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Anthrax toxin receptor 1 (Tumor endothelial marker 8)
ANTR1_MOUSE Reviewed; 562 AA.
Q9CZ52; Q505H2;
02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
02-NOV-2001, sequence version 2.
13-FEB-2019, entry version 155.
RecName: Full=Anthrax toxin receptor 1;
AltName: Full=Tumor endothelial marker 8;
Flags: Precursor;
Name=Antxr1; Synonyms=Atr, Tem8;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=11559528;
Carson-Walter E.B., Watkins D.N., Nanda A., Vogelstein B.,
Kinzler K.W., St Croix B.;
"Cell surface tumor endothelial markers are conserved in mice and
humans.";
Cancer Res. 61:6649-6655(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Brain;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 88-562 (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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 (By similarity).
{ECO:0000250}.
-!- 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 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}. Cell projection,
lamellipodium membrane {ECO:0000250}; Single-pass type I membrane
protein {ECO:0000250}. Cell projection, filopodium membrane
{ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Note=At the membrane of lamellipodia and at the tip of actin-
enriched filopodia. Colocalizes with actin at the base of
lamellipodia (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9CZ52-1; Sequence=Displayed;
Name=2;
IsoId=Q9CZ52-2; Sequence=VSP_000450;
Note=No experimental confirmation available.;
-!- DOMAIN: Binding to PA occurs through the VWA domain.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the ATR family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB28591.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF378762; AAL11999.1; -; mRNA.
EMBL; BC094544; AAH94544.1; -; mRNA.
EMBL; AK013005; BAB28591.1; ALT_INIT; mRNA.
CCDS; CCDS20318.1; -. [Q9CZ52-1]
RefSeq; NP_473382.1; NM_054041.2. [Q9CZ52-1]
UniGene; Mm.232525; -.
ProteinModelPortal; Q9CZ52; -.
SMR; Q9CZ52; -.
BioGrid; 213512; 1.
STRING; 10090.ENSMUSP00000045634; -.
iPTMnet; Q9CZ52; -.
PhosphoSitePlus; Q9CZ52; -.
SwissPalm; Q9CZ52; -.
jPOST; Q9CZ52; -.
PaxDb; Q9CZ52; -.
PeptideAtlas; Q9CZ52; -.
PRIDE; Q9CZ52; -.
Ensembl; ENSMUST00000042025; ENSMUSP00000045634; ENSMUSG00000033420. [Q9CZ52-1]
Ensembl; ENSMUST00000204805; ENSMUSP00000145105; ENSMUSG00000033420. [Q9CZ52-2]
GeneID; 69538; -.
KEGG; mmu:69538; -.
UCSC; uc009cte.1; mouse. [Q9CZ52-1]
CTD; 84168; -.
MGI; MGI:1916788; Antxr1.
eggNOG; ENOG410IK1W; Eukaryota.
eggNOG; ENOG410YC57; LUCA.
GeneTree; ENSGT00940000156522; -.
HOGENOM; HOG000264249; -.
HOVERGEN; HBG050514; -.
InParanoid; Q9CZ52; -.
KO; K20909; -.
OrthoDB; 613698at2759; -.
PhylomeDB; Q9CZ52; -.
TreeFam; TF328943; -.
ChiTaRS; Antxr1; mouse.
PRO; PR:Q9CZ52; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000033420; Expressed in 254 organ(s), highest expression level in embryo.
ExpressionAtlas; Q9CZ52; baseline and differential.
Genevisible; Q9CZ52; MM.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
GO; GO:0031527; C:filopodium membrane; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031258; C:lamellipodium membrane; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
GO; GO:0005518; F:collagen binding; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004888; F:transmembrane signaling receptor activity; ISS:UniProtKB.
GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
GO; GO:0001568; P:blood vessel development; IMP:MGI.
GO; GO:1901202; P:negative regulation of extracellular matrix assembly; IMP:MGI.
GO; GO:1905050; P:positive regulation of metallopeptidase activity; IMP:MGI.
GO; GO:0022414; P:reproductive process; IMP:MGI.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
GO; GO:1901998; P:toxin transport; IBA:GO_Central.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR017360; Anthrax_toxin_rcpt.
InterPro; IPR008399; Anthrax_toxin_rcpt_C.
InterPro; IPR008400; Anthrax_toxin_rcpt_extracel.
InterPro; IPR002035; VWF_A.
InterPro; IPR036465; vWFA_dom_sf.
PANTHER; PTHR16059; PTHR16059; 1.
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;
Alternative splicing; Cell membrane; Cell projection;
Complete proteome; Disulfide bond; Glycoprotein; Membrane;
Metal-binding; Phosphoprotein; Receptor; Reference proteome; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 30 {ECO:0000255}.
CHAIN 31 562 Anthrax toxin receptor 1.
/FTId=PRO_0000002693.
TOPO_DOM 31 319 Extracellular. {ECO:0000255}.
TRANSMEM 320 340 Helical. {ECO:0000255}.
TOPO_DOM 341 562 Cytoplasmic. {ECO:0000255}.
DOMAIN 42 213 VWFA. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
REGION 152 158 Interaction with PA. {ECO:0000250}.
COMPBIAS 358 366 Asp/Glu-rich (highly acidic).
COMPBIAS 501 562 Pro-rich.
METAL 50 50 Divalent metal cation. {ECO:0000250}.
METAL 52 52 Divalent metal cation. {ECO:0000250}.
METAL 116 116 Divalent metal cation. {ECO:0000250}.
MOD_RES 360 360 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 164 164 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 182 182 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 260 260 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 37 218 {ECO:0000250}.
VAR_SEQ 477 562 GRCINFTRVKNSQPAKYPLNNTYHPSSPPPAPIYTPPPPAP
HCPPPAPSAPTPPIPSPPSTLPPPPQAPPPNRAPPPSRPPP
RPSV -> RFRGWRLTICLGSKHVHPGRHDKGPETPLLKQA
WMFSSFLERAFQ (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_000450.
SEQUENCE 562 AA; 62308 MW; 6AC92049B4BB4F7C CRC64;
MDRAGRLGAG LRGLCVAALV LVCAGHGGRR EDGGPACYGG FDLYFILDKS GSVLHHWNEI
YYFVEQLAHR FISPQLRMSF IVFSTRGTTL MKLTEDREQI RQGLEELQKV LPGGDTYMHE
GFERASEQIY YENSQGYRTA SVIIALTDGE LHEDLFFYSE REANRSRDLG AIVYCVGVKD
FNETQLARIA DSKDHVFPVN DGFQALQGII HSILKKSCIE ILAAEPSTIC AGESFQVVVR
GNGFRHARNV DRVLCSFKIN DSVTLNEKPF AVEDTYLLCP APILKEVGMK AALQVSMNDG
LSFISSSVII TTTHCSDGSI LAIALLVLFL LLALALLWWF WPLCCTVIIK EVPPPPVEES
EEEDDDGLPK KKWPTVDASY YGGRGVGGIK RMEVRWGEKG STEEGAKLEK AKNARVKMPE
QEYEFPEPRN LNNNMRRPSS PRKWYSPIKG KLDALWVLLR KGYDRVSVMR PQPGDTGRCI
NFTRVKNSQP AKYPLNNTYH PSSPPPAPIY TPPPPAPHCP PPAPSAPTPP IPSPPSTLPP
PPQAPPPNRA PPPSRPPPRP SV
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Pathways :
WP1004: Kit Receptor Signaling Pathway
WP1011: T Cell Receptor Signaling Pathway
WP1014: Androgen receptor signaling pathway
WP1025: B Cell Receptor Signaling Pathway
WP1045: TGF-beta Receptor Signaling Pathway
WP1046: Signaling of Hepatocyte Growth Factor Receptor
WP1067: Toll-like receptor signaling pathway
WP1112: EPO Receptor Signaling
WP1121: Kit Receptor Signaling Pathway
WP1130: T Cell Receptor Signaling Pathway
WP1133: Androgen receptor signaling pathway
WP1144: B Cell Receptor Signaling Pathway
WP1161: TGF-beta Receptor Signaling Pathway
WP1162: Signaling of Hepatocyte Growth Factor Receptor
WP1183: Toll-like receptor signaling pathway
WP1206: Signaling of Hepatocyte Growth Factor Receptor
WP1235: Signaling of Hepatocyte Growth Factor Receptor
WP1249: EPO Receptor Signaling
WP1271: Toll-like receptor signaling pathway
WP1284: EPO Receptor Signaling
WP1309: Toll-like receptor signaling pathway
WP1336: EPO Receptor Signaling
WP1341: Kit Receptor Signaling Pathway
WP1345: T Cell Receptor Signaling Pathway
WP1348: Androgen Receptor Signaling Pathway
Related Genes :
Bibliography :
[29303078] Molecular Adjuvants Based on Plasmids Encoding Protein Aggregation Domains Affect Bone Marrow Niche Homeostasis.
[27029946] Administration of DNA Plasmid Coding Protein Aggregating Domain Induces Inflammatory Bone Loss.
[26785120] Anthrax Toxin Receptor 1 Is Essential for Arteriogenesis in a Mouse Model of Hindlimb Ischemia.
[25572963] Regulatory mechanisms of anthrax toxin receptor 1-dependent vascular and connective tissue homeostasis.
[23271637] The receptors that mediate the direct lethality of anthrax toxin.
[22340594] TEM8/ANTXR1 blockade inhibits pathological angiogenesis and potentiates tumoricidal responses against multiple cancer types.
[21829615] Tumor endothelial marker 8 amplifies canonical Wnt signaling in blood vessels.
[21206026] Crystallization and preliminary X-ray analysis of the vWA domain of human anthrax toxin receptor 1.
[20690680] Anthrax toxin receptor 1/tumor endothelial marker 8: mutation of conserved inserted domain residues overrides cytosolic control of protective antigen binding.
[20382142] Endosomal recycling regulates Anthrax Toxin Receptor 1/Tumor Endothelial Marker 8-dependent cell spreading.
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