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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.
20-DEC-2017, entry version 148.
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; -.
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; ENSGT00430000031214; -.
HOGENOM; HOG000264249; -.
HOVERGEN; HBG050514; -.
InParanoid; Q9CZ52; -.
KO; K20909; -.
OMA; FTVEDTY; -.
OrthoDB; EOG091G08TW; -.
PhylomeDB; Q9CZ52; -.
TreeFam; TF328943; -.
ChiTaRS; Antxr1; mouse.
PRO; PR:Q9CZ52; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000033420; -.
CleanEx; MM_ANTXR1; -.
CleanEx; MM_ATR; -.
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:0070062; C:extracellular exosome; 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.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR008399; Anthrax_toxin_rcpt_C.
InterPro; IPR008400; Anthrax_toxin_rcpt_extracel.
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;
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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