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Collagen alpha-1(XVIII) chain [Cleaved into: Endostatin]

 COIA1_HUMAN             Reviewed;        1754 AA.
P39060; A8MVI4; Q58EX6; Q6RZ39; Q6RZ40; Q6RZ41; Q8N4S4; Q8WXI5;
Q96T70; Q9UK38; Q9Y6Q7; Q9Y6Q8;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 5.
22-NOV-2017, entry version 193.
RecName: Full=Collagen alpha-1(XVIII) chain;
Contains:
RecName: Full=Endostatin;
Contains:
RecName: Full=Non-collagenous domain 1;
Short=NC1;
Flags: Precursor;
Name=COL18A1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), AND VARIANT ILE-1076.
PubMed=9503365; DOI=10.1016/S0945-053X(98)90003-8;
Saarela J., Ylikarppa R., Rehn M., Purmonen S., Pihlajaniemi T.;
"Complete primary structure of two variant forms of human type XVIII
collagen and tissue-specific differences in the expression of the
corresponding transcripts.";
Matrix Biol. 16:319-328(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3), AND VARIANTS
ILE-1076 AND ASN-1675.
PubMed=14614989; DOI=10.1016/S0945-053X(03)00073-8;
Elamaa H., Snellman A., Rehn M., Autio-Harmainen H., Pihlajaniemi T.;
"Characterization of the human type XVIII collagen gene and
proteolytic processing and tissue location of the variant containing a
frizzled motif.";
Matrix Biol. 22:427-442(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10830953; DOI=10.1038/35012518;
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
Lehrach H., Reinhardt R., Yaspo M.-L.;
"The DNA sequence of human chromosome 21.";
Nature 405:311-319(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
ILE-1076.
TISSUE=Kidney, and PNS;
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1069-1754, AND VARIANT ARG-1121.
PubMed=8188291; DOI=10.1006/geno.1994.1098;
Oh S.P., Warman M.L., Seldin M.F., Cheng S., Knoll J.H., Timmons S.,
Olsen B.R.;
"Cloning of cDNA and genomic DNA encoding human type XVIII collagen
and localization of the alpha 1(XVIII) collagen gene to mouse
chromosome 10 and human chromosome 21.";
Genomics 19:494-499(1994).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1568-1754.
PubMed=11517600;
Feng Y., Cui L.B., Liu C.X., Ma Q.J.;
"Inhibition effect in vitro of purified endostatin expressed in Pichia
pastoris.";
Sheng Wu Gong Cheng Xue Bao 17:278-282(2001).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1572-1754, AND VARIANT ASN-1675.
TISSUE=Placenta;
Zhi-Yong H., Biao L., Wei-Jie Z., Xiang-Fu W.;
"Cloning and expression of human endostatin gene in Escherichia
coli.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1642-1743.
Deininger M.H., Trautmann K., Schluesener H.J.;
"Endostatin promotes delayed secondary damage following traumatic
brain injury.";
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
[9]
FUNCTION.
PubMed=9459295;
Staendker L., Schrader M., Kanse S.M., Juergens M., Forssmann W.G.,
Preissner K.T.;
"Isolation and characterization of the circulating form of human
endostatin.";
FEBS Lett. 420:129-133(1997).
[10]
GLYCOSYLATION AT THR-1567, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
PubMed=10441114; DOI=10.1021/bi990787+;
John H., Preissner K.T., Forssmann W.G., Staendker L.;
"Novel glycosylated forms of human plasma endostatin and circulating
endostatin-related fragments of collagen XV.";
Biochemistry 38:10217-10224(1999).
[11]
PROTEOLYTIC CLEAVAGE.
PubMed=10626789;
Wen W., Moses M.A., Wiederschain D., Arbiser J.L., Folkman J.;
"The generation of endostatin is mediated by elastase.";
Cancer Res. 59:6052-6056(1999).
[12]
FUNCTION, AND SUBUNIT.
PubMed=11257123;
Kuo C.J., LaMontagne K.R. Jr., Garcia-Cardena G., Ackley B.D.,
Kalman D., Park S., Christofferson R., Kamihara J., Ding Y.H.,
Lo K.M., Gillies S., Folkman J., Mulligan R.C., Javaherian K.;
"Oligomerization-dependent regulation of motility and morphogenesis by
the collagen XVIII NC1/endostatin domain.";
J. Cell Biol. 152:1233-1246(2001).
[13]
BIOTECHNOLOGY.
PubMed=17644065; DOI=10.1016/j.bbrc.2007.06.155;
Ling Y., Yang Y., Lu N., You Q.D., Wang S., Gao Y., Chen Y., Guo Q.L.;
"Endostar, a novel recombinant human endostatin, exerts antiangiogenic
effect via blocking VEGF-induced tyrosine phosphorylation of KDR/Flk-1
of endothelial cells.";
Biochem. Biophys. Res. Commun. 361:79-84(2007).
[14]
INVOLVEMENT IN KNO1.
PubMed=23667181; DOI=10.1136/jmedgenet-2013-101755;
Aldahmesh M.A., Khan A.O., Mohamed J.Y., Levin A.V., Wuthisiri W.,
Lynch S., McCreery K., Alkuraya F.S.;
"No evidence for locus heterogeneity in Knobloch syndrome.";
J. Med. Genet. 50:565-566(2013).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-696, 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).
[16]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1572-1749, AND ZINC-BINDING
SITE.
PubMed=9724722; DOI=10.1073/pnas.95.18.10443;
Ding Y.-H., Javaherian K., Lo K.-M., Chopra R., Boehm T.,
Lanciotti J., Harris B.A., Li Y., Shapiro R., Hohenester E., Timpl R.,
Folkman J., Wiley D.C.;
"Zinc-dependent dimers observed in crystals of human endostatin.";
Proc. Natl. Acad. Sci. U.S.A. 95:10443-10448(1998).
[17]
INVOLVEMENT IN KNO1, AND FUNCTION.
PubMed=10942434; DOI=10.1093/hmg/9.13.2051;
Sertie A.L., Sossi V., Camargo A.A., Zatz M., Brahe C.,
Passos-Bueno M.R.;
"Collagen XVIII, containing an endogenous inhibitor of angiogenesis
and tumor growth, plays a critical role in the maintenance of retinal
structure and in neural tube closure.";
Hum. Mol. Genet. 9:2051-2058(2000).
[18]
VARIANTS ILE-1076 AND ASN-1675.
PubMed=11606364;
Iughetti P., Suzuki O., Godoi P.H., Alves V.A., Sertie A.L.,
Zorick T., Soares F., Camargo A.A., Moreira E.S., di Loreto C.,
Moreira-Filho C.A., Simpson A., Oliva G., Passos-Bueno M.R.;
"A polymorphism in endostatin, an angiogenesis inhibitor, predisposes
for the development of prostatic adenocarcinoma.";
Cancer Res. 61:7375-7378(2001).
[19]
VARIANTS LEU-49; ARG-111; ILE-1076 AND ARG-1121, AND CHARACTERIZATION
OF VARIANT ASN-1675.
PubMed=14695535; DOI=10.1002/humu.10284;
Menzel O., Bekkeheien R.C.J., Reymond A., Fukai N., Boye E.,
Kosztolanyi G., Aftimos S., Deutsch S., Scott H.S., Olsen B.R.,
Antonarakis S.E., Guipponi M.;
"Knobloch syndrome: novel mutations in COL18A1, evidence for genetic
heterogeneity, and a functionally impaired polymorphism in
endostatin.";
Hum. Mutat. 23:77-84(2004).
[20]
VARIANT [LARGE SCALE ANALYSIS] ARG-1121.
PubMed=18987736; DOI=10.1038/nature07485;
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J.,
Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C.,
Graubert T.A., DiPersio J.F., Wilson R.K.;
"DNA sequencing of a cytogenetically normal acute myeloid leukaemia
genome.";
Nature 456:66-72(2008).
-!- FUNCTION: Probably plays a major role in determining the retinal
structure as well as in the closure of the neural tube.
{ECO:0000269|PubMed:10942434}.
-!- FUNCTION: Non-collagenous domain 1: May regulate extracellular
matrix-dependent motility and morphogenesis of endothelial and
non-endothelial cells; the function requires homotrimerization and
implicates MAPK signaling. {ECO:0000269|PubMed:11257123}.
-!- FUNCTION: Endostatin: Potently inhibits endothelial cell
proliferation and angiogenesis (PubMed:9459295). May inhibit
angiogenesis by binding to the heparan sulfate proteoglycans
involved in growth factor signaling (By similarity). Inhibits
VEGFA-induced endothelial cell proliferation and migration. Seems
to inhibit VEGFA-mediated signaling by blocking the interaction of
VEGFA to its receptor KDR/VEGFR2. Modulates endothelial cell
migration in an integrin-dependent manner implicating integrin
ITGA5:ITGB1 and to a lesser extent ITGAV:ITGB3 and ITGAV:ITGB5 (By
similarity). May negatively regulate the activity of homotrimeric
non-collagenous domain 1 (PubMed:11257123).
{ECO:0000250|UniProtKB:P39061, ECO:0000269|PubMed:11257123,
ECO:0000269|PubMed:9459295}.
-!- SUBUNIT: Non-collagenous domain 1 forms homotrimers. Endostatin is
monomeric (PubMed:11257123). Recombinant non-collagenous domain 1
has stronger affinity to NID1, HSPG2 and laminin-1:NID1 complex
and lower affinity to FBLN1 and FBLN2 than endostatin. Endostatin
interacts with KDR/VEGFR2. Endostatin interacts with the
ITGA5:ITGB1 complex (By similarity).
{ECO:0000250|UniProtKB:P39061, ECO:0000269|PubMed:11257123}.
-!- INTERACTION:
P05067:APP; NbExp=2; IntAct=EBI-2566375, EBI-821758;
P19338:NCL; NbExp=12; IntAct=EBI-2566375, EBI-346967;
Q15113:PCOLCE; NbExp=4; IntAct=EBI-2566375, EBI-8869614;
P21980:TGM2; NbExp=2; IntAct=EBI-2566375, EBI-727668;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000250}. Secreted, extracellular space, extracellular
matrix, basement membrane {ECO:0000250|UniProtKB:P39061}.
-!- SUBCELLULAR LOCATION: Non-collagenous domain 1: Secreted,
extracellular space, extracellular matrix, basement membrane
{ECO:0000250|UniProtKB:P39061}. Secreted
{ECO:0000250|UniProtKB:P39061}.
-!- SUBCELLULAR LOCATION: Endostatin: Secreted
{ECO:0000269|PubMed:10441114}. Secreted, extracellular space,
extracellular matrix, basement membrane {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=3;
Name=1; Synonyms=NC1-728;
IsoId=P39060-3; Sequence=Displayed;
Note=Produced by alternative promoter usage.;
Name=2; Synonyms=Long, NC-493;
IsoId=P39060-1; Sequence=VSP_023131;
Note=Produced by alternative splicing of isoform 1.;
Name=3; Synonyms=Short, NC1-303;
IsoId=P39060-2; Sequence=VSP_023130, VSP_023132;
Note=Produced by alternative promoter usage.;
-!- TISSUE SPECIFICITY: Present in multiple organs with highest levels
in liver, lung and kidney.
-!- PTM: Prolines at the third position of the tripeptide repeating
unit (G-X-Y) of the triple-helical regions are hydroxylated.
-!- PTM: Circulating endostatins are found as sialoglycoprotein and
asialoglycoprotein structures. {ECO:0000269|PubMed:10441114}.
-!- PTM: Undergoes proteolytic processing by cathepsin-L and elastase-
like proteases to generate both NC1 trimers and endostatin
monomers (PubMed:10626789). In vitro, several proteolytic cleavage
sites in the non-collagenous domain 1 hinge region generating
different endostatin-like peptides are reported (By similarity).
{ECO:0000250|UniProtKB:P39061, ECO:0000269|PubMed:10626789}.
-!- POLYMORPHISM: There is an association between a polymorphism in
position 1675 and prostate cancer. Heterozygous Asn-1675
individuals have a 2.5 times increased chance of developing
prostate cancer as compared with homozygous Asp-1675 individuals.
-!- DISEASE: Knobloch syndrome 1 (KNO1) [MIM:267750]: A developmental
disorder primarily characterized by typical eye abnormalities,
including high myopia, cataracts, dislocated lens, vitreoretinal
degeneration, and retinal detachment, with occipital skull
defects, which can range from occipital encephalocele to occult
cutis aplasia. {ECO:0000269|PubMed:10942434,
ECO:0000269|PubMed:23667181}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- BIOTECHNOLOGY: Endostatin is available under the name Endostar
(Jiangsu Simcere Pharmaceutical) for the treatment of non-small-
cell lung cancer. {ECO:0000269|PubMed:17644065, ECO:0000305}.
-!- SIMILARITY: Belongs to the multiplexin collagen family.
{ECO:0000305}.
-!- CAUTION: Non-collagenous domain 1 seems to be the predominant
tissue form from which endostatin is cleaved. However, the
proteolytic cleavage site to generate non-collagenous domain 1 is
not known. Soluble recombinant non-collagenous domain 1 amenable
to biochemical studies has been used instead. {ECO:0000305}.
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EMBL; AF018081; AAC39658.1; -; mRNA.
EMBL; AF018082; AAC39659.1; -; mRNA.
EMBL; AY484971; AAR83296.1; -; Genomic_DNA.
EMBL; AY484968; AAR83296.1; JOINED; Genomic_DNA.
EMBL; AY484969; AAR83296.1; JOINED; Genomic_DNA.
EMBL; AY484970; AAR83296.1; JOINED; Genomic_DNA.
EMBL; AY484971; AAR83297.1; -; Genomic_DNA.
EMBL; AY484968; AAR83297.1; JOINED; Genomic_DNA.
EMBL; AY484969; AAR83297.1; JOINED; Genomic_DNA.
EMBL; AY484970; AAR83297.1; JOINED; Genomic_DNA.
EMBL; AY484971; AAR83298.1; -; Genomic_DNA.
EMBL; AY484967; AAR83298.1; JOINED; Genomic_DNA.
EMBL; AY484969; AAR83298.1; JOINED; Genomic_DNA.
EMBL; AY484970; AAR83298.1; JOINED; Genomic_DNA.
EMBL; AL163302; CAB90482.1; -; Genomic_DNA.
EMBL; BX322561; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC033715; AAH33715.1; -; mRNA.
EMBL; BC063833; AAH63833.1; -; mRNA.
EMBL; L22548; AAA51864.1; -; mRNA.
EMBL; AF416592; AAL37720.1; -; mRNA.
EMBL; AF184060; AAF01310.1; -; mRNA.
EMBL; AF333247; AAK50626.1; -; mRNA.
RefSeq; NP_085059.2; NM_030582.3.
RefSeq; NP_569711.2; NM_130444.2.
RefSeq; NP_569712.2; NM_130445.3.
UniGene; Hs.517356; -.
PDB; 1BNL; X-ray; 2.90 A; A/B/C/D=1572-1749.
PDB; 3HON; X-ray; 3.00 A; A=1441-1496.
PDB; 3HSH; X-ray; 1.80 A; A/B/C/D/E/F=1441-1496.
PDBsum; 1BNL; -.
PDBsum; 3HON; -.
PDBsum; 3HSH; -.
ProteinModelPortal; P39060; -.
SMR; P39060; -.
BioGrid; 123311; 33.
CORUM; P39060; -.
IntAct; P39060; 16.
STRING; 9606.ENSP00000347665; -.
ChEMBL; CHEMBL2364188; -.
iPTMnet; P39060; -.
PhosphoSitePlus; P39060; -.
UniCarbKB; P39060; -.
BioMuta; COL18A1; -.
DMDM; 215274264; -.
EPD; P39060; -.
PaxDb; P39060; -.
PeptideAtlas; P39060; -.
PRIDE; P39060; -.
Ensembl; ENST00000355480; ENSP00000347665; ENSG00000182871. [P39060-1]
Ensembl; ENST00000359759; ENSP00000352798; ENSG00000182871. [P39060-3]
Ensembl; ENST00000400337; ENSP00000383191; ENSG00000182871. [P39060-2]
GeneID; 80781; -.
KEGG; hsa:80781; -.
UCSC; uc062awf.1; human. [P39060-3]
CTD; 80781; -.
DisGeNET; 80781; -.
EuPathDB; HostDB:ENSG00000182871.14; -.
GeneCards; COL18A1; -.
HGNC; HGNC:2195; COL18A1.
HPA; CAB001961; -.
HPA; HPA011025; -.
HPA; HPA036104; -.
MalaCards; COL18A1; -.
MIM; 120328; gene.
MIM; 267750; phenotype.
neXtProt; NX_P39060; -.
OpenTargets; ENSG00000182871; -.
Orphanet; 1571; Knobloch syndrome.
PharmGKB; PA26711; -.
eggNOG; KOG3546; Eukaryota.
eggNOG; ENOG410XQ04; LUCA.
GeneTree; ENSGT00710000106713; -.
HOVERGEN; HBG053241; -.
InParanoid; P39060; -.
KO; K06823; -.
OMA; AFVGQWT; -.
OrthoDB; EOG091G013X; -.
PhylomeDB; P39060; -.
TreeFam; TF315821; -.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-3000157; Laminin interactions.
Reactome; R-HSA-8948216; Collagen chain trimerization.
SIGNOR; P39060; -.
ChiTaRS; COL18A1; human.
EvolutionaryTrace; P39060; -.
GeneWiki; Collagen,_type_XVIII,_alpha_1; -.
GenomeRNAi; 80781; -.
PRO; PR:P39060; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000182871; -.
ExpressionAtlas; P39060; baseline and differential.
Genevisible; P39060; HS.
GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
GO; GO:0005581; C:collagen 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; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
GO; GO:0001886; P:endothelial cell morphogenesis; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0051599; P:response to hydrostatic pressure; IEA:Ensembl.
GO; GO:0007601; P:visual perception; TAS:ProtInc.
CDD; cd07455; CRD_Collagen_XVIII; 1.
CDD; cd00247; Endostatin-like; 1.
Gene3D; 1.10.2000.10; -; 1.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR008160; Collagen.
InterPro; IPR035523; Collagen_XVIII_Fz.
InterPro; IPR010515; Collagenase_NC10/endostatin.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR010363; DUF959_COL18_N.
InterPro; IPR020067; Frizzled_dom.
InterPro; IPR036790; Frizzled_dom_sf.
InterPro; IPR001791; Laminin_G.
Pfam; PF01391; Collagen; 5.
Pfam; PF06121; DUF959; 1.
Pfam; PF06482; Endostatin; 1.
Pfam; PF01392; Fz; 1.
SMART; SM00063; FRI; 1.
SMART; SM00210; TSPN; 1.
SUPFAM; SSF49899; SSF49899; 1.
SUPFAM; SSF56436; SSF56436; 1.
SUPFAM; SSF63501; SSF63501; 1.
PROSITE; PS50038; FZ; 1.
1: Evidence at protein level;
3D-structure; Alternative promoter usage; Alternative splicing;
Basement membrane; Cell adhesion; Collagen; Complete proteome;
Disulfide bond; Extracellular matrix; Glycoprotein; Hydroxylation;
Metal-binding; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; Secreted; Signal; Zinc.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 1754 Collagen alpha-1(XVIII) chain.
/FTId=PRO_0000005793.
CHAIN 1572 1754 Endostatin.
/FTId=PRO_0000005794.
CHAIN ? 1754 Non-collagenous domain 1.
/FTId=PRO_0000441861.
DOMAIN 329 446 FZ. {ECO:0000255|PROSITE-
ProRule:PRU00090}.
DOMAIN 456 644 Laminin G-like.
REGION 645 751 Nonhelical region 1 (NC1).
REGION 752 785 Triple-helical region 1 (COL1).
REGION 786 795 Nonhelical region 2 (NC2).
REGION 796 875 Triple-helical region 2 (COL2).
REGION 876 899 Nonhelical region 3 (NC3).
REGION 900 1021 Triple-helical region 3 (COL3).
REGION 1022 1044 Nonhelical region 4 (NC4).
REGION 1045 1127 Triple-helical region 4 (COL4).
REGION 1128 1141 Nonhelical region 5 (NC5).
REGION 1142 1183 Triple-helical region 5 (COL5).
REGION 1184 1196 Nonhelical region 6 (NC6).
REGION 1197 1269 Triple-helical region 6 (COL6).
REGION 1270 1279 Nonhelical region 7 (NC7).
REGION 1280 1312 Triple-helical region 7 (COL7).
REGION 1313 1324 Nonhelical region 8 (NC8).
REGION 1325 1346 Triple-helical region 8 (COL8).
REGION 1347 1353 Nonhelical region 9 (NC9).
REGION 1354 1411 Triple-helical region 9 (COL9).
REGION 1412 1424 Nonhelical region 10 (NC10).
REGION 1425 1442 Triple-helical region 10 (COL10).
REGION 1443 1754 Nonhelical region 11 (NC11).
REGION 1456 1501 Non-collagenous domain 1 association
domain. {ECO:0000250|UniProtKB:P39061}.
REGION 1502 1571 Non-collagenous domain 1 hinge region.
{ECO:0000250|UniProtKB:P39061}.
MOTIF 1330 1332 Cell attachment site. {ECO:0000255}.
METAL 1572 1572 Zinc.
METAL 1574 1574 Zinc.
METAL 1582 1582 Zinc.
METAL 1647 1647 Zinc.
MOD_RES 696 696 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
CARBOHYD 68 68 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 129 129 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 164 164 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 926 926 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1567 1567 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:10441114}.
/FTId=CAR_000150.
DISULFID 334 397 {ECO:0000255|PROSITE-ProRule:PRU00090}.
DISULFID 344 390 {ECO:0000255|PROSITE-ProRule:PRU00090}.
DISULFID 381 419 {ECO:0000255|PROSITE-ProRule:PRU00090}.
DISULFID 408 443 {ECO:0000255|PROSITE-ProRule:PRU00090}.
DISULFID 412 432 {ECO:0000255|PROSITE-ProRule:PRU00090}.
DISULFID 1604 1744 {ECO:0000255|PROSITE-ProRule:PRU00090}.
DISULFID 1706 1736 {ECO:0000255|PROSITE-ProRule:PRU00090}.
VAR_SEQ 1 415 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9503365}.
/FTId=VSP_023130.
VAR_SEQ 216 450 Missing (in isoform 2).
{ECO:0000303|PubMed:9503365}.
/FTId=VSP_023131.
VAR_SEQ 416 450 QDACWSRLGGGRLPVACASLPTQEDGYCVLIGPAA -> MA
PRCPWPWPRRRRLLDVLAPLVLLLGVRAASAEP (in
isoform 3). {ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9503365}.
/FTId=VSP_023132.
VARIANT 49 49 Q -> L (in dbSNP:rs61735029).
{ECO:0000269|PubMed:14695535}.
/FTId=VAR_018053.
VARIANT 111 111 G -> R (in dbSNP:rs114139997).
{ECO:0000269|PubMed:14695535}.
/FTId=VAR_018054.
VARIANT 288 288 A -> T (in dbSNP:rs11702494).
/FTId=VAR_059232.
VARIANT 379 379 T -> M (in dbSNP:rs8133886).
/FTId=VAR_061115.
VARIANT 1076 1076 V -> I (in dbSNP:rs62000962).
{ECO:0000269|PubMed:11606364,
ECO:0000269|PubMed:14614989,
ECO:0000269|PubMed:14695535,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9503365}.
/FTId=VAR_018055.
VARIANT 1121 1121 P -> R (in dbSNP:rs79980197).
{ECO:0000269|PubMed:14695535,
ECO:0000269|PubMed:18987736,
ECO:0000269|PubMed:8188291}.
/FTId=VAR_018056.
VARIANT 1195 1195 Q -> H (in dbSNP:rs2230693).
/FTId=VAR_059233.
VARIANT 1675 1675 D -> N (functional polymorphism;
associated with increased risk for
prostate cancer; may cause Knobloch
syndrome in compound heterozygotes
carrying a frameshift/truncating
mutation; results in decreased affinity
for laminin; dbSNP:rs12483377).
{ECO:0000269|PubMed:11606364,
ECO:0000269|PubMed:14614989,
ECO:0000269|PubMed:14695535,
ECO:0000269|Ref.7}.
/FTId=VAR_012709.
CONFLICT 299 299 R -> K (in Ref. 2; AAR83296).
{ECO:0000305}.
CONFLICT 663 663 S -> F (in Ref. 1; AAC39658/AAC39659).
{ECO:0000305}.
CONFLICT 1112 1112 V -> L (in Ref. 5; AAA51864).
{ECO:0000305}.
CONFLICT 1147 1147 P -> R (in Ref. 5; AAA51864).
{ECO:0000305}.
CONFLICT 1168 1168 R -> L (in Ref. 5; AAA51864).
{ECO:0000305}.
CONFLICT 1210 1210 P -> L (in Ref. 5; AAA51864).
{ECO:0000305}.
CONFLICT 1299 1299 A -> P (in Ref. 5; AAA51864).
{ECO:0000305}.
CONFLICT 1319 1319 L -> K (in Ref. 5; AAA51864).
{ECO:0000305}.
CONFLICT 1355 1355 P -> A (in Ref. 5; AAA51864).
{ECO:0000305}.
CONFLICT 1358 1358 P -> A (in Ref. 5; AAA51864).
{ECO:0000305}.
CONFLICT 1362 1364 Missing (in Ref. 1; AAC39658/AAC39659, 2;
AAR83296/AAR83297/AAR83298, 4; AAH33715/
AAH63833 and 5; AAA51864). {ECO:0000305}.
CONFLICT 1444 1444 G -> GQ (in Ref. 5; AAA51864).
{ECO:0000305}.
CONFLICT 1542 1542 R -> G (in Ref. 5; AAA51864).
{ECO:0000305}.
CONFLICT 1552 1552 A -> G (in Ref. 5; AAA51864).
{ECO:0000305}.
CONFLICT 1561 1562 LR -> CG (in Ref. 5; AAA51864).
{ECO:0000305}.
CONFLICT 1681 1681 R -> T (in Ref. 7; AAF01310).
{ECO:0000305}.
CONFLICT 1685 1685 W -> R (in Ref. 8; AAK50626).
{ECO:0000305}.
CONFLICT 1721 1721 S -> Y (in Ref. 7; AAF01310).
{ECO:0000305}.
CONFLICT 1736 1736 C -> S (in Ref. 8; AAK50626).
{ECO:0000305}.
STRAND 1445 1450 {ECO:0000244|PDB:3HSH}.
HELIX 1451 1457 {ECO:0000244|PDB:3HSH}.
HELIX 1458 1460 {ECO:0000244|PDB:3HSH}.
STRAND 1466 1469 {ECO:0000244|PDB:3HSH}.
TURN 1470 1473 {ECO:0000244|PDB:3HSH}.
STRAND 1474 1479 {ECO:0000244|PDB:3HSH}.
STRAND 1482 1486 {ECO:0000244|PDB:3HSH}.
STRAND 1488 1493 {ECO:0000244|PDB:3HSH}.
STRAND 1581 1585 {ECO:0000244|PDB:1BNL}.
HELIX 1597 1610 {ECO:0000244|PDB:1BNL}.
STRAND 1617 1621 {ECO:0000244|PDB:1BNL}.
HELIX 1629 1631 {ECO:0000244|PDB:1BNL}.
HELIX 1634 1636 {ECO:0000244|PDB:1BNL}.
STRAND 1649 1652 {ECO:0000244|PDB:1BNL}.
HELIX 1654 1657 {ECO:0000244|PDB:1BNL}.
HELIX 1679 1681 {ECO:0000244|PDB:1BNL}.
STRAND 1689 1691 {ECO:0000244|PDB:1BNL}.
HELIX 1706 1709 {ECO:0000244|PDB:1BNL}.
STRAND 1716 1722 {ECO:0000244|PDB:1BNL}.
HELIX 1723 1725 {ECO:0000244|PDB:1BNL}.
STRAND 1727 1729 {ECO:0000244|PDB:1BNL}.
STRAND 1732 1735 {ECO:0000244|PDB:1BNL}.
STRAND 1743 1747 {ECO:0000244|PDB:1BNL}.
SEQUENCE 1754 AA; 178188 MW; 23A327DCBD3B328D CRC64;
MAPYPCGCHI LLLLFCCLAA ARANLLNLNW LWFNNEDTSH AATTIPEPQG PLPVQPTADT
TTHVTPRNGS TEPATAPGSP EPPSELLEDG QDTPTSAESP DAPEENIAGV GAEILNVAKG
IRSFVQLWND TVPTESLARA ETLVLETPVG PLALAGPSST PQENGTTLWP SRGIPSSPGA
HTTEAGTLPA PTPSPPSLGR PWAPLTGPSV PPPSSGRASL SSLLGGAPPW GSLQDPDSQG
LSPAAAAPSQ QLQRPDVRLR TPLLHPLVMG SLGKHAAPSA FSSGLPGALS QVAVTTLTRD
SGAWVSHVAN SVGPGLANNS ALLGADPEAP AGRCLPLPPS LPVCGHLGIS RFWLPNHLHH
ESGEQVRAGA RAWGGLLQTH CHPFLAWFFC LLLVPPCGSV PPPAPPPCCQ FCEALQDACW
SRLGGGRLPV ACASLPTQED GYCVLIGPAA ERISEEVGLL QLLGDPPPQQ VTQTDDPDVG
LAYVFGPDAN SGQVARYHFP SLFFRDFSLL FHIRPATEGP GVLFAITDSA QAMVLLGVKL
SGVQDGHQDI SLLYTEPGAG QTHTAASFRL PAFVGQWTHL ALSVAGGFVA LYVDCEEFQR
MPLARSSRGL ELEPGAGLFV AQAGGADPDK FQGVIAELKV RRDPQVSPMH CLDEEGDDSD
GASGDSGSGL GDARELLREE TGAALKPRLP APPPVTTPPL AGGSSTEDSR SEEVEEQTTV
ASLGAQTLPG SDSVSTWDGS VRTPGGRVKE GGLKGQKGEP GVPGPPGRAG PPGSPCLPGP
PGLPCPVSPL GPAGPALQTV PGPQGPPGPP GRDGTPGRDG EPGDPGEDGK PGDTGPQGFP
GTPGDVGPKG DKGDPGVGER GPPGPQGPPG PPGPSFRHDK LTFIDMEGSG FGGDLEALRG
PRGFPGPPGP PGVPGLPGEP GRFGVNSSDV PGPAGLPGVP GREGPPGFPG LPGPPGPPGR
EGPPGRTGQK GSLGEAGAPG HKGSKGAPGP AGARGESGLA GAPGPAGPPG PPGPPGPPGP
GLPAGFDDME GSGGPFWSTA RSADGPQGPP GLPGLKGDPG VPGLPGAKGE VGADGVPGFP
GLPGREGIAG PQGPKGDRGS RGEKGDPGKD GVGQPGLPGP PGPPGPVVYV SEQDGSVLSV
PGPEGRPGFA GFPGPAGPKG NLGSKGERGS PGPKGEKGEP GSIFSPDGGA LGPAQKGAKG
EPGFRGPPGP YGRPGYKGEI GFPGRPGRPG MNGLKGEKGE PGDASLGFGM RGMPGPPGPP
GPPGPPGTPV YDSNVFAESS RPGPPGLPGN QGPPGPKGAK GEVGPPGPPG QFPFDFLQLE
AEMKGEKGDR GDAGQKGERG EPGGGGFFGS SLPGPPGPPG PPGPRGYPGI PGPKGESIRG
QPGPPGPQGP PGIGYEGRQG PPGPPGPPGP PSFPGPHRQT ISVPGPPGPP GPPGPPGTMG
ASSGVRLWAT RQAMLGQVHE VPEGWLIFVA EQEELYVRVQ NGFRKVQLEA RTPLPRGTDN
EVAALQPPVV QLHDSNPYPR REHPHPTARP WRADDILASP PRLPEPQPYP GAPHHSSYVH
LRPARPTSPP AHSHRDFQPV LHLVALNSPL SGGMRGIRGA DFQCFQQARA VGLAGTFRAF
LSSRLQDLYS IVRRADRAAV PIVNLKDELL FPSWEALFSG SEGPLKPGAR IFSFDGKDVL
RHPTWPQKSV WHGSDPNGRR LTESYCETWR TEAPSATGQA SSLLGGRLLG QSAASCHHAY
IVLCIENSFM TASK


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