ADAP2_RAT
ID ADAP2_RAT Reviewed; 376 AA.
AC Q9JK15;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
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 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], INTERACTION WITH PTDINS(4,5)P2; PTDINS(3,4,5)P3
RP AND INS(1,3,4,5)P4, TISSUE SPECIFICITY, AND MUTAGENESIS OF ARG-151 AND
RP ARG-275.
RC TISSUE=Adipocyte;
RX PubMed=12018390; DOI=10.1078/0171-9335-00242;
RA Whitley P., Gibbard A.M., Koumanov F., Oldfield S., Kilgour E.E.,
RA Prestwich G.D., Holman G.D.;
RT "Identification of centaurin-alpha2: a phosphatidylinositide-binding
RT protein present in fat, heart and skeletal muscle.";
RL Eur. J. Cell Biol. 81:222-230(2002).
CC -!- FUNCTION: GTPase-activating protein for the ADP ribosylation factor
CC family (Potential). Binds phosphatidylinositol 4,5-bisphosphate,
CC phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and inositol
CC 1,3,4,5-tetrakisphosphate (InsP4). Binding of phosphatidylinositol 3,5-
CC bisphosphate and phosphatidylinositol 3,4-bisphosphate occurs at a much
CC lower affinity. Possesses a stoichiometry of two binding sites for
CC InsP4 with identical affinity (By similarity). {ECO:0000250,
CC 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}.
CC -!- TISSUE SPECIFICITY: Expressed in many tissues, with highest levels in
CC fat, heart and skeletal muscle. Also detected in kidney, liver and
CC lung. {ECO:0000269|PubMed:12018390}.
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DR EMBL; AJ238993; CAB88403.1; -; mRNA.
DR RefSeq; NP_064486.1; NM_020101.1.
DR AlphaFoldDB; Q9JK15; -.
DR SMR; Q9JK15; -.
DR STRING; 10116.ENSRNOP00000053112; -.
DR PhosphoSitePlus; Q9JK15; -.
DR PaxDb; Q9JK15; -.
DR PRIDE; Q9JK15; -.
DR GeneID; 56826; -.
DR KEGG; rno:56826; -.
DR CTD; 55803; -.
DR RGD; 708487; Adap2.
DR eggNOG; KOG0703; Eukaryota.
DR InParanoid; Q9JK15; -.
DR OrthoDB; 1274375at2759; -.
DR PhylomeDB; Q9JK15; -.
DR PRO; PR:Q9JK15; -.
DR Proteomes; UP000002494; Unplaced.
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; IDA:RGD.
DR GO; GO:0005740; C:mitochondrial envelope; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; IDA:RGD.
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; IDA:UniProtKB.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0048017; P:inositol lipid-mediated signaling; ISO:RGD.
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..376
FT /note="Arf-GAP with dual PH domain-containing protein 2"
FT /id="PRO_0000074208"
FT DOMAIN 9..130
FT /note="Arf-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00288"
FT DOMAIN 131..232
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 254..360
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"
FT MUTAGEN 151
FT /note="R->C: Almost complete loss of InsP4 binding."
FT /evidence="ECO:0000269|PubMed:12018390"
FT MUTAGEN 275
FT /note="R->C: No loss of InsP4 binding. Almost complete loss
FT of InsP4 binding; when associated with C-151."
FT /evidence="ECO:0000269|PubMed:12018390"
SQ SEQUENCE 376 AA; 43524 MW; E357392F38F07166 CRC64;
MGDRERNKKR LLELLQAAGT GNGHCADCGA ADPDWASYKL GVFICLHCSG VHRNFPDISK
VKSVRLDFWD DSMVEFMTHN GNLSVKAKFE ARVPTFYYVP QASDCLVLKE QWIRAKYERQ
EFMAEKAVSP PGDREGFLWK RGRDNSQFLR RRFVLLSREG LLKYYTKEEG KTPKAIINIK
DLNATFQTEK IGHPHGLQIT YRKEGQTRNL FVYHDSGKEI VDWFNALRAA RLQYLKLAFP
DLPESELVPL ITRNYLKQGF MEKTGPKHRE PFKKRWFALD PQERRLLYYK NPLDAFEQGQ
VFLGSNEQGY EVWEGLPQGI RGNRWKVGLT VITPERKFVF TCPTEKEQRE WLESLRGVLS
SPLSPLHLLT TSAKSG
