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Anthrax toxin receptor 1 (Tumor endothelial marker 8)

 ANTR1_HUMAN             Reviewed;         564 AA.
Q9H6X2; A8K7U8; J7K7G4; J7KF88; Q4ZFV6; Q53QD8; Q96P02; Q9NVP3;
02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
02-NOV-2001, sequence version 2.
25-OCT-2017, entry version 174.
RecName: Full=Anthrax toxin receptor 1;
AltName: Full=Tumor endothelial marker 8;
Flags: Precursor;
Name=ANTXR1; Synonyms=ATR, TEM8;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10947988; DOI=10.1126/science.289.5482.1197;
St Croix B., Rago C., Velculescu V.E., Traverso G., Romans K.E.,
Montgomery E., Lal A., Riggins G.J., Lengauer C., Vogelstein B.,
Kinzler K.W.;
"Genes expressed in human tumor endothelium.";
Science 289:1197-1202(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH ANTHRAX
TOXIN.
PubMed=11700562; DOI=10.1038/n35101999;
Bradley K.A., Mogridge J., Mourez M., Collier R.J., Young J.A.T.;
"Identification of the cellular receptor for anthrax toxin.";
Nature 414:225-229(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6), AND ALTERNATIVE
SPLICING.
TISSUE=Brain, and Prostate;
PubMed=22912819; DOI=10.1371/journal.pone.0043174;
Vargas M., Karamsetty R., Leppla S.H., Chaudry G.J.;
"Broad expression analysis of human ANTXR1/TEM8 transcripts reveals
differential expression and novel splizce variants.";
PLoS ONE 7:E43174-E43174(2012).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 184-564 (ISOFORM 1),
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND VARIANT
LYS-7.
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).
[5]
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Kidney;
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).
[7]
INTERACTION WITH ANTHRAX TOXIN.
TISSUE=Placenta;
PubMed=12700348; DOI=10.1073/pnas.0431098100;
Scobie H.M., Rainey G.J.A., Bradley K.A., Young J.A.T.;
"Human capillary morphogenesis protein 2 functions as an anthrax toxin
receptor.";
Proc. Natl. Acad. Sci. U.S.A. 100:5170-5174(2003).
[8]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
[9]
FUNCTION, INDUCTION, INTERACTION WITH TYPE 1 COLLAGEN AND GELATIN, AND
TISSUE SPECIFICITY.
PubMed=15777794; DOI=10.1016/j.yexcr.2004.12.025;
Hotchkiss K.A., Basile C.M., Spring S.C., Bonuccelli G., Lisanti M.P.,
Terman B.I.;
"TEM8 expression stimulates endothelial cell adhesion and migration by
regulating cell-matrix interactions on collagen.";
Exp. Cell Res. 305:133-144(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TYPE 1 COLLAGEN;
THE ACTIN CYTOSKELETON AND BACILLUS ANTHRACIS PROTECTIVE ANTIGEN.
PubMed=16762926; DOI=10.1074/jbc.M603676200;
Werner E., Kowalczyk A.P., Faundez V.;
"Anthrax toxin receptor 1/tumor endothelium marker 8 mediates cell
spreading by coupling extracellular ligands to the actin
cytoskeleton.";
J. Biol. Chem. 281:23227-23236(2006).
[12]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-184.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[13]
INVOLVEMENT IN GAPO.
PubMed=23602711; DOI=10.1016/j.ajhg.2013.03.023;
Stranecky V., Hoischen A., Hartmannova H., Zaki M.S., Chaudhary A.,
Zudaire E., Noskova L., Baresova V., Pristoupilova A., Hodanova K.,
Sovova J., Hulkova H., Piherova L., Hehir-Kwa J.Y., de Silva D.,
Senanayake M.P., Farrag S., Zeman J., Martasek P., Baxova A.,
Afifi H.H., St Croix B., Brunner H.G., Temtamy S., Kmoch S.;
"Mutations in ANTXR1 cause GAPO syndrome.";
Am. J. Hum. Genet. 92:792-799(2013).
[14]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 38-220, SUBUNIT, INTERACTION
WITH ANTHRAX TOXIN, AND DISULFIDE BOND.
PubMed=20585457; DOI=10.1371/journal.pone.0011203;
Fu S., Tong X., Cai C., Zhao Y., Wu Y., Li Y., Xu J., Zhang X.C.,
Xu L., Chen W., Rao Z.;
"The structure of tumor endothelial marker 8 (TEM8) extracellular
domain and implications for its receptor function for recognizing
anthrax toxin.";
PLoS ONE 5:E11203-E11203(2010).
[15]
VARIANT HCI SUSCEPTIBILITY THR-326.
PubMed=18931684; DOI=10.1038/nm.1877;
Jinnin M., Medici D., Park L., Limaye N., Liu Y., Boscolo E.,
Bischoff J., Vikkula M., Boye E., Olsen B.R.;
"Suppressed NFAT-dependent VEGFR1 expression and constitutive VEGFR2
signaling in infantile hemangioma.";
Nat. Med. 14:1236-1246(2008).
-!- FUNCTION: Plays a role in cell attachment and migration. Interacts
with extracellular matrix proteins and with the actin
cytoskeleton. Mediates adhesion of cells to type 1 collagen and
gelatin, reorganization of the actin cytoskeleton and promotes
cell spreading. Plays a role in the angiogenic response of
cultured umbilical vein endothelial cells.
{ECO:0000269|PubMed:15777794, ECO:0000269|PubMed:16762926}.
-!- SUBUNIT: Interacts with gelatin and type 1 collagen. Interacts
with the actin cytoskeleton. Binds to the protective antigen (PA)
of Bacillus anthracis. Binding does not occur in the presence of
calcium. {ECO:0000269|PubMed:11700562,
ECO:0000269|PubMed:12700348, ECO:0000269|PubMed:15777794,
ECO:0000269|PubMed:16762926, ECO:0000269|PubMed:20585457}.
-!- INTERACTION:
O75581:LRP6; NbExp=3; IntAct=EBI-905643, EBI-910915;
P13423:pagA (xeno); NbExp=3; IntAct=EBI-905659, EBI-456868;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16762926};
Single-pass type I membrane protein {ECO:0000269|PubMed:16762926}.
Cell projection, lamellipodium membrane
{ECO:0000269|PubMed:16762926}; Single-pass type I membrane protein
{ECO:0000269|PubMed:16762926}. Cell projection, filopodium
membrane {ECO:0000269|PubMed:16762926}; Single-pass type I
membrane protein {ECO:0000269|PubMed:16762926}. Note=At the
membrane of lamellipodia and at the tip of actin-enriched
filopodia. Colocalizes with actin at the base of lamellipodia.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Comment=Experimental confirmation may be lacking for some
isoforms.;
Name=1;
IsoId=Q9H6X2-1; Sequence=Displayed;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=2;
IsoId=Q9H6X2-2; Sequence=VSP_000444, VSP_000445;
Name=3;
IsoId=Q9H6X2-3; Sequence=VSP_000446, VSP_000447;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q9H6X2-4; Sequence=VSP_000448, VSP_000449;
Name=5; Synonyms=V4;
IsoId=Q9H6X2-5; Sequence=VSP_047865;
Name=6; Synonyms=V5;
IsoId=Q9H6X2-6; Sequence=VSP_047863, VSP_047864;
Note=Prostate-specific.;
-!- TISSUE SPECIFICITY: Detected in umbilical vein endothelial cells
(at protein level). Highly expressed in tumor endothelial cells.
{ECO:0000269|PubMed:15777794}.
-!- INDUCTION: Up-regulated in cultured angiogenic umbilical vein
endothelial cells. {ECO:0000269|PubMed:15777794}.
-!- DOMAIN: Binding to PA occurs through the VWA domain.
-!- DISEASE: Hemangioma, capillary infantile (HCI) [MIM:602089]: A
condition characterized by dull red, firm, dome-shaped
hemangiomas, sharply demarcated from surrounding skin, usually
presenting at birth or occurring within the first two or three
months of life. They result from highly proliferative, localized
growth of capillary endothelium and generally undergo regression
and involution without scarring. {ECO:0000269|PubMed:18931684}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- DISEASE: GAPO syndrome (GAPO) [MIM:230740]: A disease
characterized by growth retardation, alopecia, failure of tooth
eruption, and progressive optic atrophy in some patients.
{ECO:0000269|PubMed:23602711}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the ATR family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA91707.1; Type=Miscellaneous discrepancy; Note=Erroneous initiation (Translation N-terminally extended) due to a conflict with the genome, including a frameshift.; Evidence={ECO:0000305};
Sequence=BAB15128.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF279145; AAK52094.1; -; mRNA.
EMBL; AF421380; AAL26496.1; -; mRNA.
EMBL; JX424838; AFQ94038.1; -; mRNA.
EMBL; JX424839; AFQ94039.1; -; mRNA.
EMBL; AK001463; BAA91707.1; ALT_SEQ; mRNA.
EMBL; AK025429; BAB15128.1; ALT_INIT; mRNA.
EMBL; AK292113; BAF84802.1; -; mRNA.
EMBL; AC112230; AAX88860.1; -; Genomic_DNA.
EMBL; AC114802; AAY24067.1; -; Genomic_DNA.
EMBL; BC012074; AAH12074.1; -; mRNA.
CCDS; CCDS1892.1; -. [Q9H6X2-1]
CCDS; CCDS46313.1; -. [Q9H6X2-2]
CCDS; CCDS46314.1; -. [Q9H6X2-4]
RefSeq; NP_060623.2; NM_018153.3. [Q9H6X2-4]
RefSeq; NP_115584.1; NM_032208.2. [Q9H6X2-1]
RefSeq; NP_444262.1; NM_053034.2. [Q9H6X2-2]
UniGene; Hs.165859; -.
PDB; 3N2N; X-ray; 1.80 A; A/B/C/D/E/F=38-220.
PDBsum; 3N2N; -.
ProteinModelPortal; Q9H6X2; -.
SMR; Q9H6X2; -.
BioGrid; 123924; 62.
IntAct; Q9H6X2; 14.
STRING; 9606.ENSP00000301945; -.
iPTMnet; Q9H6X2; -.
PhosphoSitePlus; Q9H6X2; -.
SwissPalm; Q9H6X2; -.
BioMuta; ANTXR1; -.
DMDM; 17366074; -.
EPD; Q9H6X2; -.
MaxQB; Q9H6X2; -.
PaxDb; Q9H6X2; -.
PeptideAtlas; Q9H6X2; -.
PRIDE; Q9H6X2; -.
DNASU; 84168; -.
Ensembl; ENST00000303714; ENSP00000301945; ENSG00000169604. [Q9H6X2-1]
Ensembl; ENST00000409349; ENSP00000386494; ENSG00000169604. [Q9H6X2-2]
Ensembl; ENST00000409829; ENSP00000387058; ENSG00000169604. [Q9H6X2-4]
GeneID; 84168; -.
KEGG; hsa:84168; -.
UCSC; uc002sfe.4; human. [Q9H6X2-1]
CTD; 84168; -.
DisGeNET; 84168; -.
EuPathDB; HostDB:ENSG00000169604.19; -.
GeneCards; ANTXR1; -.
HGNC; HGNC:21014; ANTXR1.
HPA; HPA052046; -.
HPA; HPA054785; -.
MalaCards; ANTXR1; -.
MIM; 230740; phenotype.
MIM; 602089; phenotype.
MIM; 606410; gene.
neXtProt; NX_Q9H6X2; -.
OpenTargets; ENSG00000169604; -.
Orphanet; 91415; Familial capillary hemangioma.
Orphanet; 2067; GAPO syndrome.
PharmGKB; PA134956382; -.
eggNOG; ENOG410IK1W; Eukaryota.
eggNOG; ENOG410YC57; LUCA.
GeneTree; ENSGT00430000031214; -.
HOGENOM; HOG000264249; -.
HOVERGEN; HBG050514; -.
InParanoid; Q9H6X2; -.
KO; K20909; -.
OMA; FTVEDTY; -.
OrthoDB; EOG091G08TW; -.
PhylomeDB; Q9H6X2; -.
TreeFam; TF328943; -.
Reactome; R-HSA-5210891; Uptake and function of anthrax toxins.
ChiTaRS; ANTXR1; human.
GeneWiki; ANTXR1; -.
GenomeRNAi; 84168; -.
PRO; PR:Q9H6X2; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000169604; -.
CleanEx; HS_ANTXR1; -.
CleanEx; HS_ATR; -.
ExpressionAtlas; Q9H6X2; baseline and differential.
Genevisible; Q9H6X2; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031527; C:filopodium membrane; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031258; C:lamellipodium membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
GO; GO:0005518; F:collagen binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:UniProtKB.
GO; GO:0031532; P:actin cytoskeleton reorganization; IDA:UniProtKB.
GO; GO:0001568; P:blood vessel development; IEA:Ensembl.
GO; GO:1901202; P:negative regulation of extracellular matrix assembly; IEA:Ensembl.
GO; GO:1905050; P:positive regulation of metallopeptidase activity; IEA:Ensembl.
GO; GO:0022414; P:reproductive process; IEA:Ensembl.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:UniProtKB.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR008399; Anthrax_toxin_rcpt_C.
InterPro; IPR008400; Anthrax_toxin_rcpt_extracel.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR002035; VWF_A.
InterPro; IPR036465; vWFA_dom_sf.
Pfam; PF05586; Ant_C; 1.
Pfam; PF05587; Anth_Ig; 1.
Pfam; PF00092; VWA; 1.
ProDom; PD377005; Anthrax_toxin_rcpt_C; 1.
SMART; SM00327; VWA; 1.
SUPFAM; SSF53300; SSF53300; 1.
PROSITE; PS50234; VWFA; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Cell projection;
Complete proteome; Disulfide bond; Glycoprotein; Hypotrichosis;
Membrane; Metal-binding; Phosphoprotein; Polymorphism; Receptor;
Reference proteome; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 32 {ECO:0000255}.
CHAIN 33 564 Anthrax toxin receptor 1.
/FTId=PRO_0000002692.
TOPO_DOM 33 321 Extracellular. {ECO:0000255}.
TRANSMEM 322 342 Helical. {ECO:0000255}.
TOPO_DOM 343 564 Cytoplasmic. {ECO:0000255}.
DOMAIN 44 215 VWFA. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
REGION 154 160 Interaction with PA.
COMPBIAS 360 368 Asp/Glu-rich (highly acidic).
COMPBIAS 506 564 Pro-rich.
METAL 52 52 Divalent metal cation. {ECO:0000250}.
METAL 54 54 Divalent metal cation. {ECO:0000250}.
METAL 118 118 Divalent metal cation. {ECO:0000250}.
MOD_RES 362 362 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
CARBOHYD 166 166 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 184 184 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 262 262 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 39 220 {ECO:0000269|PubMed:20585457}.
VAR_SEQ 268 297 NEKPFSVEDTYLLCPAPILKEVGMKAALQV -> SKSLQSP
WVSSTSGFKEGNSHPCLPARPHT (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_000446.
VAR_SEQ 298 564 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_000447.
VAR_SEQ 315 358 THCSDGSILAIALLILFLLLALALLWWFWPLCCTVIIKEVP
PPP -> FHPSPSSPGSTSQQGTSSLPPSSKAFCLEPKVPA
LGSLRNFRRC (in isoform 6).
{ECO:0000303|PubMed:22912819}.
/FTId=VSP_047863.
VAR_SEQ 319 333 DGSILAIALLILFLL -> LHKIASGPTTAACME (in
isoform 4). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_000448.
VAR_SEQ 334 564 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_000449.
VAR_SEQ 359 564 Missing (in isoform 6).
{ECO:0000303|PubMed:22912819}.
/FTId=VSP_047864.
VAR_SEQ 365 368 EDDD -> NKIK (in isoform 2).
{ECO:0000303|PubMed:11700562}.
/FTId=VSP_000444.
VAR_SEQ 369 564 Missing (in isoform 2).
{ECO:0000303|PubMed:11700562}.
/FTId=VSP_000445.
VAR_SEQ 522 557 Missing (in isoform 5).
{ECO:0000303|PubMed:22912819}.
/FTId=VSP_047865.
VARIANT 7 7 R -> K (in dbSNP:rs28365986).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_053015.
VARIANT 326 326 A -> T (in HCI susceptibility; expression
of FLT1 in hemangioma endothelial cells
is markedly reduced compared to controls;
low FLT1 expression in hemangioma cells
is caused by reduced activity of a
pathway involving ITGB1, ANTXR1, KDR and
NFATC2IP; the mutation disrupts
interaction of these molecules in a
dominant-negative manner;
dbSNP:rs119475040).
{ECO:0000269|PubMed:18931684}.
/FTId=VAR_063146.
STRAND 40 50 {ECO:0000244|PDB:3N2N}.
HELIX 53 58 {ECO:0000244|PDB:3N2N}.
HELIX 59 72 {ECO:0000244|PDB:3N2N}.
STRAND 78 96 {ECO:0000244|PDB:3N2N}.
HELIX 99 110 {ECO:0000244|PDB:3N2N}.
HELIX 120 135 {ECO:0000244|PDB:3N2N}.
STRAND 141 149 {ECO:0000244|PDB:3N2N}.
HELIX 155 170 {ECO:0000244|PDB:3N2N}.
STRAND 173 179 {ECO:0000244|PDB:3N2N}.
HELIX 185 188 {ECO:0000244|PDB:3N2N}.
TURN 189 191 {ECO:0000244|PDB:3N2N}.
STRAND 192 194 {ECO:0000244|PDB:3N2N}.
HELIX 195 197 {ECO:0000244|PDB:3N2N}.
STRAND 198 200 {ECO:0000244|PDB:3N2N}.
HELIX 201 217 {ECO:0000244|PDB:3N2N}.
SEQUENCE 564 AA; 62789 MW; B118A00AD5DF2233 CRC64;
MATAERRALG IGFQWLSLAT LVLICAGQGG RREDGGPACY GGFDLYFILD KSGSVLHHWN
EIYYFVEQLA HKFISPQLRM SFIVFSTRGT TLMKLTEDRE QIRQGLEELQ KVLPGGDTYM
HEGFERASEQ IYYENRQGYR TASVIIALTD GELHEDLFFY SEREANRSRD LGAIVYCVGV
KDFNETQLAR IADSKDHVFP VNDGFQALQG IIHSILKKSC IEILAAEPST ICAGESFQVV
VRGNGFRHAR NVDRVLCSFK INDSVTLNEK PFSVEDTYLL CPAPILKEVG MKAALQVSMN
DGLSFISSSV IITTTHCSDG SILAIALLIL FLLLALALLW WFWPLCCTVI IKEVPPPPAE
ESEEEDDDGL PKKKWPTVDA SYYGGRGVGG IKRMEVRWGE KGSTEEGAKL EKAKNARVKM
PEQEYEFPEP RNLNNNMRRP SSPRKWYSPI KGKLDALWVL LRKGYDRVSV MRPQPGDTGR
CINFTRVKNN QPAKYPLNNA YHTSSPPPAP IYTPPPPAPH CPPPPPSAPT PPIPSPPSTL
PPPPQAPPPN RAPPPSRPPP RPSV


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