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Anthrax toxin receptor 2 (Capillary morphogenesis gene 2 protein) (CMG-2)

 ANTR2_HUMAN             Reviewed;         489 AA.
P58335; Q4W5H6; Q59E98; Q5JPE9; Q86UI1; Q8N4J8; Q8NB13; Q96NC7;
02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 5.
25-OCT-2017, entry version 167.
RecName: Full=Anthrax toxin receptor 2;
AltName: Full=Capillary morphogenesis gene 2 protein;
Short=CMG-2;
Flags: Precursor;
Name=ANTXR2; Synonyms=CMG2;
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 2), FUNCTION, AND VARIANT PRO-357.
PubMed=11683410;
Bell S.E., Mavila A., Salazar R., Bayless K.J., Kanagala S.,
Maxwell S.A., Davis G.E.;
"Differential gene expression during capillary morphogenesis in 3D
collagen matrices: regulated expression of genes involved in basement
membrane matrix assembly, cell cycle progression, cellular
differentiation and G-protein signaling.";
J. Cell Sci. 114:2755-2773(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH ANTHRAX
TOXIN, AND VARIANT PRO-357.
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 63-489 (ISOFORM 3).
TISSUE=Synovial cell;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT
PRO-357.
TISSUE=Aortic endothelium;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[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] OF 137-489 (ISOFORM 4).
TISSUE=Lymph node;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 248-489 (ISOFORM 4), AND
VARIANT PRO-357.
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).
[8]
INTERACTION WITH ANTHRAX TOXIN, AND CLATHRIN-DEPENDENT
INTERNALIZATION.
PubMed=12551953; DOI=10.1083/jcb.200211018;
Abrami L., Liu S., Cosson P., Leppla S.H., van der Goot F.G.;
"Anthrax toxin triggers endocytosis of its receptor via a lipid raft-
mediated clathrin-dependent process.";
J. Cell Biol. 160:321-328(2003).
[9]
INTERNALIZATION.
PubMed=15337774; DOI=10.1083/jcb.200312072;
Abrami L., Lindsay M., Parton R.G., Leppla S.H., van der Goot F.G.;
"Membrane insertion of anthrax protective antigen and cytoplasmic
delivery of lethal factor occur at different stages of the endocytic
pathway.";
J. Cell Biol. 166:645-651(2004).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[11]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 40-212 OF COMPLEX WITH THE
PROTECTIVE ANTIGEN OF BACILLUS ANTHRACIS.
PubMed=15243628; DOI=10.1038/nature02763;
Santelli E., Bankston L.A., Leppla S.H., Liddington R.C.;
"Crystal structure of a complex between anthrax toxin and its host
cell receptor.";
Nature 430:905-908(2004).
[12]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 38-217.
PubMed=15079089; DOI=10.1073/pnas.0401506101;
Lacy D.B., Wigelsworth D.J., Scobie H.M., Young J.A.T., Collier R.J.;
"Crystal structure of the von Willebrand factor A domain of human
capillary morphogenesis protein 2: an anthrax toxin receptor.";
Proc. Natl. Acad. Sci. U.S.A. 101:6367-6372(2004).
[13]
X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 38-218 OF COMPLEX WITH THE
PROTECTIVE ANTIGEN OF BACILLUS ANTHRACIS.
PubMed=15326297; DOI=10.1073/pnas.0405405101;
Lacy D.B., Wigelsworth D.J., Melnyk R.A., Harrison S.C., Collier R.J.;
"Structure of heptameric protective antigen bound to an anthrax toxin
receptor: a role for receptor in pH-dependent pore formation.";
Proc. Natl. Acad. Sci. U.S.A. 101:13147-13151(2004).
[14]
VARIANTS HFS PRO-45; THR-189; ARG-218; GLN-293 INS AND CYS-381,
VARIANT PRO-357, AND TISSUE SPECIFICITY.
PubMed=14508707; DOI=10.1086/378418;
Hanks S., Adams S., Douglas J., Arbour L., Atherton D.J., Balci S.,
Bode H., Campbell M.E., Feingold M., Keser G., Kleijer W., Mancini G.,
McGrath J.A., Muntoni F., Nanda A., Teare M.D., Warman M., Pope F.M.,
Superti-Furga A., Futreal P.A., Rahman N.;
"Mutations in the gene encoding capillary morphogenesis protein 2
cause juvenile hyaline fibromatosis and infantile systemic
hyalinosis.";
Am. J. Hum. Genet. 73:791-800(2003).
[15]
VARIANTS HFS ASP-105; THR-189 AND ARG-329, AND FUNCTION.
PubMed=12973667; DOI=10.1086/378781;
Dowling O., Difeo A., Ramirez M.C., Tukel T., Narla G., Bonafe L.,
Kayserili H., Yuksel-Apak M., Paller A.S., Norton K., Teebi A.S.,
Grum-Tokars V., Martin G.S., Davis G.E., Glucksman M.J.,
Martignetti J.A.;
"Mutations in capillary morphogenesis gene-2 result in the allelic
disorders juvenile hyaline fibromatosis and infantile systemic
hyalinosis.";
Am. J. Hum. Genet. 73:957-966(2003).
[16]
INVOLVEMENT IN HFS.
PubMed=15725249; DOI=10.1111/j.1365-2230.2004.01698.x;
Lee J.Y.-Y., Tsai Y.-M., Chao S.-C., Tu Y.-F.;
"Capillary morphogenesis gene-2 mutation in infantile systemic
hyalinosis: ultrastructural study and mutation analysis in a Taiwanese
infant.";
Clin. Exp. Dermatol. 30:176-179(2005).
-!- FUNCTION: Necessary for cellular interactions with laminin and the
extracellular matrix. {ECO:0000269|PubMed:11683410,
ECO:0000269|PubMed:12973667}.
-!- SUBUNIT: Binds laminin, and possibly also collagen type IV. Binds
to the protective antigen (PA) of Bacillus anthracis in a divalent
cation-dependent manner, with the following preference: calcium >
manganese > magnesium > zinc. Binding of PA leads to
heptamerization of the receptor-PA complex.
-!- INTERACTION:
P13423:pagA (xeno); NbExp=7; IntAct=EBI-456840, EBI-456868;
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
membrane protein. Note=Expressed at the cell surface.
-!- SUBCELLULAR LOCATION: Isoform 2: Endoplasmic reticulum membrane;
Single-pass type I membrane protein. Note=Expressed predominantly
within the endoplasmic reticulum and not at the plasma membrane.
-!- SUBCELLULAR LOCATION: Isoform 3: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P58335-1; Sequence=Displayed;
Name=2;
IsoId=P58335-2; Sequence=VSP_008343;
Name=3;
IsoId=P58335-3; Sequence=VSP_008344, VSP_008345;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=4;
IsoId=P58335-4; Sequence=VSP_008346;
-!- TISSUE SPECIFICITY: Expressed in prostate, thymus, ovary, testis,
pancreas, colon, heart, kidney, lung, liver, peripheral blood
leukocytes, placenta, skeletal muscle, small intestine and spleen.
{ECO:0000269|PubMed:14508707}.
-!- DOMAIN: Binding to PA seems to be effected through the VWA domain.
-!- DISEASE: Hyaline fibromatosis syndrome (HFS) [MIM:228600]: An
autosomal recessive syndrome characterized by abnormal growth of
hyalinized fibrous tissue usually affecting subcutaneous regions
on the scalp, ears, neck, face, hands, and feet. The lesions
appear as pearly papules or fleshy nodules. Additional features
include gingival hypertrophy, progressive joint contractures
resulting in severe limitation of mobility, osteopenia, and
osteoporosis. Disease severity is variable. Some individuals
manifest symptoms in infancy and have additional visceral or
systemic involvement. Hyaline deposits in multiple organs,
recurrent infections and intractable diarrhea often lead to early
death. Surviving children may suffer from severely reduced
mobility due to joint contractures. Other patients have later
onset of a milder disorder affecting only the face and digits.
{ECO:0000269|PubMed:12973667, ECO:0000269|PubMed:14508707,
ECO:0000269|PubMed:15725249}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Upon binding of the protective antigen (PA) of
Bacillus anthracis the complex moves to glycosphingolipid-rich
lipid rafts, where it is internalized via a clathrin-dependent
pathway. In the endosomal membrane, at pH under 7, the complex
then rearranges and forms a pore allowing the other components of
anthrax toxin to escape to the cytoplasm.
-!- SIMILARITY: Belongs to the ATR family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAY40907.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=BAB70976.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAD93150.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AY040326; AAK77222.1; -; mRNA.
EMBL; AY233452; AAP04016.1; -; mRNA.
EMBL; AK055636; BAB70976.1; ALT_INIT; mRNA.
EMBL; AK091721; BAC03731.1; -; mRNA.
EMBL; AB209913; BAD93150.1; ALT_INIT; mRNA.
EMBL; AC097711; AAY40907.1; ALT_SEQ; Genomic_DNA.
EMBL; AC109518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC114773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL832851; CAI46157.2; -; mRNA.
EMBL; BC034001; AAH34001.2; -; mRNA.
CCDS; CCDS47085.1; -. [P58335-4]
CCDS; CCDS47086.1; -. [P58335-1]
RefSeq; NP_001139266.1; NM_001145794.1. [P58335-1]
RefSeq; NP_001273709.1; NM_001286780.1.
RefSeq; NP_001273710.1; NM_001286781.1.
RefSeq; NP_477520.2; NM_058172.5. [P58335-4]
UniGene; Hs.162963; -.
PDB; 1SHT; X-ray; 1.81 A; X=38-217.
PDB; 1SHU; X-ray; 1.50 A; X=38-218.
PDB; 1T6B; X-ray; 2.50 A; Y=40-212.
PDB; 1TZN; X-ray; 4.30 A; a/b/c/d/e/f/g/h/i/j/k/l/m/o=38-218.
PDBsum; 1SHT; -.
PDBsum; 1SHU; -.
PDBsum; 1T6B; -.
PDBsum; 1TZN; -.
ProteinModelPortal; P58335; -.
SMR; P58335; -.
BioGrid; 125602; 12.
DIP; DIP-32476N; -.
IntAct; P58335; 4.
MINT; MINT-1184613; -.
STRING; 9606.ENSP00000306185; -.
iPTMnet; P58335; -.
PhosphoSitePlus; P58335; -.
SwissPalm; P58335; -.
BioMuta; ANTXR2; -.
DMDM; 306526289; -.
EPD; P58335; -.
MaxQB; P58335; -.
PaxDb; P58335; -.
PeptideAtlas; P58335; -.
PRIDE; P58335; -.
Ensembl; ENST00000307333; ENSP00000306185; ENSG00000163297. [P58335-1]
Ensembl; ENST00000346652; ENSP00000314883; ENSG00000163297. [P58335-2]
Ensembl; ENST00000403729; ENSP00000385575; ENSG00000163297. [P58335-4]
GeneID; 118429; -.
KEGG; hsa:118429; -.
UCSC; uc003hly.5; human. [P58335-1]
CTD; 118429; -.
DisGeNET; 118429; -.
EuPathDB; HostDB:ENSG00000163297.16; -.
GeneCards; ANTXR2; -.
GeneReviews; ANTXR2; -.
HGNC; HGNC:21732; ANTXR2.
MalaCards; ANTXR2; -.
MIM; 228600; phenotype.
MIM; 608041; gene.
neXtProt; NX_P58335; -.
OpenTargets; ENSG00000163297; -.
Orphanet; 2176; Infantile systemic hyalinosis.
Orphanet; 2028; Juvenile hyaline fibromatosis.
PharmGKB; PA128394752; -.
eggNOG; ENOG410IK1W; Eukaryota.
eggNOG; ENOG410YC57; LUCA.
GeneTree; ENSGT00430000031214; -.
HOVERGEN; HBG050514; -.
InParanoid; P58335; -.
KO; K20909; -.
OMA; GLMWWFW; -.
OrthoDB; EOG091G08TW; -.
PhylomeDB; P58335; -.
TreeFam; TF328943; -.
Reactome; R-HSA-5210891; Uptake and function of anthrax toxins.
ChiTaRS; ANTXR2; human.
EvolutionaryTrace; P58335; -.
GeneWiki; ANTXR2; -.
GenomeRNAi; 118429; -.
PRO; PR:P58335; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000163297; -.
CleanEx; HS_ANTXR2; -.
ExpressionAtlas; P58335; baseline and differential.
Genevisible; P58335; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004872; F:receptor activity; IEA:InterPro.
GO; GO:0022414; P:reproductive process; IEA:Ensembl.
GO; GO:1901998; P:toxin transport; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR017360; Anthrax_toxin_rcpt.
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.
PIRSF; PIRSF038023; Anthrax_toxin_receptor_2; 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; Complete proteome;
Disease mutation; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
Membrane; Metal-binding; Phosphoprotein; Polymorphism; Receptor;
Reference proteome; Secreted; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 33 {ECO:0000255}.
CHAIN 34 489 Anthrax toxin receptor 2.
/FTId=PRO_0000002694.
TOPO_DOM 34 318 Extracellular. {ECO:0000255}.
TRANSMEM 319 341 Helical. {ECO:0000255}.
TOPO_DOM 342 489 Cytoplasmic. {ECO:0000255}.
DOMAIN 44 213 VWFA. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
COMPBIAS 352 360 Poly-Pro.
COMPBIAS 362 366 Poly-Glu.
METAL 52 52 Divalent metal cation.
METAL 54 54 Divalent metal cation.
METAL 118 118 Divalent metal cation.
MOD_RES 147 147 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
CARBOHYD 250 250 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 260 260 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 39 218
VAR_SEQ 213 315 Missing (in isoform 2).
{ECO:0000303|PubMed:11683410}.
/FTId=VSP_008343.
VAR_SEQ 290 322 TLDVSVSFNGGKSVISGSLIVTATECSNGIAAI -> WGLT
VTQAGVKWHDLTHCTFGLSGSGDPPTSAS (in isoform
3). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_008344.
VAR_SEQ 323 489 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_008345.
VAR_SEQ 477 489 VCIWECIEKELTA -> GRCINFSRVPSQ (in isoform
4). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005,
ECO:0000303|Ref.4}.
/FTId=VSP_008346.
VARIANT 45 45 L -> P (in HFS; infantile form).
{ECO:0000269|PubMed:14508707}.
/FTId=VAR_022687.
VARIANT 105 105 G -> D (in HFS; dbSNP:rs137852902).
{ECO:0000269|PubMed:12973667}.
/FTId=VAR_022688.
VARIANT 189 189 I -> T (in HFS; infantile form;
dbSNP:rs137852905).
{ECO:0000269|PubMed:12973667,
ECO:0000269|PubMed:14508707}.
/FTId=VAR_022689.
VARIANT 218 218 C -> R (in HFS; infantile form;
dbSNP:rs781637328).
{ECO:0000269|PubMed:14508707}.
/FTId=VAR_022690.
VARIANT 293 293 V -> VQ (in HFS).
{ECO:0000269|PubMed:14508707}.
/FTId=VAR_022691.
VARIANT 329 329 L -> R (in HFS; dbSNP:rs137852903).
{ECO:0000269|PubMed:12973667}.
/FTId=VAR_022692.
VARIANT 357 357 A -> P (in dbSNP:rs12647691).
{ECO:0000269|PubMed:11683410,
ECO:0000269|PubMed:12700348,
ECO:0000269|PubMed:14508707,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.4}.
/FTId=VAR_022693.
VARIANT 381 381 Y -> C (in HFS; dbSNP:rs137852901).
{ECO:0000269|PubMed:14508707}.
/FTId=VAR_022694.
STRAND 43 50 {ECO:0000244|PDB:1SHU}.
HELIX 53 58 {ECO:0000244|PDB:1SHU}.
HELIX 59 72 {ECO:0000244|PDB:1SHU}.
STRAND 78 96 {ECO:0000244|PDB:1SHU}.
HELIX 99 110 {ECO:0000244|PDB:1SHU}.
HELIX 120 134 {ECO:0000244|PDB:1SHU}.
HELIX 136 138 {ECO:0000244|PDB:1SHU}.
STRAND 141 147 {ECO:0000244|PDB:1SHU}.
HELIX 155 168 {ECO:0000244|PDB:1SHU}.
STRAND 172 177 {ECO:0000244|PDB:1SHU}.
HELIX 183 189 {ECO:0000244|PDB:1SHU}.
STRAND 190 192 {ECO:0000244|PDB:1SHU}.
HELIX 193 195 {ECO:0000244|PDB:1SHU}.
STRAND 196 201 {ECO:0000244|PDB:1SHU}.
HELIX 204 215 {ECO:0000244|PDB:1SHU}.
SEQUENCE 489 AA; 53666 MW; B9F66CCE7A13F807 CRC64;
MVAERSPARS PGSWLFPGLW LLVLSGPGGL LRAQEQPSCR RAFDLYFVLD KSGSVANNWI
EIYNFVQQLA ERFVSPEMRL SFIVFSSQAT IILPLTGDRG KISKGLEDLK RVSPVGETYI
HEGLKLANEQ IQKAGGLKTS SIIIALTDGK LDGLVPSYAE KEAKISRSLG ASVYCVGVLD
FEQAQLERIA DSKEQVFPVK GGFQALKGII NSILAQSCTE ILELQPSSVC VGEEFQIVLS
GRGFMLGSRN GSVLCTYTVN ETYTTSVKPV SVQLNSMLCP APILNKAGET LDVSVSFNGG
KSVISGSLIV TATECSNGIA AIIVILVLLL LLGIGLMWWF WPLCCKVVIK DPPPPPAPAP
KEEEEEPLPT KKWPTVDASY YGGRGVGGIK RMEVRWGDKG STEEGARLEK AKNAVVKIPE
ETEEPIRPRP PRPKPTHQPP QTKWYTPIKG RLDALWALLR RQYDRVSLMR PQEGDEVCIW
ECIEKELTA


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