ADAP2_MOUSE
ID ADAP2_MOUSE Reviewed; 381 AA.
AC Q8R2V5;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Arf-GAP with dual PH domain-containing protein 2;
DE AltName: Full=Centaurin-alpha-2;
DE Short=Cnt-a2;
GN Name=Adap2; Synonyms=Centa2;
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=FVB/N; TISSUE=Mammary tumor;
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=Spleen;
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: GTPase-activating protein for the ADP ribosylation factor
CC family (Potential). Binds phosphatidylinositol 3,4,5-trisphosphate
CC (PtdInsP3) and inositol 1,3,4,5-tetrakisphosphate (InsP4). Possesses a
CC stoichiometry of two binding sites for InsP4 with identical affinity
CC (By similarity). {ECO:0000250, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Note=Constitutively associated with the plasma membrane.
CC Excluded from the nucleus (By similarity). {ECO:0000250}.
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DR EMBL; BC027165; AAH27165.1; -; mRNA.
DR CCDS; CCDS25128.1; -.
DR RefSeq; NP_742145.1; NM_172133.1.
DR AlphaFoldDB; Q8R2V5; -.
DR SMR; Q8R2V5; -.
DR BioGRID; 229830; 1.
DR STRING; 10090.ENSMUSP00000021050; -.
DR iPTMnet; Q8R2V5; -.
DR PhosphoSitePlus; Q8R2V5; -.
DR EPD; Q8R2V5; -.
DR MaxQB; Q8R2V5; -.
DR PaxDb; Q8R2V5; -.
DR PRIDE; Q8R2V5; -.
DR ProteomicsDB; 296061; -.
DR Antibodypedia; 26908; 187 antibodies from 30 providers.
DR DNASU; 216991; -.
DR Ensembl; ENSMUST00000021050; ENSMUSP00000021050; ENSMUSG00000020709.
DR GeneID; 216991; -.
DR KEGG; mmu:216991; -.
DR UCSC; uc007klk.1; mouse.
DR CTD; 55803; -.
DR MGI; MGI:2663075; Adap2.
DR VEuPathDB; HostDB:ENSMUSG00000020709; -.
DR eggNOG; KOG0703; Eukaryota.
DR GeneTree; ENSGT00940000156498; -.
DR HOGENOM; CLU_061583_0_0_1; -.
DR InParanoid; Q8R2V5; -.
DR OMA; MVLKEQW; -.
DR OrthoDB; 1274375at2759; -.
DR PhylomeDB; Q8R2V5; -.
DR TreeFam; TF324540; -.
DR BioGRID-ORCS; 216991; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Adap2; mouse.
DR PRO; PR:Q8R2V5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8R2V5; protein.
DR Bgee; ENSMUSG00000020709; Expressed in rostral migratory stream and 137 other tissues.
DR ExpressionAtlas; Q8R2V5; baseline and differential.
DR Genevisible; Q8R2V5; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005740; C:mitochondrial envelope; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0043533; F:inositol 1,3,4,5 tetrakisphosphate binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0048017; P:inositol lipid-mediated signaling; ISO:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR CDD; cd13252; PH1_ADAP; 1.
DR CDD; cd01251; PH2_ADAP; 1.
DR Gene3D; 1.10.220.150; -; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR037849; PH1_ADAP.
DR InterPro; IPR037851; PH2_ADAP.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00169; PH; 2.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 2.
DR SUPFAM; SSF57863; SSF57863; 1.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; GTPase activation; Membrane; Metal-binding;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..381
FT /note="Arf-GAP with dual PH domain-containing protein 2"
FT /id="PRO_0000074207"
FT DOMAIN 9..132
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT DOMAIN 132..233
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 255..361
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 25..48
FT /note="C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
SQ SEQUENCE 381 AA; 43989 MW; 2E504CEF0ACD84D5 CRC64;
MGDRERNKKR LLELLQAAGT GNGHCADCGA ADPDWASYKL GIFICLHCSG VHRNFPDISK
VKSVRLDFWD DSMVEFMTHH GNLNVKAKFE ARVPAFYYVP QANDCLVLKE QWIRAKYERQ
EFTAIDKAVS HPGNREGFLW KRGRDNAQFL RRRFVLLSRE GLLKYYTKEE GKAPKAVISI
KDLNATFQTE KIGHPHGLQI TYRKEGHTRN LFVYHDSGKE IVDWFNALRA ARLQYLKLAF
PDLPESELVP LITRNYLKQG FMEKTGPKHR EPFKKRWFAL DPQERRLLYY KNPLDAFELG
QVFLGSNEQG YEVWEDLPKG IRGNRWKAGL TVITPERKFI FTCPTEKEQR EWLESLRGVL
SSPLSPLHLL TTSAETGCGL G
