ID A0A3B4XGL1_SERLL Unreviewed; 1107 AA.
AC A0A3B4XGL1;
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 3-like {ECO:0000313|Ensembl:ENSSLDP00000017029.1};
GN Name=AGAP3 {ECO:0000313|Ensembl:ENSSLDP00000017029.1};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000017029.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000017029.1}
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; A0A3B4XGL1; -.
DR STRING; 1841481.ENSSLDP00000017029; -.
DR Ensembl; ENSSLDT00000017634.1; ENSSLDP00000017029.1; ENSSLDG00000013245.1.
DR GeneTree; ENSGT00940000159586; -.
DR Proteomes; UP000261360; 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; cd08855; ArfGap_AGAP3; 1.
DR CDD; cd04103; Centaurin_gamma; 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); 1.
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:SF2; ARF-GAP WITH GTPASE, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 3; 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 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; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50115; ARFGAP; 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 848..968
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REPEAT 1007..1039
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1040..1064
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 16..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1068..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1107 AA; 121923 MW; 3AA52D13447074AF CRC64;
MRRSWRRPRS VCMLAGPGPV LSETQTQQPF RRAGILENSQ QHRSRRAELR AVDGLNPIVA
QRPPVPADVT PRVRQRSWRP RPVSMTVLEL RKRGSDDEID SQKSSHTGSD GGFLKGSFRW
RLFSKAPQDK SKEMDGGNDV KPSPKLSKPD APKSTLSNLR RSLSLRIRRT RPRDKVSLGS
EGEWKEGSRT KSTAEEITMP PRPFSYLTGR TLPTSSEQIE DGGMQYIQYH SRGKVKVMEV
PLCPTKLSSK PVQEEPSIWQ LIANRFRRKE QPYSGKCESQ QSQSKDTGQY PLAGDNKSEP
VSIETLAGID SHKGQDSFVN SQEWTLSRSV PELKVGIVGN LSSGKSALVH RYLTGTYVQE
ESPEGGRFKK EIVVDGQSYL LLIRDEGGPP ELQFAAWVDA VVFVFSLEDE ISFQTVYNYF
VRLSSYRNTA EVPMVLVGTQ DAISAANPRV IDDSRARKLS NDLKRCTYYE TCSTYGLNVE
RVFQDVAQKV VAMRKKQQLS IGPCKSLPNS PSHSSVPAAS IPSVHINQAA NGGGAFSDYS
SSVPSTPSIS QREMRIETIA ASNTPTPIRK QSKRRSNIFT SRKASEQAKS VDSKTDSIGS
GRAIPIKQGI LLKRSGKSLN KEWKKKYVTL CDNGVLTYHP SLHDYMQNVH GKEIDLLRTT
VKVPGKRPPR AVATVAPTAS PKTNGLTKDR STLQLGIGNT GAPHSNSSTS LQTGASVFAG
SKDGMHQRSF SVSSADQWNE AINTTNGTSD PANSSVGSAT SPKLEPPPSP HANRKKHRRK
KSTGITKPDG LSGGNEGTKN YINGLRRFLT GQIFTYQFCL IYGAIRSFPL TYSFPCSSQS
RLGSQSDAMA IQSIRNVRGN SFCVDCDAPN PDWASLNLGA LMCIECSGIH RNLGTHLSRV
RSLDLDDWPV ELSMVMTAIG NTMANSVWEG ALEGYTKPGS DSTREEKERW IRAKYEQKLF
VVGLPQSDVP LGQQLLRAVV EDDLRLVVVL LAHGTKEEVN ETYGDGDGRT ALHLSCAMAN
VVITQLLIWY GVDVKSRDAR GQTPLSYARR AGSQECADIL LQHGCPNDTS TLTSVPTPNM
SRRNPNPNPN INNNNAQCEL NRSISIM
//
