ID A0A3P8SEA6_AMPPE Unreviewed; 862 AA.
AC A0A3P8SEA6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=ArfGAP with GTPase domain, ankyrin repeat and PH domain 1 {ECO:0000313|Ensembl:ENSAPEP00000010049.1};
GN Name=AGAP1 {ECO:0000313|Ensembl:ENSAPEP00000010049.1};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000010049.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000010049.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000010049.1}
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; A0A3P8SEA6; -.
DR Ensembl; ENSAPET00000010323.1; ENSAPEP00000010049.1; ENSAPEG00000007151.1.
DR GeneTree; ENSGT00940000154793; -.
DR OMA; WYGANIK; -.
DR Proteomes; UP000265080; Chromosome 24.
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 Reference proteome {ECO:0000313|Proteomes:UP000265080};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00288}.
FT DOMAIN 346..591
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 612..732
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REPEAT 771..803
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 266..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 862 AA; 94550 MW; 1CFA46874031055D CRC64;
MNYQQHLANS AAIRAEIQRF ESVHPNIYSI YELLERLDEP LLQNQIREHV IAIEDAFVNS
QEWTLSRTVP ELKVGIVGNL ASGKSALVHR YLTGTYVQEE SPEGGRFKKE MVVDGQSHLL
LIRDEGGPPE AQFALWVDAV IFVFSLEDEI SFQTVYHYFS RLAGFRNTAE LPLVLVGTQD
AISSANPRVI DDSRARKLSS DLKRCTYYET CATYGLNVER VFQDVAQKIV ATRKKQQLSI
GPCKSLPNSP SHSSVCSTQV SAVHISQTSN GGGSLSDYSS SVPSTPSTSQ KELRIDVPPA
TNTPTPVRKQ SKRRSNLFTS RKASEADKDK KGLEARADSI GSGRAIPIKQ GMLLKRSGKS
LNKEWKKKYV TLCDNGLLTY HPSLHDYMQN VHGKEIDLLR TTVKVPGKRP PRAVSTCAAV
PSPKTNGLTK DMSSLQLGQN PGSVTSSSSA SQMASGVSLV SFNSRGGLEG MHQRSYSISS
ADQWTDATVI ANSGVSTDTG LGDSVCSSPS ISSTTSPKME PPPSPHANRK KHRRKKSTSN
FKADGLSGTA EEQEENFEFT IVSLTGQSWH FEATSYEERD AWVQVIESQI LASLQSCESS
KNKSRLTSQT EAMALQSIRS IRGNGRCADC EAQNPDWASL NLGALICIEC SGIHRNLGTH
LSRVRSLDLD EWPLELIKVM SAIGNELANS VWEANAQGRL KPGPDASREE RERWIRAKYE
QRLFVASLPC MDLPLGQQLL RATADEDLRA VVLLLAHGNR QQVNETCGEG DGRNALHLAS
RKGNVVITQL LIWYGVDLMA KDAHGNSAMA YARQASCQEC VDTLTQYGCP DDRYPLMATP
NLSRRNTNRN NSCSSAGSAA LI
//
