-419037; NCAM1 interactions.
Reactome; R-HSA-8948216; Collagen chain trimerization.
ChiTaRS; COL6A2; human.
GeneWiki; COL6A2; -.
GenomeRNAi; 1292; -.
PMAP-CutDB; P12110; -.
PRO; PR:P12110; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000142173; -.
ExpressionAtlas; P12110; baseline and differential.
Genevisible; P12110; HS.
GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IDA:MGI.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:1903561; C:extracellular vesicle; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IPI:MGI.
GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0070208; P:protein heterotrimerization; IPI:MGI.
GO; GO:0009749; P:response to glucose; IEA:Ensembl.
Gene3D; 3.40.50.410; -; 3.
InterPro; IPR008160; Collagen.
InterPro; IPR002035; VWF_A.
Pfam; PF01391; Collagen; 4.
Pfam; PF00092; VWA; 3.
SMART; SM00327; VWA; 3.
SUPFAM; SSF53300; SSF53300; 3.
PROSITE; PS50234; VWFA; 3.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Collagen; Complete proteome;
Congenital muscular dystrophy; Direct protein sequencing;
Disease mutation; Extracellular matrix; Glycoprotein; Hydroxylation;
Membrane; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Secreted; Signal.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 1019 Collagen alpha-2(VI) chain.
/FTId=PRO_0000005832.
DOMAIN 46 234 VWFA 1. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
DOMAIN 615 805 VWFA 2. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
DOMAIN 833 1014 VWFA 3. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
REGION 21 256 Nonhelical region.
REGION 257 590 Triple-helical region.
REGION 591 1019 Nonhelical region.
MOTIF 366 368 Cell attachment site. {ECO:0000255}.
MOTIF 426 428 Cell attachment site. {ECO:0000255}.
MOTIF 489 491 Cell attachment site. {ECO:0000255}.
MOTIF 498 500 Cell attachment site. {ECO:0000255}.
MOTIF 539 541 Cell attachment site. {ECO:0000255}.
MOD_RES 701 701 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 705 705 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
CARBOHYD 140 140 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 327 327 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 630 630 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 785 785 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 897 897 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 954 954 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
VAR_SEQ 821 991 ELSVAQCTQRPVDIVFLLDGSERLGEQNFHKARRFVEQVAR
RLTLARRDDDPLNARVALLQFGGPGEQQVAFPLSHNLTAIH
EALETTQYLNSFSHVGAGVVHAINAIVRSPRGGARRHAELS
FVFLTDGVTGNDSLHESAHSMRKQNVVPTVLALGSDVDMDV
LTTLSLG -> DAPWPGGEPPVTFLRTEEGPDATFPRTIPL
IQQLLNATELTQDPAAYSQLVAVLVYTAERAKFATGVERQD
WMELFIDTFKLVHRDIVGDPETALALC (in isoform
2C2A). {ECO:0000303|PubMed:2551668}.
/FTId=VSP_001163.
VAR_SEQ 821 828 ELSVAQCT -> GLDGAVLC (in isoform 2C2A').
{ECO:0000305}.
/FTId=VSP_001161.
VAR_SEQ 829 1019 Missing (in isoform 2C2A').
{ECO:0000305}.
/FTId=VSP_001162.
VAR_SEQ 992 1019 Missing (in isoform 2C2A).
{ECO:0000303|PubMed:2551668}.
/FTId=VSP_001164.
VARIANT 106 106 E -> K (in dbSNP:rs141703710).
{ECO:0000269|PubMed:15689448,
ECO:0000269|PubMed:23040494}.
/FTId=VAR_058225.
VARIANT 227 227 D -> N (in dbSNP:rs35881321).
{ECO:0000269|PubMed:15563506,
ECO:0000269|PubMed:15689448,
ECO:0000269|PubMed:17886299,
ECO:0000269|Ref.1}.
/FTId=VAR_048801.
VARIANT 271 271 G -> S (in BTHLM1; dbSNP:rs121912940).
{ECO:0000269|PubMed:8782832}.
/FTId=VAR_013589.
VARIANT 283 283 G -> R (in UCMD1; dbSNP:rs267606748).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_058226.
VARIANT 377 377 R -> C (in dbSNP:rs144801620).
{ECO:0000269|PubMed:23040494}.
/FTId=VAR_076959.
VARIANT 399 399 S -> N (in dbSNP:rs2839110).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:15563506,
ECO:0000269|PubMed:15689448,
ECO:0000269|PubMed:1765372,
ECO:0000269|PubMed:17886299,
ECO:0000269|Ref.1}.
/FTId=VAR_030315.
VARIANT 446 446 D -> N (in dbSNP:rs535007570).
{ECO:0000269|PubMed:23040494}.
/FTId=VAR_076960.
VARIANT 489 489 R -> Q (in dbSNP:rs61735828).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_058227.
VARIANT 498 498 R -> H (in UCMD1; dbSNP:rs267606749).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_058228.
VARIANT 518 518 P -> S (in dbSNP:rs141166141).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_058229.
VARIANT 531 531 G -> R (in UCMD1).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_058230.
VARIANT 621 621 D -> N (in BTHLM1; dbSNP:rs267606750).
{ECO:0000269|PubMed:11865138}.
/FTId=VAR_013590.
VARIANT 680 680 R -> H (in dbSNP:rs1042917).
{ECO:0000269|PubMed:15563506,
ECO:0000269|PubMed:15689448,
ECO:0000269|PubMed:1690728,
ECO:0000269|PubMed:17886299,
ECO:0000269|Ref.1}.
/FTId=VAR_030316.
VARIANT 700 700 G -> S (in BTHLM1; dbSNP:rs794727418).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_058231.
VARIANT 724 724 R -> C (in dbSNP:rs150098077).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_058232.
VARIANT 728 728 V -> M (in dbSNP:rs200585528).
{ECO:0000269|PubMed:23040494}.
/FTId=VAR_076961.
VARIANT 777 777 C -> R (in BTHLM1; dbSNP:rs267606747).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_058233.
VARIANT 784 784 R -> H (in UCMD1; dbSNP:rs75120695).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_058234.
VARIANT 804 804 V -> G (in dbSNP:rs779847082).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_058235.
VARIANT 837 837 L -> P (in UCMD1; prevents collagen VI
assembly). {ECO:0000269|PubMed:15563506}.
/FTId=VAR_058236.
VARIANT 843 843 R -> Q (in dbSNP:rs201736323).
{ECO:0000269|PubMed:23040494}.
/FTId=VAR_076962.
VARIANT 853 853 R -> Q (in dbSNP:rs144830948).
{ECO:0000269|PubMed:15689448,
ECO:0000269|PubMed:23040494,
ECO:0000269|PubMed:27535533}.
/FTId=VAR_058237.
VARIANT 876 876 R -> S (in UCMD1; dbSNP:rs387906608).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_058238.
VARIANT 895 895 S -> R (in dbSNP:rs141233891).
{ECO:0000269|PubMed:17886299}.
/FTId=VAR_058239.
VARIANT 897 897 Missing (in UCMD1; results in severe
collagen VI matrix deficiencies).
{ECO:0000269|PubMed:15563506}.
/FTId=VAR_058240.
VARIANT 932 932 P -> L (in BTHLM1; results in reduced
intracellular collagen VI assembly and
secretion; dbSNP:rs117725825).
{ECO:0000269|PubMed:17886299}.
/FTId=VAR_058241.
VARIANT 935 935 G -> R (in dbSNP:rs35548026).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_048802.
VARIANT 1010 1010 F -> C. {ECO:0000269|PubMed:23040494}.
/FTId=VAR_076963.
VARIANT 1015 1015 I -> L (in dbSNP:rs11910483).
/FTId=VAR_048803.
CONFLICT 507 507 K -> S (in Ref. 7; AAB20836).
{ECO:0000305}.
CONFLICT 966 967 KQ -> NE (in Ref. 1; AAA52056 and 11;
AAA35620). {ECO:0000305}.
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


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