ID   ANTR2_MOUSE             Reviewed;         487 AA.
AC   Q6DFX2; Q99L17;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   02-SEP-2026, entry version 145.
DE   RecName: Full=Anthrax toxin receptor 2;
DE   Flags: Precursor;
GN   Name=Antxr2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Eye, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart, and Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Necessary for cellular interactions with laminin and the
CC       extracellular matrix. {ECO:0000250|UniProtKB:P58335}.
CC   -!- SUBUNIT: Binds laminin, and possibly also collagen type IV.
CC       {ECO:0000250|UniProtKB:P58335}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P58335}; Single-
CC       pass type I membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the ATR family. {ECO:0000305}.
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DR   EMBL; BC003908; AAH03908.1; -; mRNA.
DR   EMBL; BC076595; AAH76595.1; -; mRNA.
DR   CCDS; CCDS39177.1; -.
DR   RefSeq; NP_598499.1; NM_133738.3.
DR   AlphaFoldDB; Q6DFX2; -.
DR   SMR; Q6DFX2; -.
DR   BioGRID; 215027; 3.
DR   FunCoup; Q6DFX2; 299.
DR   STRING; 10090.ENSMUSP00000031281; -.
DR   GlyCosmos; Q6DFX2; 1 site, No reported glycans.
DR   GlyGen; Q6DFX2; 1 site, 1 N-linked glycan (1 site).
DR   iPTMnet; Q6DFX2; -.
DR   PhosphoSitePlus; Q6DFX2; -.
DR   SwissPalm; Q6DFX2; -.
DR   PaxDb; 10090-ENSMUSP00000031281; -.
DR   ProteomicsDB; 282125; -.
DR   Pumba; Q6DFX2; -.
DR   Antibodypedia; 24968; 189 antibodies from 33 providers.
DR   DNASU; 71914; -.
DR   Ensembl; ENSMUST00000031281.14; ENSMUSP00000031281.10; ENSMUSG00000029338.14.
DR   GeneID; 71914; -.
DR   KEGG; mmu:71914; -.
DR   UCSC; uc008yga.1; mouse.
DR   AGR; MGI:1919164; -.
DR   CTD; 118429; -.
DR   MGI; MGI:1919164; Antxr2.
DR   VEuPathDB; HostDB:ENSMUSG00000029338; -.
DR   eggNOG; ENOG502QT7Y; Eukaryota.
DR   GeneTree; ENSGT00940000156320; -.
DR   HOGENOM; CLU_029760_0_0_1; -.
DR   InParanoid; Q6DFX2; -.
DR   OMA; NFNRVPH; -.
DR   OrthoDB; 69748at9989; -.
DR   PhylomeDB; Q6DFX2; -.
DR   BioGRID-ORCS; 71914; 1 hit in 80 CRISPR screens.
DR   PRO; PR:Q6DFX2; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q6DFX2; protein.
DR   Bgee; ENSMUSG00000029338; Expressed in decidua and 206 other cell types or tissues.
DR   ExpressionAtlas; Q6DFX2; baseline and differential.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:GO_Central.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:GO_Central.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
DR   GO; GO:0032963; P:collagen metabolic process; IMP:MGI.
DR   GO; GO:0007338; P:single fertilization; IMP:MGI.
DR   GO; GO:0060065; P:uterus development; IMP:MGI.
DR   CDD; cd01474; vWA_ATR; 1.
DR   FunFam; 3.40.50.410:FF:000024; Anthrax toxin receptor; 1.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   InterPro; IPR017360; Anthrax_toxin_rcpt.
DR   InterPro; IPR008399; Anthrax_toxin_rcpt_C.
DR   InterPro; IPR008400; Anthrax_toxin_rcpt_extracel.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR16059; ANTHRAX TOXIN RECEPTOR; 1.
DR   PANTHER; PTHR16059:SF13; ANTHRAX TOXIN RECEPTOR 2; 1.
DR   Pfam; PF05586; Ant_C; 1.
DR   Pfam; PF05587; Anth_Ig; 1.
DR   Pfam; PF00092; VWA; 1.
DR   PIRSF; PIRSF038023; Anthrax_toxin_receptor_2; 1.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS50234; VWFA; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Membrane; Metal-binding; Phosphoprotein;
KW   Receptor; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..487
FT                   /note="Anthrax toxin receptor 2"
FT                   /id="PRO_0000002695"
FT   TOPO_DOM        32..318
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        319..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        340..487
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          44..213
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   BINDING         52
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P58335"
FT   BINDING         54
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P58335"
FT   BINDING         118
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P58335"
FT   MOD_RES         147
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P58335"
FT   CARBOHYD        260
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        39..218
FT                   /evidence="ECO:0000250|UniProtKB:P58335"
SQ   SEQUENCE   487 AA;  53184 MW;  61A400D60BC8DE69 CRC64;
     MVAGRSRARS PGSWLFPGLW LLAVGGPGSL LQAQEQPSCK KAFDLYFVLD KSGSVANNWI
     EIYNFVHQLT ERFVSPEMRL SFIVFSSQAT IILPLTGDRY KIGKGLEDLK AVKPVGETYI
     HEGLKLANEQ IQNAGGLKAS SIIIALTDGK LDGLVPSYAE NEAKKSRSLG ASVYCVGVLD
     FEQAQLERIA DSKDQVFPVK GGFQALKGII NSILAQSCTE ILELSPSSVC VGEKFQVVLT
     GRAVTSISHD GSVLCTFTAN STYTKSEKPV SIQPSSILCP APVLNKDGET LEVSISYNDG
     KSAVSRSLTI TATECTNGIA AIVAILVLLL LLGAALMWWF WPLCCKVVIK DPPPPPSAPM
     EEEEEDPLPN KKWPTVDASY YGGRGVGGIK RMEVRWGDKG STEEGARLEK AKNAVVMVPE
     EEIPIPSRPP RPRPTHQAPQ TKWYTPIKGR LDALWALIMK QYDRVSLMRP QEGDEGRCIN
     FSRVPHQ
//