ID A0A3B4TMJ4_SERDU Unreviewed; 724 AA.
AC A0A3B4TMJ4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein {ECO:0000256|RuleBase:RU369028};
DE Short=Cnt-b {ECO:0000256|RuleBase:RU369028};
DE AltName: Full=Centaurin-beta {ECO:0000256|RuleBase:RU369028};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000007217.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000007217.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation factor 6
CC (ARF6). {ECO:0000256|ARBA:ARBA00037592}.
CC -!- FUNCTION: GTPase-activating protein for the ADP ribosylation factor
CC family. {ECO:0000256|RuleBase:RU369028}.
CC -!- ACTIVITY REGULATION: GAP activity stimulated by phosphatidylinositol
CC 4,5-bisphosphate (PIP2) and phosphatidic acid.
CC {ECO:0000256|RuleBase:RU369028}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000256|ARBA:ARBA00004481,
CC ECO:0000256|RuleBase:RU369028}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004481, ECO:0000256|RuleBase:RU369028}.
CC Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- DOMAIN: PH domain binds phospholipids including phosphatidic acid,
CC phosphatidylinositol 3-phosphate, phosphatidylinositol 3,5-bisphosphate
CC (PIP2) and phosphatidylinositol 3,4,5-trisphosphate (PIP3). May mediate
CC protein binding to PIP2 or PIP3 containing membranes.
CC {ECO:0000256|RuleBase:RU369028}.
CC -!- DOMAIN: The BAR domain mediates homodimerization, it can neither bind
CC membrane nor impart curvature, but instead requires the neighboring PH
CC domain to achieve these functions. {ECO:0000256|RuleBase:RU369028}.
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DR AlphaFoldDB; A0A3B4TMJ4; -.
DR Ensembl; ENSSDUT00000007355.1; ENSSDUP00000007217.1; ENSSDUG00000005231.1.
DR GeneTree; ENSGT00940000156389; -.
DR OMA; DWEPEIL; -.
DR Proteomes; UP000261420; Unplaced.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd08835; ArfGap_ACAP; 1.
DR CDD; cd13250; PH_ACAP; 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; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR045258; ACAP1/2/3-like.
DR InterPro; IPR027267; AH/BAR_dom_sf.
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; IPR004148; BAR_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR23180:SF241; ARF-GAP WITH COILED-COIL, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 2; 1.
DR PANTHER; PTHR23180; CENTAURIN/ARF; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF16746; BAR_3; 1.
DR Pfam; PF00169; PH; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 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; PS50003; PH_DOMAIN; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Endosome {ECO:0000256|ARBA:ARBA00022753, ECO:0000256|RuleBase:RU369028};
KW GTPase activation {ECO:0000256|RuleBase:RU369028};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU369028}; Repeat {ECO:0000256|RuleBase:RU369028};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU369028};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00288}.
FT DOMAIN 254..349
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 387..494
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REPEAT 585..617
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 618..650
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 355..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 724 AA; 81837 MW; BD31AFE1C0D3CC01 CRC64;
MVALDFIWVF FCPHRATIEE VEGDVCELES KLDKLVKLCI GMIDAGKAYN AANKQFVNGI
RELAQQSTRD ERGVFTLFCL SLQILFDQAQ RSIKTQLQTF VKDDLRKFKE AKKQFDKVSE
EKEAALIKNA QAPRNKQHEV EEATNILTAT RKCFRHIVLD YVLQINVLQS KRRSEILKSM
LSFMYAHLTF FHQGYDLFSE LQPLMKQLGG QLDQLVVDAA KEKRDMEQKH STIQQKDFSH
DDTKLEYNVD ADNGIAMEGY LFKRASNAFK TWNRRWFSIQ NNQLVYQKKF KDNPTVVVED
LRLCTVKHCE DIERRFCFEV VSPTKSCMMQ ADSEKLRQAW IKAVQNSIAT AFRDKGDDGE
KLDRKSSTST GSLDSGGEPK ERSLKGESAL QKVLAIPGNA CCCDCGQPDP RWASINLGIT
LCIQCSGIHR SLGVHFSKVR SLTLDTWEPE LLKLMCELGN KVINEIYEAR REELGARKPQ
PGDPRLHEED VRAEDCVVPQ KVIQTLCLTV KSADSGIQNS ADGSREMLAN TPSNNSLADE
MVFYEPKEYS PGLQLYWASC ARSLPDMAEA LAHGAEVNWV NTEDDKRTPL IMAVQGGSLV
TCEFLLQNAA NVNQQDTQGR GPLHHATMLG HTGQVCLFLK RGANQNAADI DEKTPLAIAV
EAANADIVTL LRLAKMNEEM REAEGPYSQS GDETYQDIFQ DFTHMASNDP DKLNRYQQYD
PQRP
//
