ID A0A1U7QW48_MESAU Unreviewed; 857 AA.
AC A0A1U7QW48;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1 isoform X5 {ECO:0000313|RefSeq:XP_005082279.1};
GN Name=Agap1 {ECO:0000313|RefSeq:XP_005082279.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_005082279.1};
RN [1] {ECO:0000313|RefSeq:XP_005082279.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the centaurin gamma-like family.
CC {ECO:0000256|ARBA:ARBA00005430}.
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DR RefSeq; XP_005082279.1; XM_005082222.3.
DR AlphaFoldDB; A0A1U7QW48; -.
DR STRING; 10036.ENSMAUP00000013095; -.
DR GeneID; 101839678; -.
DR KEGG; maua:101839678; -.
DR CTD; 116987; -.
DR eggNOG; KOG0705; Eukaryota.
DR OrthoDB; 1449795at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
DR CDD; cd08853; ArfGap_AGAP2; 1.
DR CDD; cd04103; Centaurin_gamma; 1.
DR CDD; cd01250; PH_AGAP; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001806; Small_GTPase.
DR PANTHER; PTHR45819:SF1; ARF-GAP WITH GTPASE, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR45819; CENTAURIN-GAMMA-1A; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00173; RAS; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS51419; RAB; 1.
DR PROSITE; PS51421; RAS; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00288}.
FT DOMAIN 346..588
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 609..729
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REPEAT 768..800
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 267..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 857 AA; 94403 MW; F13BF0CA045732CD CRC64;
MNYQQQLANS AAIRAEIQRF ESVHPNIYAI YDLIERIEDL ALQNQIREHV IAIEDAFVNS
QEWTLSRSVP ELKVGIVGNL ASGKSALVHR YLTGTYVQEE SPEGGRFKKE IVVDGQSYLL
LIRDEGGPPE AQFAMWVDAV IFVFSLEDEI SFQTVYHYYS RMANYRNTSE IPLVLVGTQD
AISSTNPRVI DDARARKLSN DLKRCTYYET CATYGLNVER VFQDVAQKIV ATRKKQQLSI
GPCKSLPNSP SHSSVCSAQV SAVHISQTSN GGGSLSDYSS SVPSTPSTSQ KELRIDVPPT
ANTPTPVRKQ SKRRSNLFTS RKGSDPDKEK KGLESRADSI GSGRAIPIKQ GMLLKRSGKS
LNKEWKKKYV TLCDNGVLTY HPSLHDYMQN VHGKEIDLLR TTVKVPGKRP PRATSACAPI
SSPKTNGLSK DMSSLHISPN SGNVTSASGS QMASGISLVS FNSRPDGMHQ RSYSVSSADQ
WSDATVIANS AISSDTGLGD SVCSSPSISS STSPKLDPPP SPHANRKKHR RKKSTSNFKA
DGLSGTAEEQ EENFEFIIVS LTGQTWHFEA TTYEERDAWV QAIESQILAS LQSCESSKNK
SRLTSQSEAM ALQSIRNMRG NSHCVDCDVQ NPNWASLNLG ALMCIECSGI HRNLGTHLSR
VRSLDLDDWP MELIKVMSSI GNELANSVWE ESSQGRTKPS LDSTREEKER WIRAKYEQKL
FLAPLPCAEF SLGQQLLRAT AEEDLRTVIL LLAHGSRDEV NETCGEGDGR TALHLACRKG
NVVLAQLLIW YGVDVMARDA HGNTALAYAR QASSQECIDV LLQYGCPDER FVLMATPNLS
RKSNSRNNSS GRAPSII
//
