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Collagen alpha-4(IV) chain

 CO4A4_HUMAN             Reviewed;        1690 AA.
P53420; A8MTZ1; Q53RW9; Q53S42; Q53WR1;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
22-SEP-2009, sequence version 3.
27-SEP-2017, entry version 184.
RecName: Full=Collagen alpha-4(IV) chain;
Flags: Precursor;
Name=COL4A4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANTS LEU-1004;
MET-1327 AND PRO-1403.
TISSUE=Kidney;
PubMed=7523402;
Leinonen A., Mariyama M., Mochizuki T., Tryggvason K., Reeders S.T.;
"Complete primary structure of the human type IV collagen alpha 4(IV)
chain. Comparison with structure and expression of the other alpha
(IV) chains.";
J. Biol. Chem. 269:26172-26177(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS APSAR VAL-1030 AND
LEU-1572, AND VARIANTS ALA-545; GLN-570; THR-931; LEU-1004; MET-1327;
SER-1402 AND PRO-1403.
PubMed=9792860; DOI=10.1086/302106;
Boye E., Mollet G., Forestier L., Cohen-Solal L., Heidet L.,
Cochat P., Gruenfeld J.-P., Palcoux J.-B., Gubler M.-C., Antignac C.;
"Determination of the genomic structure of the COL4A4 gene and of
novel mutations causing autosomal recessive Alport syndrome.";
Am. J. Hum. Genet. 63:1329-1340(1998).
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
PubMed=9537506; DOI=10.1016/S0014-5793(98)00128-8;
Momota R., Sugimoto M., Oohashi T., Kigasawa K., Yoshioka H.,
Ninomiya Y.;
"Two genes, COL4A3 and COL4A4 coding for the human alpha3(IV) and
alpha4(IV) collagen chains are arranged head-to-head on chromosome
2q36.";
FEBS Lett. 424:11-16(1998).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1219-1690, AND VARIANTS MET-1327 AND
PRO-1403.
TISSUE=Eye;
PubMed=8365481; DOI=10.1016/0014-5793(93)80256-T;
Sugimoto M., Oohashi T., Yoshioka H., Matsuo N., Ninomiya Y.;
"cDNA isolation and partial gene structure of the human alpha 4(IV)
collagen chain.";
FEBS Lett. 330:122-128(1993).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1407-1507.
PubMed=1429714;
Kamagata Y., Mattei M.-G., Ninomiya Y.;
"Isolation and sequencing of cDNAs and genomic DNAs encoding the alpha
4 chain of basement membrane collagen type IV and assignment of the
gene to the distal long arm of human chromosome 2.";
J. Biol. Chem. 267:23753-23758(1992).
[7]
TISSUE SPECIFICITY.
PubMed=8083201;
Mariyama M., Leinonen A., Mochizuki T., Tryggvason K., Reeders S.T.;
"Complete primary structure of the human alpha 3(IV) collagen chain.
Coexpression of the alpha 3(IV) and alpha 4(IV) collagen chains in
human tissues.";
J. Biol. Chem. 269:23013-23017(1994).
[8]
HEXAMERIZATION.
PubMed=12193605; DOI=10.1074/jbc.M207769200;
Borza D.B., Bondar O., Todd P., Sundaramoorthy M., Sado Y.,
Ninomiya Y., Hudson B.G.;
"Quaternary organization of the goodpasture autoantigen, the alpha
3(IV) collagen chain. Sequestration of two cryptic autoepitopes by
intrapromoter interactions with the alpha4 and alpha5 NC1 domains.";
J. Biol. Chem. 277:40075-40083(2002).
[9]
REVIEW ON VARIANTS.
PubMed=9195222;
DOI=10.1002/(SICI)1098-1004(1997)9:6<477::AID-HUMU1>3.3.CO;2-H;
Lemmink H.H., Schroeder C.H., Monnens L.A.H., Smeets H.J.M.;
"The clinical spectrum of type IV collagen mutations.";
Hum. Mutat. 9:477-499(1997).
[10]
VARIANT APSAR SER-1201.
PubMed=7987396; DOI=10.1038/ng0994-77;
Mochizuki T., Lemmink H.H., Mariyama M., Antignac C., Gubler M.-C.,
Pirson Y., Verellen-Dumoulin C., Chan B., Schroeder C.H.,
Smeets H.J.M., Reeders S.T.;
"Identification of mutations in the alpha 3(IV) and alpha 4(IV)
collagen genes in autosomal recessive Alport syndrome.";
Nat. Genet. 8:77-82(1994).
[11]
VARIANT BFH GLU-897.
PubMed=8787673; DOI=10.1172/JCI118893;
Lemmink H.H., Nillesen W.N., Mochizuki T., Schroeder C.H.,
Brunner H.G., van Oost B.A., Monnens L.A.H., Smeets H.J.M.;
"Benign familial hematuria due to mutation of the type IV collagen
alpha4 gene.";
J. Clin. Invest. 98:1114-1118(1996).
[12]
VARIANT BFH ARG-960, AND VARIANTS THR-6; SER-482 AND ALA-545.
PubMed=11961012;
Badenas C., Praga M., Tazon B., Heidet L., Arrondel C., Armengol A.,
Andres A., Morales E., Camacho J.A., Lens X., Davila S., Mila M.,
Antignac C., Darnell A., Torra R.;
"Mutations in the COL4A4 and COL4A3 genes cause familial benign
hematuria.";
J. Am. Soc. Nephrol. 13:1248-1254(2002).
[13]
VARIANTS BFH GLU-116; ARG-960; GLU-999 AND LEU-1132, AND VARIANT
SER-482.
PubMed=12631110; DOI=10.1046/j.1523-1755.2003.00780.x;
Buzza M., Dagher H., Wang Y.Y., Wilson D., Babon J.J., Cotton R.G.,
Savige J.;
"Mutations in the COL4A4 gene in thin basement membrane disease.";
Kidney Int. 63:447-453(2003).
-!- 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.
-!- 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. The alpha
3(IV) chain forms a triple helical protomer with alpha 4(IV) and
alpha 5(IV); this triple helical structure dimerizes through NC1-
NC1 domain interactions such that the alpha 3(IV), alpha 4(IV) and
alpha 5(IV) chains of one protomer connect with the alpha 5(IV),
alpha 4(IV) and alpha 3(IV) chains of the opposite protomer,
respectively. Associates with LAMB2 at the neuromuscular junction
and in GBM (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix, basement membrane {ECO:0000255|PROSITE-ProRule:PRU00736}.
Note=Colocalizes with COL4A4 and COL4A5 in GBM, tubular basement
membrane (TBM) and synaptic basal lamina (BL). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Alpha 3 and alpha 4 type IV collagens are
colocalized and present in kidney, eye, basement membranes of lens
capsule, cochlea, lung, skeletal muscle, aorta, synaptic fibers,
fetal kidney and fetal lung. PubMed:8083201 reports similar levels
of expression of alpha 3 and alpha 4 type IV collagens in kidney,
but PubMed:7523402 reports that in kidney levels of alpha 3 type
IV collagen are significantly lower than those of alpha 4 type IV
collagen. Highest levels of expression of alpha 4 type IV collagen
are detected in kidney, calvaria, neuroretina and cardiac muscle.
Lower levels of expression are observed in brain, lung and thymus,
and no expression is detected in choroid plexus, liver, adrenal,
pancreas, ileum or skin. {ECO:0000269|PubMed:7523402,
ECO:0000269|PubMed:8083201}.
-!- 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}.
-!- DISEASE: Alport syndrome, autosomal recessive (APSAR)
[MIM:203780]: A syndrome characterized by progressive
glomerulonephritis, glomerular basement membrane defects, renal
failure, sensorineural deafness and specific eye abnormalities
(lenticonous and macular flecks). The disorder shows considerable
heterogeneity in that families differ in the age of end-stage
renal disease and the occurrence of deafness.
{ECO:0000269|PubMed:7987396, ECO:0000269|PubMed:9792860}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Hematuria, benign familial (BFH) [MIM:141200]: An
autosomal dominant condition characterized by non-progressive
isolated microscopic hematuria that does not result in renal
failure. It is characterized pathologically by thinning of the
glomerular basement membrane. {ECO:0000269|PubMed:11961012,
ECO:0000269|PubMed:12631110, ECO:0000269|PubMed:8787673}. Note=The
disease is caused by mutations 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; X81053; CAA56943.1; -; mRNA.
EMBL; Y17397; CAA76763.1; -; Genomic_DNA.
EMBL; Y17398; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17399; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17400; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17401; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17402; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17403; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17404; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17405; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17406; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17407; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17408; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17409; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17410; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17411; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17412; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17413; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17427; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17426; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17414; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17415; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17416; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17417; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17418; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17419; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17420; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17443; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17442; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17441; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17440; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17439; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17438; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17437; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17436; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17435; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17434; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17433; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17432; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17431; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17430; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17429; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17428; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17421; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17422; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17423; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17424; CAA76763.1; JOINED; Genomic_DNA.
EMBL; Y17425; CAA76763.1; JOINED; Genomic_DNA.
EMBL; AC073149; AAY24061.1; -; Genomic_DNA.
EMBL; AC079235; AAY14670.1; -; Genomic_DNA.
EMBL; AB008496; BAA25065.1; -; Genomic_DNA.
EMBL; D17391; BAA04214.1; -; mRNA.
CCDS; CCDS42828.1; -.
PIR; A55360; CGHU1B.
RefSeq; NP_000083.3; NM_000092.4.
RefSeq; XP_005246338.1; XM_005246281.3.
UniGene; Hs.591645; -.
ProteinModelPortal; P53420; -.
SMR; P53420; -.
BioGrid; 107683; 1.
IntAct; P53420; 1.
STRING; 9606.ENSP00000379866; -.
ChEMBL; CHEMBL2364188; -.
iPTMnet; P53420; -.
PhosphoSitePlus; P53420; -.
BioMuta; COL4A4; -.
DMDM; 259016360; -.
EPD; P53420; -.
PaxDb; P53420; -.
PeptideAtlas; P53420; -.
PRIDE; P53420; -.
Ensembl; ENST00000396625; ENSP00000379866; ENSG00000081052.
GeneID; 1286; -.
KEGG; hsa:1286; -.
UCSC; uc061teu.1; human.
CTD; 1286; -.
DisGeNET; 1286; -.
EuPathDB; HostDB:ENSG00000081052.11; -.
GeneCards; COL4A4; -.
GeneReviews; COL4A4; -.
H-InvDB; HIX0030014; -.
HGNC; HGNC:2206; COL4A4.
MalaCards; COL4A4; -.
MIM; 120131; gene.
MIM; 141200; phenotype.
MIM; 203780; phenotype.
neXtProt; NX_P53420; -.
OpenTargets; ENSG00000081052; -.
Orphanet; 88918; Autosomal dominant Alport syndrome.
Orphanet; 88919; Autosomal recessive Alport syndrome.
Orphanet; 97562; Benign familial hematuria.
PharmGKB; PA26721; -.
eggNOG; KOG3544; Eukaryota.
eggNOG; ENOG410YAVF; LUCA.
GeneTree; ENSGT00840000129673; -.
HOGENOM; HOG000085652; -.
HOVERGEN; HBG004933; -.
InParanoid; P53420; -.
KO; K06237; -.
OMA; CNVTYPG; -.
OrthoDB; EOG091G0613; -.
PhylomeDB; P53420; -.
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-419037; NCAM1 interactions.
Reactome; R-HSA-8948216; Collagen chain trimerization.
SIGNOR; P53420; -.
ChiTaRS; COL4A4; human.
GeneWiki; COL4A4; -.
GenomeRNAi; 1286; -.
PRO; PR:P53420; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000081052; -.
CleanEx; HS_COL4A4; -.
Genevisible; P53420; HS.
GO; GO:0005605; C:basal lamina; IDA:UniProtKB.
GO; GO:0005587; C:collagen type IV trimer; IDA:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005201; F:extracellular matrix structural constituent; IMP:UniProtKB.
GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0032836; P:glomerular basement membrane development; IMP:UniProtKB.
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; 14.
SMART; SM00111; C4; 2.
SUPFAM; SSF56436; SSF56436; 2.
PROSITE; PS51403; NC1_IV; 1.
1: Evidence at protein level;
Alport syndrome; Basement membrane; Collagen; Complete proteome;
Deafness; Disease mutation; Disulfide bond; Extracellular matrix;
Glycoprotein; Hydroxylation; Polymorphism; Reference proteome; Repeat;
Secreted; Signal.
SIGNAL 1 38 {ECO:0000255}.
CHAIN 39 1690 Collagen alpha-4(IV) chain.
/FTId=PRO_0000005850.
DOMAIN 1465 1690 Collagen IV NC1. {ECO:0000255|PROSITE-
ProRule:PRU00736}.
REGION 39 64 7S domain.
REGION 65 1459 Triple-helical region.
MOTIF 94 96 Cell attachment site. {ECO:0000255}.
MOTIF 145 147 Cell attachment site. {ECO:0000255}.
MOTIF 189 191 Cell attachment site. {ECO:0000255}.
MOTIF 310 312 Cell attachment site. {ECO:0000255}.
MOTIF 724 726 Cell attachment site. {ECO:0000255}.
MOTIF 785 787 Cell attachment site. {ECO:0000255}.
MOTIF 989 991 Cell attachment site. {ECO:0000255}.
MOTIF 1212 1214 Cell attachment site. {ECO:0000255}.
SITE 1206 1207 Cleavage; by collagenase. {ECO:0000250}.
CARBOHYD 142 142 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 669 669 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 1480 1569 Or C-1480 with C-1566.
{ECO:0000255|PROSITE-ProRule:PRU00736}.
DISULFID 1513 1566 Or C-1513 with C-1569.
{ECO:0000255|PROSITE-ProRule:PRU00736}.
DISULFID 1525 1531 {ECO:0000255|PROSITE-ProRule:PRU00736}.
DISULFID 1588 1686 Or C-1588 with C-1683.
{ECO:0000255|PROSITE-ProRule:PRU00736}.
DISULFID 1622 1683 Or C-1622 with C-1686.
{ECO:0000255|PROSITE-ProRule:PRU00736}.
DISULFID 1634 1641 {ECO:0000255|PROSITE-ProRule:PRU00736}.
VARIANT 6 6 I -> T (in dbSNP:rs16823264).
{ECO:0000269|PubMed:11961012}.
/FTId=VAR_031622.
VARIANT 116 116 G -> E (in BFH).
{ECO:0000269|PubMed:12631110}.
/FTId=VAR_031623.
VARIANT 441 446 Missing (in APSAR).
/FTId=VAR_008148.
VARIANT 482 482 P -> S (in dbSNP:rs2229814).
{ECO:0000269|PubMed:11961012,
ECO:0000269|PubMed:12631110}.
/FTId=VAR_022069.
VARIANT 545 545 G -> A (in dbSNP:rs1800516).
{ECO:0000269|PubMed:11961012,
ECO:0000269|PubMed:9792860}.
/FTId=VAR_008149.
VARIANT 570 570 E -> Q. {ECO:0000269|PubMed:9792860}.
/FTId=VAR_008150.
VARIANT 594 594 E -> G (in dbSNP:rs35998949).
/FTId=VAR_055680.
VARIANT 670 670 V -> I (in dbSNP:rs34236495).
/FTId=VAR_055681.
VARIANT 759 759 P -> L (in dbSNP:rs36121515).
/FTId=VAR_055682.
VARIANT 897 897 G -> E (in BFH; dbSNP:rs121912860).
{ECO:0000269|PubMed:8787673}.
/FTId=VAR_001912.
VARIANT 931 931 A -> T (in dbSNP:rs75875272).
{ECO:0000269|PubMed:9792860}.
/FTId=VAR_008151.
VARIANT 960 960 G -> R (in BFH; dbSNP:rs769783985).
{ECO:0000269|PubMed:11961012,
ECO:0000269|PubMed:12631110}.
/FTId=VAR_031624.
VARIANT 999 999 G -> E (in BFH; dbSNP:rs13027659).
{ECO:0000269|PubMed:12631110}.
/FTId=VAR_031625.
VARIANT 1004 1004 P -> L (in dbSNP:rs1800517).
{ECO:0000269|PubMed:7523402,
ECO:0000269|PubMed:9792860}.
/FTId=VAR_008152.
VARIANT 1030 1030 G -> V (in APSAR).
{ECO:0000269|PubMed:9792860}.
/FTId=VAR_008153.
VARIANT 1132 1132 P -> L (in BFH).
{ECO:0000269|PubMed:12631110}.
/FTId=VAR_031626.
VARIANT 1201 1201 G -> S (in APSAR; dbSNP:rs121912858).
{ECO:0000269|PubMed:7987396}.
/FTId=VAR_001913.
VARIANT 1327 1327 V -> M (in dbSNP:rs2229813).
{ECO:0000269|PubMed:7523402,
ECO:0000269|PubMed:8365481,
ECO:0000269|PubMed:9792860}.
/FTId=VAR_031627.
VARIANT 1402 1402 P -> S. {ECO:0000269|PubMed:9792860}.
/FTId=VAR_008154.
VARIANT 1403 1403 S -> P (in dbSNP:rs3752895).
{ECO:0000269|PubMed:7523402,
ECO:0000269|PubMed:8365481,
ECO:0000269|PubMed:9792860}.
/FTId=VAR_031628.
VARIANT 1572 1572 P -> L (in APSAR; dbSNP:rs121912863).
{ECO:0000269|PubMed:9792860}.
/FTId=VAR_008155.
CONFLICT 1361 1363 GPR -> AIS (in Ref. 3; AAY24061).
{ECO:0000305}.
CONFLICT 1659 1660 LQ -> FE (in Ref. 5; BAA04214).
{ECO:0000305}.
SEQUENCE 1690 AA; 164038 MW; C55711CDF14A57DB CRC64;
MWSLHIVLMR CSFRLTKSLA TGPWSLILIL FSVQYVYGSG KKYIGPCGGR DCSVCHCVPE
KGSRGPPGPP GPQGPIGPLG APGPIGLSGE KGMRGDRGPP GAAGDKGDKG PTGVPGFPGL
DGIPGHPGPP GPRGKPGMSG HNGSRGDPGF PGGRGALGPG GPLGHPGEKG EKGNSVFILG
AVKGIQGDRG DPGLPGLPGS WGAGGPAGPT GYPGEPGLVG PPGQPGRPGL KGNPGVGVKG
QMGDPGEVGQ QGSPGPTLLV EPPDFCLYKG EKGIKGIPGM VGLPGPPGRK GESGIGAKGE
KGIPGFPGPR GDPGSYGSPG FPGLKGELGL VGDPGLFGLI GPKGDPGNRG HPGPPGVLVT
PPLPLKGPPG DPGFPGRYGE TGDVGPPGPP GLLGRPGEAC AGMIGPPGPQ GFPGLPGLPG
EAGIPGRPDS APGKPGKPGS PGLPGAPGLQ GLPGSSVIYC SVGNPGPQGI KGKVGPPGGR
GPKGEKGNEG LCACEPGPMG PPGPPGLPGR QGSKGDLGLP GWLGTKGDPG PPGAEGPPGL
PGKHGASGPP GNKGAKGDMV VSRVKGHKGE RGPDGPPGFP GQPGSHGRDG HAGEKGDPGP
PGDHEDATPG GKGFPGPLGP PGKAGPVGPP GLGFPGPPGE RGHPGVPGHP GVRGPDGLKG
QKGDTISCNV TYPGRHGPPG FDGPPGPKGF PGPQGAPGLS GSDGHKGRPG TPGTAEIPGP
PGFRGDMGDP GFGGEKGSSP VGPPGPPGSP GVNGQKGIPG DPAFGHLGPP GKRGLSGVPG
IKGPRGDPGC PGAEGPAGIP GFLGLKGPKG REGHAGFPGV PGPPGHSCER GAPGIPGQPG
LPGYPGSPGA PGGKGQPGDV GPPGPAGMKG LPGLPGRPGA HGPPGLPGIP GPFGDDGLPG
PPGPKGPRGL PGFPGFPGER GKPGAEGCPG AKGEPGEKGM SGLPGDRGLR GAKGAIGPPG
DEGEMAIISQ KGTPGEPGPP GDDGFPGERG DKGTPGMQGR RGEPGRYGPP GFHRGEPGEK
GQPGPPGPPG PPGSTGLRGF IGFPGLPGDQ GEPGSPGPPG FSGIDGARGP KGNKGDPASH
FGPPGPKGEP GSPGCPGHFG ASGEQGLPGI QGPRGSPGRP GPPGSSGPPG CPGDHGMPGL
RGQPGEMGDP GPRGLQGDPG IPGPPGIKGP SGSPGLNGLH GLKGQKGTKG ASGLHDVGPP
GPVGIPGLKG ERGDPGSPGI SPPGPRGKKG PPGPPGSSGP PGPAGATGRA PKDIPDPGPP
GDQGPPGPDG PRGAPGPPGL PGSVDLLRGE PGDCGLPGPP GPPGPPGPPG YKGFPGCDGK
DGQKGPVGFP GPQGPHGFPG PPGEKGLPGP PGRKGPTGLP GPRGEPGPPA DVDDCPRIPG
LPGAPGMRGP EGAMGLPGMR GPSGPGCKGE PGLDGRRGVD GVPGSPGPPG RKGDTGEDGY
PGGPGPPGPI GDPGPKGFGP GYLGGFLLVL HSQTDQEPTC PLGMPRLWTG YSLLYLEGQE
KAHNQDLGLA GSCLPVFSTL PFAYCNIHQV CHYAQRNDRS YWLASAAPLP MMPLSEEAIR
PYVSRCAVCE APAQAVAVHS QDQSIPPCPQ TWRSLWIGYS FLMHTGAGDQ GGGQALMSPG
SCLEDFRAAP FLECQGRQGT CHFFANKYSF WLTTVKADLQ FSSAPAPDTL KESQAQRQKI
SRCQVCVKYS


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