ID A0A3B3DRI5_ORYME Unreviewed; 1150 AA.
AC A0A3B3DRI5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1 {ECO:0000313|Ensembl:ENSOMEP00000031970.1};
GN Name=AGAP1 {ECO:0000313|Ensembl:ENSOMEP00000031970.1};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000031970.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000031970.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the centaurin gamma-like family.
CC {ECO:0000256|ARBA:ARBA00005430}.
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DR AlphaFoldDB; A0A3B3DRI5; -.
DR Ensembl; ENSOMET00000034020.1; ENSOMEP00000031970.1; ENSOMEG00000017185.1.
DR GeneTree; ENSGT00940000154793; -.
DR Proteomes; UP000261560; 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 CDD; cd08836; ArfGap_AGAP; 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; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00173; RAS; 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 Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00288}.
FT DOMAIN 610..879
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 900..1020
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REPEAT 1059..1091
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 27..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1129..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1150 AA; 125759 MW; AA511F98E34C3CBB CRC64;
MYLLDSMERG SPQRRTVYRI SLTLVKKESM DEDQPQQAGD ATPGGFGREG SMEVQRGGQL
EELREVEDEA EEFSPSRGFL RSFRTFSTGQ LELGKLKSCK KLLKARSPLA EQKKEMPGPG
PDGEGSGPAQ NGSSSKRKRL LKAKSVEDKR SEPPVNGDGP ACPGTPPLKP APLHRSFSFR
HWSGSELLRA LSRDKQHSSS GSIAPRPPDP AREKSRTLEV GAVLNRTESL TELSREAKNR
TLDNSDLLLL KDADGRGGFL RGGGGRSSER RLVRFFSGIF RREGAASPAG SPGTGRSLRR
SRRTPLTQSS SESMNGTDDA FVNSQEWTLS RTVPELKVGI VGNLASGKSA LVHRYLTGTY
VQEESPEGGR FKKEIVVDGQ SHLLLIRDEG GPPEAQFALW VDAVIFVFSL EDEISFQTVY
HYYNRLANFR NTTELPLVLV GTQDAISSTN PRVIDDSRAR KLSNELKRCT YYETCATYGL
NVERVFQDVA QKIVATRKKQ QLSIGPCKSL PNSPSHSSVC TTQVSAVHVS QTSNGGGSLS
DYSSSVPSTP STSQKELRID VPPATNTPTP VRKQSKRRSN LFTSRKANEP DKEKKGLEAR
ADSIGSGRAI PIKQGMLLKR SGKSLNKEWK KKYVTLCDNG VLTYHPSLHD YMQNVHGKEI
NLLRTTVKVP GKRPPRAIST CAAVPSPNTN GLTKEMSGLQ LGQTPGSVSS SASVSQMPSG
VSLVSFSSRG VEGMHQRSFS VSSADQWADA TVIANSGVST DTGLGDSVCS SPSISSTSPK
MEPPPSPHAN RKKHRRKKST SNFKADGLSG TAEAKRRAWK LNRVSSLRSV YANSLQNSEE
QEENFEFIIV SLTGQTWHFE ATSYEERDAW VQVIESQILA SLQSCESSKI KSRLSSQTEA
LALQSIRSIR GNGRCADCDT QNPDWASLNL GALICIECSG IHRNLGTHLS RVRSLDLDDW
PLELIKVMSA IGNEVANSVW EANAQGRMKP GPDATREERE RWIRAKYEQR LFLAPLPSTD
LSLGQQLLRA TAEEDQRSVV LLLAHGSRQQ VNETCGDGDG RNALHLASLK GNVILAQLLI
WYGVDLMARD ACGNSAMAYA RQANCQECVD ILAQYGCTDE RHPLVATPNL SRRNTNRNNS
CSSTGSTALI
//
