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Collagen alpha-2(IV) chain [Cleaved into: Canstatin]

 CO4A2_HUMAN             Reviewed;        1712 AA.
P08572; Q14052; Q548C3; Q5VZA9; Q66K23;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
03-APR-2007, sequence version 4.
27-SEP-2017, entry version 193.
RecName: Full=Collagen alpha-2(IV) chain;
Contains:
RecName: Full=Canstatin;
Flags: Precursor;
Name=COL4A2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3198637;
Hostikka S.L., Tryggvason K.;
"The complete primary structure of the alpha 2 chain of human type IV
collagen and comparison with the alpha 1(IV) chain.";
J. Biol. Chem. 263:19488-19493(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-1042, AND VARIANTS LYS-517 AND
ALA-683.
TISSUE=Placenta;
PubMed=3345760; DOI=10.1111/j.1432-1033.1988.tb13852.x;
Brazel D., Pollner R., Oberbaeumer I., Kuehn K.;
"Human basement membrane collagen (type IV). The amino acid sequence
of the alpha 2(IV) chain and its comparison with the alpha 1(IV) chain
reveals deletions in the alpha 1(IV) chain.";
Eur. J. Biochem. 172:35-42(1988).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
PubMed=2846280;
Poeschl E., Pollner R., Kuehn K.;
"The genes for the alpha 1(IV) and alpha 2(IV) chains of human
basement membrane collagen type IV are arranged head-to-head and
separated by a bidirectional promoter of unique structure.";
EMBO J. 7:2687-2695(1988).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
PubMed=3182844;
Soininen R., Huotari M., Hostikka S.L., Prockop D.J., Tryggvason K.;
"The structural genes for alpha 1 and alpha 2 chains of human type IV
collagen are divergently encoded on opposite DNA strands and have an
overlapping promoter region.";
J. Biol. Chem. 263:17217-17220(1988).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
TISSUE=Skin;
PubMed=8317999; DOI=10.1042/bj2920687;
Fischer G., Schmidt C., Opitz J., Cully Z., Kuehn K., Poeschl E.;
"Identification of a novel sequence element in the common promoter
region of human collagen type IV genes, involved in the regulation of
divergent transcription.";
Biochem. J. 292:687-695(1993).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1040-1712.
TISSUE=Placenta;
PubMed=3692475; DOI=10.1007/BF00291418;
Killen P.D., Francomano C.A., Yamada Y., Modi W.S., O'Brien S.J.;
"Partial structure of the human alpha 2(IV) collagen chain and
chromosomal localization of the gene (COL4A2).";
Hum. Genet. 77:318-324(1987).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1254-1712, AND VARIANT ILE-1399.
PubMed=3582677; DOI=10.1016/0014-5793(87)80706-8;
Hostikka S.L., Kurkinen M., Tryggvason K.;
"Nucleotide sequence coding for the human type IV collagen alpha 2
chain cDNA reveals extensive homology with the NC-1 domain of alpha 1
(IV) but not with the collagenous domain or 3'-untranslated region.";
FEBS Lett. 216:281-286(1987).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1351-1712.
TISSUE=Eye;
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).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 1451-1485.
PubMed=3025878; DOI=10.1073/pnas.84.2.512;
Griffin C.A., Emanuel B.S., Hansen J.R., Cavenee W.K., Myers J.C.;
"Human collagen genes encoding basement membrane alpha 1 (IV) and
alpha 2 (IV) chains map to the distal long arm of chromosome 13.";
Proc. Natl. Acad. Sci. U.S.A. 84:512-516(1987).
[11]
PROTEIN SEQUENCE OF 1480-1535; 1545-1614; 1617-1701 AND 1705-1712.
TISSUE=Placenta;
PubMed=2844531; DOI=10.1111/j.1432-1033.1988.tb14321.x;
Siebold B., Deutzmann R., Kuehn K.;
"The arrangement of intra- and intermolecular disulfide bonds in the
carboxyterminal, non-collagenous aggregation and cross-linking domain
of basement-membrane type IV collagen.";
Eur. J. Biochem. 176:617-624(1988).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 1486-1712.
PubMed=2439508;
Myers J.C., Howard P.S., Jelen A.M., Dion A.S., Macarak E.J.;
"Duplication of type IV collagen COOH-terminal repeats and species-
specific expression of alpha 1(IV) and alpha 2(IV) collagen genes.";
J. Biol. Chem. 262:9231-9238(1987).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 1486-1712, AND FUNCTION.
PubMed=10625665; DOI=10.1074/jbc.275.2.1209;
Kamphaus G.D., Colorado P.C., Panka D.J., Hopfer H., Ramchandran R.,
Torre A., Maeshima Y., Mier J.W., Sukhatme V.P., Kalluri R.;
"Canstatin, a novel matrix-derived inhibitor of angiogenesis and tumor
growth.";
J. Biol. Chem. 275:1209-1215(2000).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 1486-1712.
Peng X., Sun W., Yin B., Yuan J., Qiang B.;
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 1486-1712.
TISSUE=Hepatocyte;
Li Y., Huang G., Qian G.;
"Molecular cloning and homologous sequence analysis of canstatin cDNA
derived from Chinese hepatocytes.";
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[16]
NUCLEOTIDE SEQUENCE [MRNA] OF 1486-1712.
Shan Z.X., Yu X.Y., Lin Q.X., Fu Y.H., Yang M., Tan H.H.;
"Cloning and expression of canstatin in yeast.";
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[17]
FUNCTION OF CANSTATIN.
PubMed=12876280; DOI=10.1074/jbc.M307339200;
Panka D.J., Mier J.W.;
"Canstatin inhibits Akt activation and induces Fas-dependent apoptosis
in endothelial cells.";
J. Biol. Chem. 278:37632-37636(2003).
[18]
FUNCTION OF CANSTATIN.
PubMed=15899827; DOI=10.1158/0008-5472.CAN-04-3536;
Magnon C., Galaup A., Mullan B., Rouffiac V., Bouquet C., Bidart J.M.,
Griscelli F., Opolon P., Perricaudet M.;
"Canstatin acts on endothelial and tumor cells via mitochondrial
damage initiated through interaction with alphavbeta3 and alphavbeta5
integrins.";
Cancer Res. 65:4353-4361(2005).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
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).
[21]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1485-1712.
PubMed=12011424; DOI=10.1073/pnas.062183499;
Than M.E., Henrich S., Huber R., Ries A., Mann K., Kuhn K., Timpl R.,
Bourenkov G.P., Bartunik H.D., Bode W.;
"The 1.9-A crystal structure of the noncollagenous (NC1) domain of
human placenta collagen IV shows stabilization via a novel type of
covalent Met-Lys cross-link.";
Proc. Natl. Acad. Sci. U.S.A. 99:6607-6612(2002).
[22]
VARIANTS PHE-192; LYS-517; ALA-683; ARG-701 AND SER-718.
PubMed=21527998;
Karolak J.A., Kulinska K., Nowak D.M., Pitarque J.A., Molinari A.,
Rydzanicz M., Bejjani B.A., Gajecka M.;
"Sequence variants in COL4A1 and COL4A2 genes in Ecuadorian families
with keratoconus.";
Mol. Vis. 17:827-843(2011).
[23]
VARIANTS POREN2 GLU-1037 AND ASP-1152.
PubMed=22209246; DOI=10.1016/j.ajhg.2011.11.016;
Yoneda Y., Haginoya K., Arai H., Yamaoka S., Tsurusaki Y., Doi H.,
Miyake N., Yokochi K., Osaka H., Kato M., Matsumoto N., Saitsu H.;
"De novo and inherited mutations in COL4A2, encoding the type IV
collagen alpha2 chain cause porencephaly.";
Am. J. Hum. Genet. 90:86-90(2012).
[24]
INVOLVEMENT IN SUSCEPTIBILITY TO ICH, VARIANTS PHE-192; LYS-517;
ALA-683; ARG-701; SER-718; GLN-1109; GLY-1123; LYS-1150; ILE-1399 AND
THR-1690, AND CHARACTERIZATION OF VARIANTS GLY-1123; LYS-1150 AND
THR-1690.
PubMed=22209247; DOI=10.1016/j.ajhg.2011.11.022;
Jeanne M., Labelle-Dumais C., Jorgensen J., Kauffman W.B.,
Mancini G.M., Favor J., Valant V., Greenberg S.M., Rosand J.,
Gould D.B.;
"COL4A2 mutations impair COL4A1 and COL4A2 secretion and cause
hemorrhagic stroke.";
Am. J. Hum. Genet. 90:91-101(2012).
[25]
VARIANT ARG-1389.
PubMed=22333902; DOI=10.1038/ejhg.2012.20;
Verbeek E., Meuwissen M.E., Verheijen F.W., Govaert P.P., Licht D.J.,
Kuo D.S., Poulton C.J., Schot R., Lequin M.H., Dudink J., Halley D.J.,
de Coo R.I., den Hollander J.C., Oegema R., Gould D.B., Mancini G.M.;
"COL4A2 mutation associated with familial porencephaly and small-
vessel disease.";
Eur. J. Hum. Genet. 20:844-851(2012).
-!- FUNCTION: Type IV collagen is the major structural component of
glomerular basement membranes (GBM), forming a 'chicken-wire'
meshwork together with laminins, proteoglycans and
entactin/nidogen.
-!- FUNCTION: Canstatin, a cleavage product corresponding to the
collagen alpha 2(IV) NC1 domain, possesses both anti-angiogenic
and anti-tumor cell activity. It inhibits proliferation and
migration of endothelial cells, reduces mitochondrial membrane
potential, and induces apoptosis. Specifically induces Fas-
dependent apoptosis and activates procaspase-8 and -9 activity.
Ligand for alphavbeta3 and alphavbeta5 integrins.
-!- SUBUNIT: There are six type IV collagen isoforms, alpha 1(IV)-
alpha 6(IV), each of which can form a triple helix structure with
2 other chains to generate type IV collagen network.
-!- INTERACTION:
P02462:COL4A1; NbExp=2; IntAct=EBI-2432506, EBI-2432478;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix, basement membrane.
-!- DOMAIN: Alpha chains of type IV collagen have a non-collagenous
domain (NC1) at their C-terminus, frequent interruptions of the G-
X-Y repeats in the long central triple-helical domain (which may
cause flexibility in the triple helix), and a short N-terminal
triple-helical 7S domain.
-!- PTM: Prolines at the third position of the tripeptide repeating
unit (G-X-Y) are hydroxylated in some or all of the chains.
-!- PTM: Type IV collagens contain numerous cysteine residues which
are involved in inter- and intramolecular disulfide bonding. 12 of
these, located in the NC1 domain, are conserved in all known type
IV collagens.
-!- PTM: The trimeric structure of the NC1 domains is stabilized by
covalent bonds between Lys and Met residues. {ECO:0000250}.
-!- PTM: Proteolytic processing produces the C-terminal NC1 peptide,
canstatin.
-!- DISEASE: Porencephaly 2 (POREN2) [MIM:614483]: A neurologic
disorder characterized by a fluid-filled cysts or cavities within
the cerebral hemispheres. Affected individuals typically have
hemiplegia, seizures, and intellectual disability. Porencephaly
type 2, or schizencephalic porencephaly, is usually symmetric and
represents a primary defect in the development of the cerebral
ventricles. {ECO:0000269|PubMed:22209246}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Intracerebral hemorrhage (ICH) [MIM:614519]: A
pathological condition characterized by bleeding into one or both
cerebral hemispheres including the basal ganglia and the cerebral
cortex. It is often associated with hypertension and
craniocerebral trauma. Intracerebral bleeding is a common cause of
stroke. {ECO:0000269|PubMed:22209247}. Note=Disease susceptibility
is associated with variations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the type IV collagen family.
{ECO:0000255|PROSITE-ProRule:PRU00736}.
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EMBL; AL139385; CAI17005.2; -; Genomic_DNA.
EMBL; AL159153; CAI17005.2; JOINED; Genomic_DNA.
EMBL; AL161773; CAI17005.2; JOINED; Genomic_DNA.
EMBL; AL159153; CAH72050.2; -; Genomic_DNA.
EMBL; AL139385; CAH72050.2; JOINED; Genomic_DNA.
EMBL; AL161773; CAH72050.2; JOINED; Genomic_DNA.
EMBL; AL161773; CAH71366.2; -; Genomic_DNA.
EMBL; AL139385; CAH71366.2; JOINED; Genomic_DNA.
EMBL; AL159153; CAH71366.2; JOINED; Genomic_DNA.
EMBL; X05562; CAA29076.1; -; mRNA.
EMBL; M36963; AAA53099.1; -; Genomic_DNA.
EMBL; J04217; AAA53097.1; -; Genomic_DNA.
EMBL; X12784; CAA31275.1; -; Genomic_DNA.
EMBL; M24766; AAA52043.1; -; mRNA.
EMBL; X05610; CAA29098.1; -; mRNA.
EMBL; BC080644; AAH80644.1; -; mRNA.
EMBL; J02760; AAA58422.1; -; mRNA.
EMBL; AF258350; AAF72631.1; -; mRNA.
EMBL; AF400430; AAK92479.1; -; mRNA.
EMBL; AY450357; AAR20245.1; -; mRNA.
EMBL; AY455978; AAR18250.1; -; mRNA.
CCDS; CCDS41907.1; -.
PIR; A32024; CGHU2B.
RefSeq; NP_001837.2; NM_001846.3.
UniGene; Hs.508716; -.
PDB; 1LI1; X-ray; 1.90 A; C/F=1485-1712.
PDBsum; 1LI1; -.
ProteinModelPortal; P08572; -.
SMR; P08572; -.
BioGrid; 107681; 40.
IntAct; P08572; 21.
MINT; MINT-1180068; -.
STRING; 9606.ENSP00000353654; -.
ChEMBL; CHEMBL2364188; -.
iPTMnet; P08572; -.
PhosphoSitePlus; P08572; -.
SwissPalm; P08572; -.
BioMuta; COL4A2; -.
DMDM; 143811377; -.
EPD; P08572; -.
MaxQB; P08572; -.
PaxDb; P08572; -.
PeptideAtlas; P08572; -.
PRIDE; P08572; -.
Ensembl; ENST00000360467; ENSP00000353654; ENSG00000134871.
GeneID; 1284; -.
KEGG; hsa:1284; -.
UCSC; uc001vqx.4; human.
CTD; 1284; -.
DisGeNET; 1284; -.
EuPathDB; HostDB:ENSG00000134871.17; -.
GeneCards; COL4A2; -.
H-InvDB; HIX0011454; -.
HGNC; HGNC:2203; COL4A2.
HPA; CAB010751; -.
HPA; HPA029118; -.
MalaCards; COL4A2; -.
MIM; 120090; gene.
MIM; 614483; phenotype.
MIM; 614519; phenotype.
neXtProt; NX_P08572; -.
OpenTargets; ENSG00000134871; -.
Orphanet; 99810; Familial porencephaly.
PharmGKB; PA26718; -.
eggNOG; KOG3544; Eukaryota.
eggNOG; ENOG410XNMM; LUCA.
GeneTree; ENSGT00840000129673; -.
HOGENOM; HOG000085652; -.
HOVERGEN; HBG004933; -.
InParanoid; P08572; -.
KO; K06237; -.
OMA; GWVGDPG; -.
OrthoDB; EOG091G0613; -.
PhylomeDB; P08572; -.
TreeFam; TF344135; -.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-1474244; Extracellular matrix organization.
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-2214320; Anchoring fibril formation.
Reactome; R-HSA-2243919; Crosslinking of collagen fibrils.
Reactome; R-HSA-3000157; Laminin interactions.
Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
Reactome; R-HSA-3000178; ECM proteoglycans.
Reactome; R-HSA-3000480; Scavenging by Class A Receptors.
Reactome; R-HSA-419037; NCAM1 interactions.
Reactome; R-HSA-8948216; Collagen chain trimerization.
SIGNOR; P08572; -.
ChiTaRS; COL4A2; human.
EvolutionaryTrace; P08572; -.
GeneWiki; COL4A2; -.
GenomeRNAi; 1284; -.
PMAP-CutDB; P08572; -.
PRO; PR:P08572; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000134871; -.
CleanEx; HS_COL4A2; -.
ExpressionAtlas; P08572; baseline and differential.
Genevisible; P08572; HS.
GO; GO:0005587; C:collagen type IV trimer; TAS:UniProtKB.
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:0005201; F:extracellular matrix structural constituent; TAS:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IEA:Ensembl.
GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0016525; P:negative regulation of angiogenesis; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:Ensembl.
Gene3D; 2.170.240.10; -; 1.
InterPro; IPR008160; Collagen.
InterPro; IPR001442; Collagen_VI_NC.
InterPro; IPR016187; CTDL_fold.
Pfam; PF01413; C4; 2.
Pfam; PF01391; Collagen; 17.
SMART; SM00111; C4; 2.
SUPFAM; SSF56436; SSF56436; 2.
PROSITE; PS51403; NC1_IV; 1.
1: Evidence at protein level;
3D-structure; Angiogenesis; Basement membrane; Collagen;
Complete proteome; Direct protein sequencing; Disease mutation;
Disulfide bond; Extracellular matrix; Glycoprotein; Hydroxylation;
Polymorphism; Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 25
PROPEP 26 183 N-terminal propeptide (7S domain).
/FTId=PRO_0000005824.
CHAIN 184 1712 Collagen alpha-2(IV) chain.
/FTId=PRO_0000005825.
CHAIN 1486 1712 Canstatin.
/FTId=PRO_0000283775.
DOMAIN 1489 1712 Collagen IV NC1. {ECO:0000255|PROSITE-
ProRule:PRU00736}.
REGION 184 1484 Triple-helical region.
CARBOHYD 138 138 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:3198637}.
DISULFID 1504 1593
DISULFID 1537 1590
DISULFID 1549 1555
DISULFID 1612 1708
DISULFID 1646 1705
DISULFID 1658 1665
VARIANT 192 192 V -> F (polymorphism; does not affect
COL4A2 and COL4A1 secretion;
dbSNP:rs62621885).
{ECO:0000269|PubMed:21527998,
ECO:0000269|PubMed:22209247}.
/FTId=VAR_067551.
VARIANT 517 517 R -> K (in dbSNP:rs7990383).
{ECO:0000269|PubMed:21527998,
ECO:0000269|PubMed:22209247,
ECO:0000269|PubMed:3345760}.
/FTId=VAR_048796.
VARIANT 683 683 G -> A (in dbSNP:rs3803230).
{ECO:0000269|PubMed:21527998,
ECO:0000269|PubMed:22209247,
ECO:0000269|PubMed:3345760}.
/FTId=VAR_048797.
VARIANT 701 701 K -> R (polymorphism; does not affect
COL4A2 and COL4A1 secretion;
dbSNP:rs78829338).
{ECO:0000269|PubMed:21527998,
ECO:0000269|PubMed:22209247}.
/FTId=VAR_067552.
VARIANT 718 718 P -> S (polymorphism; does not affect
COL4A2 and COL4A1 secretion;
dbSNP:rs9583500).
{ECO:0000269|PubMed:21527998,
ECO:0000269|PubMed:22209247}.
/FTId=VAR_067836.
VARIANT 1037 1037 G -> E (in POREN2; dbSNP:rs387906603).
{ECO:0000269|PubMed:22209246}.
/FTId=VAR_067837.
VARIANT 1109 1109 R -> Q (polymorphism; does not affect
COL4A2 and COL4A1 secretion;
dbSNP:rs184812559).
{ECO:0000269|PubMed:22209247}.
/FTId=VAR_067553.
VARIANT 1123 1123 E -> G (associated with ICH
susceptibility; results in a
significantly decreased extracellular-to-
intracellular ratio of COL4A2 and COL4A1
proteins, indicating interference with
the proper secretion of both these
proteins; dbSNP:rs117412802).
{ECO:0000269|PubMed:22209247}.
/FTId=VAR_067554.
VARIANT 1150 1150 Q -> K (associated with ICH
susceptibility; results in a
significantly decreased extracellular-to-
intracellular ratio of COL4A2 and COL4A1
proteins, indicating interference with
the proper secretion of both these
proteins; dbSNP:rs62621875).
{ECO:0000269|PubMed:22209247}.
/FTId=VAR_067555.
VARIANT 1152 1152 G -> D (in POREN2; incomplete penetrance;
dbSNP:rs387906602).
{ECO:0000269|PubMed:22209246}.
/FTId=VAR_067838.
VARIANT 1389 1389 G -> R (probable disease-associated
mutation found in a family with
porencephaly and small-vessel disease in
the form of scattered white matter
lesions; impairs COL4A2 and COL4A1
secretion; the mutant protein is retained
in the endoplasmic reticulum).
{ECO:0000269|PubMed:22333902}.
/FTId=VAR_067556.
VARIANT 1399 1399 V -> I (in dbSNP:rs45520539).
{ECO:0000269|PubMed:22209247,
ECO:0000269|PubMed:3582677}.
/FTId=VAR_067557.
VARIANT 1690 1690 A -> T (associated with ICH
susceptibility; results in a
significantly decreased extracellular-to-
intracellular ratio of COL4A2 and COL4A1
proteins, indicating interference with
the proper secretion of both these
proteins; dbSNP:rs201105747).
{ECO:0000269|PubMed:22209247}.
/FTId=VAR_067558.
CONFLICT 471 471 R -> P (in Ref. 3; CAA29076).
{ECO:0000305}.
CONFLICT 1041 1041 V -> L (in Ref. 7; AAA52043).
{ECO:0000305}.
CONFLICT 1419 1419 M -> I (in Ref. 8; CAA29098).
{ECO:0000305}.
CONFLICT 1575 1575 M -> I (in Ref. 12; AAA58422).
{ECO:0000305}.
CONFLICT 1636 1636 G -> V (in Ref. 7; AAA52043).
{ECO:0000305}.
CONFLICT 1663 1663 G -> H (in Ref. 11; AA sequence).
{ECO:0000305}.
CONFLICT 1701 1701 H -> G (in Ref. 11; AA sequence).
{ECO:0000305}.
STRAND 1490 1495 {ECO:0000244|PDB:1LI1}.
STRAND 1497 1500 {ECO:0000244|PDB:1LI1}.
STRAND 1509 1522 {ECO:0000244|PDB:1LI1}.
STRAND 1525 1528 {ECO:0000244|PDB:1LI1}.
HELIX 1534 1536 {ECO:0000244|PDB:1LI1}.
STRAND 1537 1540 {ECO:0000244|PDB:1LI1}.
STRAND 1546 1550 {ECO:0000244|PDB:1LI1}.
TURN 1551 1553 {ECO:0000244|PDB:1LI1}.
STRAND 1554 1558 {ECO:0000244|PDB:1LI1}.
STRAND 1563 1568 {ECO:0000244|PDB:1LI1}.
HELIX 1580 1586 {ECO:0000244|PDB:1LI1}.
STRAND 1589 1597 {ECO:0000244|PDB:1LI1}.
STRAND 1599 1603 {ECO:0000244|PDB:1LI1}.
STRAND 1605 1608 {ECO:0000244|PDB:1LI1}.
STRAND 1616 1629 {ECO:0000244|PDB:1LI1}.
STRAND 1635 1637 {ECO:0000244|PDB:1LI1}.
HELIX 1643 1645 {ECO:0000244|PDB:1LI1}.
STRAND 1646 1649 {ECO:0000244|PDB:1LI1}.
STRAND 1655 1659 {ECO:0000244|PDB:1LI1}.
TURN 1660 1663 {ECO:0000244|PDB:1LI1}.
STRAND 1664 1666 {ECO:0000244|PDB:1LI1}.
STRAND 1672 1677 {ECO:0000244|PDB:1LI1}.
STRAND 1680 1684 {ECO:0000244|PDB:1LI1}.
STRAND 1691 1694 {ECO:0000244|PDB:1LI1}.
HELIX 1699 1701 {ECO:0000244|PDB:1LI1}.
STRAND 1704 1710 {ECO:0000244|PDB:1LI1}.
SEQUENCE 1712 AA; 167553 MW; E0DABEEAB349D8AF CRC64;
MGRDQRAVAG PALRRWLLLG TVTVGFLAQS VLAGVKKFDV PCGGRDCSGG CQCYPEKGGR
GQPGPVGPQG YNGPPGLQGF PGLQGRKGDK GERGAPGVTG PKGDVGARGV SGFPGADGIP
GHPGQGGPRG RPGYDGCNGT QGDSGPQGPP GSEGFTGPPG PQGPKGQKGE PYALPKEERD
RYRGEPGEPG LVGFQGPPGR PGHVGQMGPV GAPGRPGPPG PPGPKGQQGN RGLGFYGVKG
EKGDVGQPGP NGIPSDTLHP IIAPTGVTFH PDQYKGEKGS EGEPGIRGIS LKGEEGIMGF
PGLRGYPGLS GEKGSPGQKG SRGLDGYQGP DGPRGPKGEA GDPGPPGLPA YSPHPSLAKG
ARGDPGFPGA QGEPGSQGEP GDPGLPGPPG LSIGDGDQRR GLPGEMGPKG FIGDPGIPAL
YGGPPGPDGK RGPPGPPGLP GPPGPDGFLF GLKGAKGRAG FPGLPGSPGA RGPKGWKGDA
GECRCTEGDE AIKGLPGLPG PKGFAGINGE PGRKGDRGDP GQHGLPGFPG LKGVPGNIGA
PGPKGAKGDS RTITTKGERG QPGVPGVPGM KGDDGSPGRD GLDGFPGLPG PPGDGIKGPP
GDPGYPGIPG TKGTPGEMGP PGLGLPGLKG QRGFPGDAGL PGPPGFLGPP GPAGTPGQID
CDTDVKRAVG GDRQEAIQPG CIGGPKGLPG LPGPPGPTGA KGLRGIPGFA GADGGPGPRG
LPGDAGREGF PGPPGFIGPR GSKGAVGLPG PDGSPGPIGL PGPDGPPGER GLPGEVLGAQ
PGPRGDAGVP GQPGLKGLPG DRGPPGFRGS QGMPGMPGLK GQPGLPGPSG QPGLYGPPGL
HGFPGAPGQE GPLGLPGIPG REGLPGDRGD PGDTGAPGPV GMKGLSGDRG DAGFTGEQGH
PGSPGFKGID GMPGTPGLKG DRGSPGMDGF QGMPGLKGRP GFPGSKGEAG FFGIPGLKGL
AGEPGFKGSR GDPGPPGPPP VILPGMKDIK GEKGDEGPMG LKGYLGAKGI QGMPGIPGLS
GIPGLPGRPG HIKGVKGDIG VPGIPGLPGF PGVAGPPGIT GFPGFIGSRG DKGAPGRAGL
YGEIGATGDF GDIGDTINLP GRPGLKGERG TTGIPGLKGF FGEKGTEGDI GFPGITGVTG
VQGPPGLKGQ TGFPGLTGPP GSQGELGRIG LPGGKGDDGW PGAPGLPGFP GLRGIRGLHG
LPGTKGFPGS PGSDIHGDPG FPGPPGERGD PGEANTLPGP VGVPGQKGDQ GAPGERGPPG
SPGLQGFPGI TPPSNISGAP GDKGAPGIFG LKGYRGPPGP PGSAALPGSK GDTGNPGAPG
TPGTKGWAGD SGPQGRPGVF GLPGEKGPRG EQGFMGNTGP TGAVGDRGPK GPKGDPGFPG
APGTVGAPGI AGIPQKIAVQ PGTVGPQGRR GPPGAPGEMG PQGPPGEPGF RGAPGKAGPQ
GRGGVSAVPG FRGDEGPIGH QGPIGQEGAP GRPGSPGLPG MPGRSVSIGY LLVKHSQTDQ
EPMCPVGMNK LWSGYSLLYF EGQEKAHNQD LGLAGSCLAR FSTMPFLYCN PGDVCYYASR
NDKSYWLSTT APLPMMPVAE DEIKPYISRC SVCEAPAIAI AVHSQDVSIP HCPAGWRSLW
IGYSFLMHTA AGDEGGGQSL VSPGSCLEDF RATPFIECNG GRGTCHYYAN KYSFWLTTIP
EQSFQGSPSA DTLKAGLIRT HISRCQVCMK NL


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