GENTAUR Molecular Products.

 ANTR1_MOUSE             Reviewed;         562 AA.
 Q9CZ52; Q505H2;
 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
 02-NOV-2001, sequence version 2.
 07-NOV-2018, entry version 152.
 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; -.
 OrthoDB; EOG091G08TW; -.
 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.
 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: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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