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Collagen alpha-3(VI) chain

 CO6A3_HUMAN             Reviewed;        3177 AA.
P12111; A8MT30; B4E3U5; B7ZMJ7; E9PFQ6; E9PGQ9; Q16501; Q53QF4;
Q53QF6;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
02-NOV-2010, sequence version 5.
27-SEP-2017, entry version 206.
RecName: Full=Collagen alpha-3(VI) chain;
Flags: Precursor;
Name=COL6A3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, HYDROXYLATION,
AND VARIANTS VAL-2431; THR-2927; VAL-2988 AND PRO-3012.
TISSUE=Fibroblast;
PubMed=1689238;
Chu M.-L., Zhang R.-Z., Pan T.-C., Stokes D., Conway D., Kuo H.-J.,
Glanville R., Mayer U., Mann K., Deutzmann R., Timpl R.;
"Mosaic structure of globular domains in the human type VI collagen
alpha 3 chain: similarity to von Willebrand factor, fibronectin,
actin, salivary proteins and aprotinin type protease inhibitors.";
EMBO J. 9:385-393(1990).
[2]
SEQUENCE REVISION.
Chu M.-L.;
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
TISSUE=Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 32-236, AND ALTERNATIVE SPLICING.
PubMed=1339440;
Zanussi S., Doliana R., Segat D., Bonaldo P., Colombatti A.;
"The human type VI collagen gene. mRNA and protein variants of the
alpha 3 chain generated by alternative splicing of an additional 5-end
exon.";
J. Biol. Chem. 267:24082-24089(1992).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 2038-2373.
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 2092-2157.
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).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 2092-2151.
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).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2677.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2079 AND ASN-2677.
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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-433, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1225, 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).
[14]
INVOLVEMENT IN DYT27, AND VARIANTS DYT27 HIS-2501; THR-2554; HIS-3043
AND ARG-3082.
PubMed=26004199; DOI=10.1016/j.ajhg.2015.04.010;
Zech M., Lam D.D., Francescatto L., Schormair B., Salminen A.V.,
Jochim A., Wieland T., Lichtner P., Peters A., Gieger C.,
Lochmueller H., Strom T.M., Haslinger B., Katsanis N., Winkelmann J.;
"Recessive mutations in the alpha3 (VI) collagen gene COL6A3 cause
early-onset isolated dystonia.";
Am. J. Hum. Genet. 96:883-893(2015).
[15]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 3108-3165.
PubMed=7533217; DOI=10.1016/S0022-2836(05)80110-X;
Arnoux B., Merigeau K., Saludjian P., Norris F., Norris K., Bjoern S.,
Olsen O., Petersen L., Ducruix A.;
"The 1.6 A structure of Kunitz-type domain from the alpha 3 chain of
human type VI collagen.";
J. Mol. Biol. 246:609-617(1995).
[16]
STRUCTURE BY NMR OF 3103-3165.
PubMed=8805527; DOI=10.1016/S0969-2126(96)00022-6;
Zweckstetter M., Czisch M., Mayer U., Chu M.-L., Zinth W., Timpl R.,
Holak T.A.;
"Structure and multiple conformations of the Kunitz-type domain from
human type VI collagen alpha3(VI) chain in solution.";
Structure 4:195-209(1996).
[17]
STRUCTURE BY NMR OF 3108-3165.
PubMed=9265624; DOI=10.1021/bi9705570;
Soerensen M.D., Bjoern S., Norris K., Olsen O., Petersen L.,
James T.L., Led J.J.;
"Solution structure and backbone dynamics of the human alpha3-chain
type VI collagen C-terminal Kunitz domain.";
Biochemistry 36:10439-10450(1997).
[18]
DISEASE.
PubMed=11992252; DOI=10.1086/340608;
Demir E., Sabatelli P., Allamand V., Ferreiro A., Moghadaszadeh B.,
Makrelouf M., Topaloglu H., Echenne B., Merlini L., Guicheney P.;
"Mutations in COL6A3 cause severe and mild phenotypes of Ullrich
congenital muscular dystrophy.";
Am. J. Hum. Genet. 70:1446-1458(2002).
[19]
VARIANT BTHLM1 GLU-1679, AND VARIANT HIS-2831.
PubMed=9536084; DOI=10.1093/hmg/7.5.807;
Pan T.-C., Zhang R.-Z., Pericak-Vance M.A., Tandan R., Fries T.,
Stajich J.M., Viles K., Vance J.M., Chu M.-L., Speer M.C.;
"Missense mutation in a von Willebrand factor type A domain of the
alpha 3(VI) collagen gene (COL6A3) in a family with Bethlem
myopathy.";
Hum. Mol. Genet. 7:807-812(1998).
[20]
VARIANT BTHLM1 ARG-2056.
PubMed=10399756; DOI=10.1016/S0960-8966(99)00014-0;
Pepe G., Bertini E., Giusti B., Brunelli T., Comeglio P., Saitta B.,
Merlini L., Chu M.L., Federici G., Abbate R.;
"A novel de novo mutation in the triple helix of the COL6A3 gene in a
two-generation Italian family affected by Bethlem myopathy. A
diagnostic approach in the mutations' screening of type VI collagen.";
Neuromuscul. Disord. 9:264-271(1999).
[21]
VARIANTS BTHLM1 HIS-677; GLU-1014; LYS-1386; ASP-1467; GLU-1679;
MET-1985; ASP-2047; ASP-2080 AND VAL-2941, VARIANTS UCMD1 GLN-1064;
GLN-1395 AND ASN-1674, AND VARIANTS VAL-411; HIS-491; SER-492;
THR-807; SER-830; GLN-1088; GLN-1576; GLN-1632; SER-1687; LEU-2218 AND
HIS-2831.
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).
[22]
VARIANT BTHLM1 ARG-1726, AND VARIANTS HIS-677; GLN-1576; VAL-2431;
LYS-2453; HIS-2831; VAL-2988 AND ILE-3069.
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).
-!- 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).
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=P12111-1; Sequence=Displayed;
Name=2;
IsoId=P12111-2; Sequence=VSP_001172;
Name=3;
IsoId=P12111-3; Sequence=VSP_001172, VSP_043434, VSP_043435,
VSP_043436;
Note=No experimental confirmation available.;
Name=4;
IsoId=P12111-4; Sequence=VSP_045718, VSP_045719;
Name=5;
IsoId=P12111-5; Sequence=VSP_001172, VSP_043435, VSP_043436;
-!- PTM: Prolines at the third position of the tripeptide repeating
unit (G-X-Y) are hydroxylated in some or all of the chains.
{ECO:0000269|PubMed:1689238}.
-!- PTM: The N-terminus is blocked.
-!- 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:10399756, ECO:0000269|PubMed:15689448,
ECO:0000269|PubMed:17886299, ECO:0000269|PubMed:9536084}. 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:15689448}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- DISEASE: Dystonia 27 (DYT27) [MIM:616411]: A form of dystonia, a
disorder defined by the presence of sustained involuntary muscle
contraction, often leading to abnormal postures. DYT27 is an
autosomal recessive form characterized by segmental isolated
dystonia involving the face, neck, bulbar muscles, and upper
limbs. {ECO:0000269|PubMed:26004199}. 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; X52022; CAA36267.1; -; mRNA.
EMBL; AK092021; BAG52467.1; -; mRNA.
EMBL; AK304870; BAG65607.1; -; mRNA.
EMBL; AC112715; AAY14906.1; -; Genomic_DNA.
EMBL; AC112721; AAY24135.1; -; Genomic_DNA.
EMBL; BC144595; AAI44596.1; -; mRNA.
EMBL; BC150625; AAI50626.1; -; mRNA.
EMBL; S49432; AAB24261.1; -; mRNA.
EMBL; M20778; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; X06196; CAA29557.1; -; mRNA.
EMBL; M27449; AAA52057.1; -; mRNA.
CCDS; CCDS33409.1; -. [P12111-2]
CCDS; CCDS33410.2; -. [P12111-4]
CCDS; CCDS33411.2; -. [P12111-5]
CCDS; CCDS33412.1; -. [P12111-1]
CCDS; CCDS54439.1; -. [P12111-3]
PIR; A59140; CGHU3A.
RefSeq; NP_004360.2; NM_004369.3. [P12111-1]
RefSeq; NP_476505.3; NM_057164.4. [P12111-3]
RefSeq; NP_476506.3; NM_057165.4. [P12111-5]
RefSeq; NP_476507.3; NM_057166.4. [P12111-4]
RefSeq; NP_476508.2; NM_057167.3. [P12111-2]
RefSeq; XP_016858792.1; XM_017003303.1. [P12111-2]
UniGene; Hs.233240; -.
PDB; 1KNT; X-ray; 1.60 A; A=3108-3165.
PDB; 1KTH; X-ray; 0.95 A; A=3108-3165.
PDB; 1KUN; NMR; -; A=3108-3165.
PDB; 2KNT; X-ray; 1.20 A; A=3108-3165.
PDBsum; 1KNT; -.
PDBsum; 1KTH; -.
PDBsum; 1KUN; -.
PDBsum; 2KNT; -.
ProteinModelPortal; P12111; -.
SMR; P12111; -.
BioGrid; 107690; 1.
CORUM; P12111; -.
IntAct; P12111; 6.
MINT; MINT-4053347; -.
STRING; 9606.ENSP00000295550; -.
ChEMBL; CHEMBL2364188; -.
MEROPS; I02.968; -.
iPTMnet; P12111; -.
PhosphoSitePlus; P12111; -.
BioMuta; COL6A3; -.
DMDM; 311033499; -.
EPD; P12111; -.
MaxQB; P12111; -.
PaxDb; P12111; -.
PeptideAtlas; P12111; -.
PRIDE; P12111; -.
Ensembl; ENST00000295550; ENSP00000295550; ENSG00000163359. [P12111-1]
Ensembl; ENST00000353578; ENSP00000315873; ENSG00000163359. [P12111-2]
Ensembl; ENST00000392003; ENSP00000375860; ENSG00000163359. [P12111-3]
Ensembl; ENST00000392004; ENSP00000375861; ENSG00000163359. [P12111-5]
Ensembl; ENST00000409809; ENSP00000386844; ENSG00000163359. [P12111-2]
Ensembl; ENST00000472056; ENSP00000418285; ENSG00000163359. [P12111-4]
GeneID; 1293; -.
KEGG; hsa:1293; -.
UCSC; uc002vwl.3; human. [P12111-1]
CTD; 1293; -.
DisGeNET; 1293; -.
EuPathDB; HostDB:ENSG00000163359.15; -.
GeneCards; COL6A3; -.
GeneReviews; COL6A3; -.
H-InvDB; HIX0002952; -.
HGNC; HGNC:2213; COL6A3.
HPA; HPA010080; -.
MalaCards; COL6A3; -.
MIM; 120250; gene.
MIM; 158810; phenotype.
MIM; 254090; phenotype.
MIM; 616411; phenotype.
neXtProt; NX_P12111; -.
OpenTargets; ENSG00000163359; -.
Orphanet; 610; Bethlem myopathy.
Orphanet; 75840; Congenital muscular dystrophy, Ullrich type.
PharmGKB; PA26729; -.
eggNOG; KOG3544; Eukaryota.
eggNOG; ENOG41103QR; LUCA.
GeneTree; ENSGT00760000119000; -.
HOGENOM; HOG000015249; -.
HOVERGEN; HBG051052; -.
InParanoid; P12111; -.
KO; K06238; -.
OMA; VTYNNEV; -.
OrthoDB; EOG091G14M8; -.
PhylomeDB; P12111; -.
TreeFam; TF337483; -.
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; COL6A3; human.
EvolutionaryTrace; P12111; -.
GeneWiki; COL6A3; -.
GenomeRNAi; 1293; -.
PRO; PR:P12111; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000163359; -.
CleanEx; HS_COL6A3; -.
ExpressionAtlas; P12111; baseline and differential.
Genevisible; P12111; HS.
GO; GO:0005589; C:collagen type VI trimer; TAS:ProtInc.
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; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:1903561; C:extracellular vesicle; IDA:UniProtKB.
GO; GO:0005578; C:proteinaceous extracellular matrix; IDA:MGI.
GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
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:0007517; P:muscle organ development; TAS:ProtInc.
CDD; cd00063; FN3; 1.
CDD; cd00109; KU; 1.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.40.50.410; -; 12.
Gene3D; 4.10.410.10; -; 1.
InterPro; IPR008160; Collagen.
InterPro; IPR003961; FN3_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR002223; Kunitz_BPTI.
InterPro; IPR020901; Prtase_inh_Kunz-CS.
InterPro; IPR002035; VWF_A.
Pfam; PF01391; Collagen; 1.
Pfam; PF00014; Kunitz_BPTI; 1.
Pfam; PF00092; VWA; 12.
PRINTS; PR00759; BASICPTASE.
SMART; SM00131; KU; 1.
SMART; SM00327; VWA; 12.
SUPFAM; SSF49265; SSF49265; 1.
SUPFAM; SSF53300; SSF53300; 12.
SUPFAM; SSF57362; SSF57362; 1.
PROSITE; PS00280; BPTI_KUNITZ_1; 1.
PROSITE; PS50279; BPTI_KUNITZ_2; 1.
PROSITE; PS50853; FN3; 1.
PROSITE; PS50234; VWFA; 12.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Collagen;
Complete proteome; Congenital muscular dystrophy;
Direct protein sequencing; Disease mutation; Disulfide bond; Dystonia;
Extracellular matrix; Glycoprotein; Hydroxylation; Phosphoprotein;
Polymorphism; Protease inhibitor; Pyrrolidone carboxylic acid;
Reference proteome; Repeat; Secreted; Serine protease inhibitor;
Signal.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 3177 Collagen alpha-3(VI) chain.
/FTId=PRO_0000005847.
DOMAIN 39 213 VWFA 1. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
DOMAIN 242 419 VWFA 2. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
DOMAIN 445 620 VWFA 3. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
DOMAIN 639 816 VWFA 4. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
DOMAIN 837 1009 VWFA 5. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
DOMAIN 1029 1205 VWFA 6. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
DOMAIN 1233 1404 VWFA 7. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
DOMAIN 1436 1609 VWFA 8. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
DOMAIN 1639 1812 VWFA 9. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
DOMAIN 1838 2024 VWFA 10. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
DOMAIN 2038 2097 Collagen-like 1.
DOMAIN 2104 2163 Collagen-like 2.
DOMAIN 2174 2233 Collagen-like 3.
DOMAIN 2249 2300 Collagen-like 4.
DOMAIN 2314 2373 Collagen-like 5.
DOMAIN 2402 2581 VWFA 11. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
DOMAIN 2619 2815 VWFA 12. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
DOMAIN 2991 3085 Fibronectin type-III.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 3112 3162 BPTI/Kunitz inhibitor.
{ECO:0000255|PROSITE-ProRule:PRU00031}.
REGION 26 2038 Nonhelical region.
REGION 2039 2375 Triple-helical region.
REGION 2376 3177 Nonhelical region.
MOTIF 2040 2042 Cell attachment site.
MOTIF 2136 2138 Cell attachment site.
MOTIF 2148 2150 Cell attachment site.
MOTIF 2154 2156 Cell attachment site.
MOTIF 2370 2372 Cell attachment site.
COMPBIAS 2863 2898 Thr-rich.
COMPBIAS 2908 2983 Ala-rich.
SITE 3122 3123 Reactive bond.
MOD_RES 26 26 Pyrrolidone carboxylic acid.
{ECO:0000305}.
MOD_RES 433 433 Phosphothreonine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1225 1225 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 2100 2100 4-hydroxyproline.
{ECO:0000269|PubMed:1689238}.
MOD_RES 2103 2103 5-hydroxylysine; alternate.
{ECO:0000269|PubMed:1689238}.
MOD_RES 2206 2206 4-hydroxyproline.
{ECO:0000269|PubMed:1689238}.
MOD_RES 2209 2209 5-hydroxylysine; alternate.
{ECO:0000269|PubMed:1689238}.
MOD_RES 2212 2212 5-hydroxylysine; alternate.
{ECO:0000269|PubMed:1689238}.
MOD_RES 2239 2239 4-hydroxyproline.
{ECO:0000269|PubMed:1689238}.
MOD_RES 2316 2316 4-hydroxyproline.
{ECO:0000269|PubMed:1689238}.
MOD_RES 2319 2319 4-hydroxyproline.
{ECO:0000269|PubMed:1689238}.
MOD_RES 2322 2322 5-hydroxylysine; alternate.
{ECO:0000269|PubMed:1689238}.
MOD_RES 2337 2337 5-hydroxylysine; alternate.
{ECO:0000269|PubMed:1689238}.
CARBOHYD 108 108 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 116 116 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 202 202 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 251 251 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2079 2079 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 2103 2103 O-linked (Gal...) hydroxylysine;
alternate.
CARBOHYD 2209 2209 O-linked (Gal...) hydroxylysine;
alternate.
CARBOHYD 2212 2212 O-linked (Gal...) hydroxylysine;
alternate.
CARBOHYD 2322 2322 O-linked (Gal...) hydroxylysine;
alternate.
CARBOHYD 2331 2331 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2337 2337 O-linked (Gal...) hydroxylysine;
alternate.
CARBOHYD 2558 2558 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2677 2677 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
CARBOHYD 2861 2861 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3037 3037 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 2087 2087 Interchain. {ECO:0000255|PROSITE-
ProRule:PRU00031}.
DISULFID 3112 3162 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 3121 3145 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 3137 3158 {ECO:0000255|PROSITE-ProRule:PRU00031}.
VAR_SEQ 31 437 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_045718.
VAR_SEQ 31 236 Missing (in isoform 2, isoform 3 and
isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_001172.
VAR_SEQ 237 437 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043434.
VAR_SEQ 633 832 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_045719.
VAR_SEQ 1429 1443 AVESDAADIVFLIDS -> GEMGASEVLLGAFSI (in
isoform 3 and isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043435.
VAR_SEQ 1444 3177 Missing (in isoform 3 and isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043436.
VARIANT 411 411 L -> V (in dbSNP:rs113716915).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_058242.
VARIANT 491 491 D -> H (in dbSNP:rs112010940).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_058243.
VARIANT 492 492 T -> S (in dbSNP:rs113897824).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_058244.
VARIANT 538 538 T -> M (in dbSNP:rs34741387).
/FTId=VAR_047279.
VARIANT 659 659 R -> H (in dbSNP:rs36092870).
/FTId=VAR_047280.
VARIANT 677 677 R -> H (in BTHLM1; unknown pathological
significance; dbSNP:rs35227432).
{ECO:0000269|PubMed:15689448,
ECO:0000269|PubMed:17886299}.
/FTId=VAR_058245.
VARIANT 807 807 A -> T (in dbSNP:rs113155945).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_058246.
VARIANT 830 830 A -> S (in dbSNP:rs77181645).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_058247.
VARIANT 886 886 V -> E (in dbSNP:rs9630964).
/FTId=VAR_047281.
VARIANT 1014 1014 K -> E (in BTHLM1; dbSNP:rs114284669).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_058248.
VARIANT 1064 1064 R -> Q (in UCMD1; unknown pathological
significance; dbSNP:rs112638391).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_058249.
VARIANT 1088 1088 K -> Q (in dbSNP:rs11896521).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_047282.
VARIANT 1386 1386 E -> K (in BTHLM1; dbSNP:rs146092501).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_058250.
VARIANT 1395 1395 R -> Q (in UCMD1; dbSNP:rs80272723).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_058251.
VARIANT 1467 1467 N -> D (in BTHLM1; dbSNP:rs138049094).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_058252.
VARIANT 1576 1576 R -> Q (in dbSNP:rs61729839).
{ECO:0000269|PubMed:15689448,
ECO:0000269|PubMed:17886299}.
/FTId=VAR_058253.
VARIANT 1632 1632 R -> Q (in dbSNP:rs111231885).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_058254.
VARIANT 1674 1674 D -> N (in UCMD1; dbSNP:rs778940391).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_058255.
VARIANT 1679 1679 G -> E (in BTHLM1; dbSNP:rs121434553).
{ECO:0000269|PubMed:15689448,
ECO:0000269|PubMed:9536084}.
/FTId=VAR_001910.
VARIANT 1687 1687 P -> S (in dbSNP:rs35273032).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_058256.
VARIANT 1726 1726 L -> R (in BTHLM1; dbSNP:rs121434555).
{ECO:0000269|PubMed:17886299}.
/FTId=VAR_058257.
VARIANT 1985 1985 V -> M (in BTHLM1; dbSNP:rs200478135).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_058258.
VARIANT 2047 2047 G -> D (in BTHLM1).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_058259.
VARIANT 2056 2056 G -> R (in BTHLM1).
{ECO:0000269|PubMed:10399756}.
/FTId=VAR_058260.
VARIANT 2080 2080 G -> D (in BTHLM1; dbSNP:rs794727188).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_058261.
VARIANT 2218 2218 P -> L (in dbSNP:rs36117715).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_047283.
VARIANT 2431 2431 D -> V. {ECO:0000269|PubMed:1689238,
ECO:0000269|PubMed:17886299}.
/FTId=VAR_058262.
VARIANT 2453 2453 E -> K. {ECO:0000269|PubMed:17886299}.
/FTId=VAR_058263.
VARIANT 2501 2501 R -> H (in DYT27; dbSNP:rs541928674).
{ECO:0000269|PubMed:26004199}.
/FTId=VAR_073836.
VARIANT 2554 2554 A -> T (in DYT27; dbSNP:rs786205870).
{ECO:0000269|PubMed:26004199}.
/FTId=VAR_073837.
VARIANT 2805 2805 N -> T (in dbSNP:rs35848091).
/FTId=VAR_047284.
VARIANT 2831 2831 D -> H (in dbSNP:rs36104025).
{ECO:0000269|PubMed:15689448,
ECO:0000269|PubMed:17886299,
ECO:0000269|PubMed:9536084}.
/FTId=VAR_001911.
VARIANT 2927 2927 M -> T (in dbSNP:rs6728818).
{ECO:0000269|PubMed:1689238}.
/FTId=VAR_047285.
VARIANT 2941 2941 A -> V (in BTHLM1; dbSNP:rs11903206).
{ECO:0000269|PubMed:15689448}.
/FTId=VAR_058264.
VARIANT 2988 2988 M -> V (in dbSNP:rs11690358).
{ECO:0000269|PubMed:1689238,
ECO:0000269|PubMed:17886299}.
/FTId=VAR_047286.
VARIANT 3012 3012 A -> P (in dbSNP:rs2270669).
{ECO:0000269|PubMed:1689238}.
/FTId=VAR_047287.
VARIANT 3043 3043 R -> H (in DYT27; dbSNP:rs552651651).
{ECO:0000269|PubMed:26004199}.
/FTId=VAR_073838.
VARIANT 3069 3069 T -> I (in dbSNP:rs1131296).
{ECO:0000269|PubMed:17886299}.
/FTId=VAR_047288.
VARIANT 3082 3082 P -> R (in DYT27; dbSNP:rs182976977).
{ECO:0000269|PubMed:26004199}.
/FTId=VAR_073839.
CONFLICT 127 128 QS -> AK (in Ref. 6; AAB24261).
{ECO:0000305}.
CONFLICT 137 137 R -> L (in Ref. 6; AAB24261).
{ECO:0000305}.
CONFLICT 381 381 A -> V (in Ref. 3; BAG65607).
{ECO:0000305}.
CONFLICT 608 608 F -> S (in Ref. 3; BAG65607).
{ECO:0000305}.
CONFLICT 885 885 K -> E (in Ref. 5; AAI44596/AAI50626).
{ECO:0000305}.
CONFLICT 1282 1282 V -> A (in Ref. 1; CAA36267).
{ECO:0000305}.
CONFLICT 1353 1354 DD -> VV (in Ref. 1; CAA36267).
{ECO:0000305}.
CONFLICT 2157 2157 P -> R (in Ref. 8; CAA29557).
{ECO:0000305}.
CONFLICT 2257 2257 A -> R (in Ref. 1; CAA36267 and 7;
M20778). {ECO:0000305}.
CONFLICT 2287 2287 R -> P (in Ref. 1; CAA36267 and 7;
M20778). {ECO:0000305}.
CONFLICT 2357 2357 D -> R (in Ref. 1; CAA36267 and 7;
M20778). {ECO:0000305}.
CONFLICT 2367 2367 K -> R (in Ref. 1; CAA36267 and 7;
M20778). {ECO:0000305}.
CONFLICT 2441 2441 R -> T (in Ref. 1; CAA36267).
{ECO:0000305}.
CONFLICT 2956 2956 Missing (in Ref. 1; CAA36267).
{ECO:0000305}.
CONFLICT 2992 2992 S -> L (in Ref. 1; CAA36267).
{ECO:0000305}.
HELIX 3110 3113 {ECO:0000244|PDB:1KTH}.
STRAND 3120 3122 {ECO:0000244|PDB:1KTH}.
STRAND 3125 3131 {ECO:0000244|PDB:1KTH}.
TURN 3132 3135 {ECO:0000244|PDB:1KTH}.
STRAND 3136 3142 {ECO:0000244|PDB:1KTH}.
STRAND 3144 3146 {ECO:0000244|PDB:1KTH}.
STRAND 3152 3154 {ECO:0000244|PDB:1KTH}.
HELIX 3155 3162 {ECO:0000244|PDB:1KTH}.
SEQUENCE 3177 AA; 343669 MW; 56D54CAC4FBB30AF CRC64;
MRKHRHLPLV AVFCLFLSGF PTTHAQQQQA DVKNGAAADI IFLVDSSWTI GEEHFQLVRE
FLYDVVKSLA VGENDFHFAL VQFNGNPHTE FLLNTYRTKQ EVLSHISNMS YIGGTNQTGK
GLEYIMQSHL TKAAGSRAGD GVPQVIVVLT DGHSKDGLAL PSAELKSADV NVFAIGVEDA
DEGALKEIAS EPLNMHMFNL ENFTSLHDIV GNLVSCVHSS VSPERAGDTE TLKDITAQDS
ADIIFLIDGS NNTGSVNFAV ILDFLVNLLE KLPIGTQQIR VGVVQFSDEP RTMFSLDTYS
TKAQVLGAVK ALGFAGGELA NIGLALDFVV ENHFTRAGGS RVEEGVPQVL VLISAGPSSD
EIRYGVVALK QASVFSFGLG AQAASRAELQ HIATDDNLVF TVPEFRSFGD LQEKLLPYIV
GVAQRHIVLK PPTIVTQVIE VNKRDIVFLV DGSSALGLAN FNAIRDFIAK VIQRLEIGQD
LIQVAVAQYA DTVRPEFYFN THPTKREVIT AVRKMKPLDG SALYTGSALD FVRNNLFTSS
AGYRAAEGIP KLLVLITGGK SLDEISQPAQ ELKRSSIMAF AIGNKGADQA ELEEIAFDSS
LVFIPAEFRA APLQGMLPGL LAPLRTLSGT PEVHSNKRDI IFLLDGSANV GKTNFPYVRD
FVMNLVNSLD IGNDNIRVGL VQFSDTPVTE FSLNTYQTKS DILGHLRQLQ LQGGSGLNTG
SALSYVYANH FTEAGGSRIR EHVPQLLLLL TAGQSEDSYL QAANALTRAG ILTFCVGASQ
ANKAELEQIA FNPSLVYLMD DFSSLPALPQ QLIQPLTTYV SGGVEEVPLA QPESKRDILF
LFDGSANLVG QFPVVRDFLY KIIDELNVKP EGTRIAVAQY SDDVKVESRF DEHQSKPEIL
NLVKRMKIKT GKALNLGYAL DYAQRYIFVK SAGSRIEDGV LQFLVLLVAG RSSDRVDGPA
SNLKQSGVVP FIFQAKNADP AELEQIVLSP AFILAAESLP KIGDLHPQIV NLLKSVHNGA
PAPVSGEKDV VFLLDGSEGV RSGFPLLKEF VQRVVESLDV GQDRVRVAVV QYSDRTRPEF
YLNSYMNKQD VVNAVRQLTL LGGPTPNTGA ALEFVLRNIL VSSAGSRITE GVPQLLIVLT
ADRSGDDVRN PSVVVKRGGA VPIGIGIGNA DITEMQTISF IPDFAVAIPT FRQLGTVQQV
ISERVTQLTR EELSRLQPVL QPLPSPGVGG KRDVVFLIDG SQSAGPEFQY VRTLIERLVD
YLDVGFDTTR VAVIQFSDDP KVEFLLNAHS SKDEVQNAVQ RLRPKGGRQI NVGNALEYVS
RNIFKRPLGS RIEEGVPQFL VLISSGKSDD EVDDPAVELK QFGVAPFTIA RNADQEELVK
ISLSPEYVFS VSTFRELPSL EQKLLTPITT LTSEQIQKLL ASTRYPPPAV ESDAADIVFL
IDSSEGVRPD GFAHIRDFVS RIVRRLNIGP SKVRVGVVQF SNDVFPEFYL KTYRSQAPVL
DAIRRLRLRG GSPLNTGKAL EFVARNLFVK SAGSRIEDGV PQHLVLVLGG KSQDDVSRFA
QVIRSSGIVS LGVGDRNIDR TELQTITNDP RLVFTVREFR ELPNIEERIM NSFGPSAATP
APPGVDTPPP SRPEKKKADI VFLLDGSINF RRDSFQEVLR FVSEIVDTVY EDGDSIQVGL
VQYNSDPTDE FFLKDFSTKR QIIDAINKVV YKGGRHANTK VGLEHLRVNH FVPEAGSRLD
QRVPQIAFVI TGGKSVEDAQ DVSLALTQRG VKVFAVGVRN IDSEEVGKIA SNSATAFRVG
NVQELSELSE QVLETLHDAM HETLCPGVTD AAKACNLDVI LGFDGSRDQN VFVAQKGFES
KVDAILNRIS QMHRVSCSGG RSPTVRVSVV ANTPSGPVEA FDFDEYQPEM LEKFRNMRSQ
HPYVLTEDTL KVYLNKFRQS SPDSVKVVIH FTDGADGDLA DLHRASENLR QEGVRALILV
GLERVVNLER LMHLEFGRGF MYDRPLRLNL LDLDYELAEQ LDNIAEKACC GVPCKCSGQR
GDRGPIGSIG PKGIPGEDGY RGYPGDEGGP GERGPPGVNG TQGFQGCPGQ RGVKGSRGFP
GEKGEVGEIG LDGLDGEDGD KGLPGSSGEK GNPGRRGDKG PRGEKGERGD VGIRGDPGNP
GQDSQERGPK GETGDLGPMG VPGRDGVPGG PGETGKNGGF GRRGPPGAKG NKGGPGQPGF
EGEQGTRGAQ GPAGPAGPPG LIGEQGISGP RGSGGAAGAP GERGRTGPLG RKGEPGEPGP
KGGIGNRGPR GETGDDGRDG VGSEGRRGKK GERGFPGYPG PKGNPGEPGL NGTTGPKGIR
GRRGNSGPPG IVGQKGDPGY PGPAGPKGNR GDSIDQCALI QSIKDKCPCC YGPLECPVFP
TELAFALDTS EGVNQDTFGR MRDVVLSIVN DLTIAESNCP RGARVAVVTY NNEVTTEIRF
ADSKRKSVLL DKIKNLQVAL TSKQQSLETA MSFVARNTFK RVRNGFLMRK VAVFFSNTPT
RASPQLREAV LKLSDAGITP LFLTRQEDRQ LINALQINNT AVGHALVLPA GRDLTDFLEN
VLTCHVCLDI CNIDPSCGFG SWRPSFRDRR AAGSDVDIDM AFILDSAETT TLFQFNEMKK
YIAYLVRQLD MSPDPKASQH FARVAVVQHA PSESVDNASM PPVKVEFSLT DYGSKEKLVD
FLSRGMTQLQ GTRALGSAIE YTIENVFESA PNPRDLKIVV LMLTGEVPEQ QLEEAQRVIL
QAKCKGYFFV VLGIGRKVNI KEVYTFASEP NDVFFKLVDK STELNEEPLM RFGRLLPSFV
SSENAFYLSP DIRKQCDWFQ GDQPTKNLVK FGHKQVNVPN NVTSSPTSNP VTTTKPVTTT
KPVTTTTKPV TTTTKPVTII NQPSVKPAAA KPAPAKPVAA KPVATKMATV RPPVAVKPAT
AAKPVAAKPA AVRPPAAAAA KPVATKPEVP RPQAAKPAAT KPATTKPMVK MSREVQVFEI
TENSAKLHWE RAEPPGPYFY DLTVTSAHDQ SLVLKQNLTV TDRVIGGLLA GQTYHVAVVC
YLRSQVRATY HGSFSTKKSQ PPPPQPARSA SSSTINLMVS TEPLALTETD ICKLPKDEGT
CRDFILKWYY DPNTKSCARF WYGGCGGNEN KFGSQKECEK VCAPVLAKPG VISVMGT


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U0572m CLIA Alpha-1 type II collagen,Col2a1,Collagen alpha-1(II) chain,Mouse,Mus musculus 96T


 

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