ANTR1_RAT
ID ANTR1_RAT Reviewed; 562 AA.
AC Q0PMD2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Anthrax toxin receptor 1;
DE Flags: Precursor;
GN Name=Antxr1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Brown Norway/Mcwi;
RA Nye S.H., Evans D.L., Baye J.;
RT "Genetic susceptibility to anthrax lethal toxin in rats.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Plays a role in cell attachment and migration. Interacts with
CC extracellular matrix proteins and with the actin cytoskeleton. Mediates
CC adhesion of cells to type 1 collagen and gelatin, reorganization of the
CC actin cytoskeleton and promotes cell spreading. Plays a role in the
CC angiogenic response of cultured umbilical vein endothelial cells.
CC {ECO:0000250|UniProtKB:Q9H6X2}.
CC -!- SUBUNIT: Interacts with gelatin and type 1 collagen. Interacts with the
CC actin cytoskeleton. {ECO:0000250|UniProtKB:Q9H6X2}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9H6X2};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9H6X2}.
CC Cell projection, lamellipodium membrane {ECO:0000250|UniProtKB:Q9H6X2};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9H6X2}.
CC Cell projection, filopodium membrane {ECO:0000250|UniProtKB:Q9H6X2};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9H6X2}.
CC Note=At the membrane of lamellipodia and at the tip of actin-enriched
CC filopodia. Colocalizes with actin at the base of lamellipodia.
CC {ECO:0000250|UniProtKB:Q9H6X2}.
CC -!- SIMILARITY: Belongs to the ATR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI31854.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=ABH03702.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ789143; ABH03702.1; ALT_INIT; mRNA.
DR EMBL; BC131853; AAI31854.1; ALT_INIT; mRNA.
DR RefSeq; NP_001037714.1; NM_001044249.2.
DR AlphaFoldDB; Q0PMD2; -.
DR SMR; Q0PMD2; -.
DR IntAct; Q0PMD2; 1.
DR STRING; 10116.ENSRNOP00000011675; -.
DR GlyGen; Q0PMD2; 3 sites.
DR iPTMnet; Q0PMD2; -.
DR PhosphoSitePlus; Q0PMD2; -.
DR PaxDb; Q0PMD2; -.
DR GeneID; 362393; -.
DR KEGG; rno:362393; -.
DR UCSC; RGD:1307144; rat.
DR CTD; 84168; -.
DR RGD; 1307144; Antxr1.
DR eggNOG; ENOG502QSKR; Eukaryota.
DR InParanoid; Q0PMD2; -.
DR OrthoDB; 613698at2759; -.
DR PhylomeDB; Q0PMD2; -.
DR TreeFam; TF328943; -.
DR PRO; PR:Q0PMD2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0031527; C:filopodium membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031258; C:lamellipodium membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; ISO:RGD.
DR GO; GO:0005518; F:collagen binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; ISO:RGD.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISO:RGD.
DR GO; GO:0001568; P:blood vessel development; ISO:RGD.
DR GO; GO:1901202; P:negative regulation of extracellular matrix assembly; ISO:RGD.
DR GO; GO:1905050; P:positive regulation of metallopeptidase activity; ISO:RGD.
DR GO; GO:0022414; P:reproductive process; ISO:RGD.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:RGD.
DR GO; GO:1901998; P:toxin transport; IBA:GO_Central.
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:SF11; PTHR16059:SF11; 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 Cell membrane; Cell projection; Disulfide bond; Glycoprotein; Membrane;
KW Metal-binding; Phosphoprotein; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..562
FT /note="Anthrax toxin receptor 1"
FT /id="PRO_0000379880"
FT TOPO_DOM 26..319
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..562
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 42..213
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT REGION 400..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..562
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P58335"
FT BINDING 52
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P58335"
FT BINDING 116
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P58335"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..218
FT /evidence="ECO:0000250|UniProtKB:P58335"
SQ SEQUENCE 562 AA; 62319 MW; 35E9ADB6C92D49F5 CRC64;
MDRAGRLGTG LRGLCVAALV LVCAGQGGRR 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 LAIALLILFL LLALALLWWF WPLCCTVIIK EVPPPPVEES
EEEDDDGLPK KKWPTVDASY YGGRGVGGIK RMEVRWGEKG STEEGAKLEK AKNARVKMPE
QEYEFPEPRN LNNNMRRPSS PRKWYSPIKG KLDALWVLLR KGYDRVSVMR PQPGDTGRCI
NFTRVKNSQP AKYPLNNSYH SSSPPPAPIY TPPPPAPHCP PPAPSAPTPP IPSPPSTLPP
PPQAPPPNRA PPPSRPPPRP SV
