ANTR2_MOUSE
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 03-AUG-2022, entry version 126.
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_133738.1.
DR AlphaFoldDB; Q6DFX2; -.
DR SMR; Q6DFX2; -.
DR BioGRID; 215027; 1.
DR STRING; 10090.ENSMUSP00000031281; -.
DR GlyGen; Q6DFX2; 1 site.
DR iPTMnet; Q6DFX2; -.
DR PhosphoSitePlus; Q6DFX2; -.
DR SwissPalm; Q6DFX2; -.
DR MaxQB; Q6DFX2; -.
DR PaxDb; Q6DFX2; -.
DR PRIDE; Q6DFX2; -.
DR ProteomicsDB; 282125; -.
DR Antibodypedia; 24968; 191 antibodies from 34 providers.
DR DNASU; 71914; -.
DR Ensembl; ENSMUST00000031281; ENSMUSP00000031281; ENSMUSG00000029338.
DR GeneID; 71914; -.
DR KEGG; mmu:71914; -.
DR UCSC; uc008yga.1; mouse.
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; QAENKWY; -.
DR OrthoDB; 613698at2759; -.
DR PhylomeDB; Q6DFX2; -.
DR TreeFam; TF328943; -.
DR BioGRID-ORCS; 71914; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Antxr2; mouse.
DR PRO; PR:Q6DFX2; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q6DFX2; protein.
DR Bgee; ENSMUSG00000029338; Expressed in decidua and 203 other tissues.
DR ExpressionAtlas; Q6DFX2; baseline and differential.
DR Genevisible; Q6DFX2; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0022414; P:reproductive process; IMP:MGI.
DR GO; GO:1901998; P:toxin transport; IMP:MGI.
DR Gene3D; 3.40.50.410; -; 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:SF13; PTHR16059:SF13; 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; SSF53300; 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
