ID A0A3B3ZSP1_9GOBI Unreviewed; 61 AA.
AC A0A3B3ZSP1;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
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 Periophthalmus magnuspinnatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000007712.1, ECO:0000313|Proteomes:UP000261520};
RN [1] {ECO:0000313|Ensembl:ENSPMGP00000007712.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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
CC {ECO:0000256|RuleBase:RU369028}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU369028}.
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; A0A3B3ZSP1; -.
DR STRING; 409849.ENSPMGP00000007712; -.
DR Ensembl; ENSPMGT00000008201.1; ENSPMGP00000007712.1; ENSPMGG00000006392.1.
DR Proteomes; UP000261520; 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 Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR InterPro; IPR045258; ACAP1/2/3-like.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR PANTHER; PTHR23180:SF415; ARF-GAP WITH COILED-COIL, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR23180; CENTAURIN/ARF; 1.
DR Pfam; PF01412; ArfGap; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR PROSITE; PS50115; ARFGAP; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|RuleBase:RU369028};
KW Endosome {ECO:0000256|RuleBase:RU369028};
KW GTPase activation {ECO:0000256|RuleBase:RU369028};
KW Metal-binding {ECO:0000256|RuleBase:RU369028};
KW Repeat {ECO:0000256|RuleBase:RU369028};
KW Zinc {ECO:0000256|RuleBase:RU369028};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00288}.
FT DOMAIN 16..61
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
SQ SEQUENCE 61 AA; 6825 MW; 7BFA1B829DA4B4A3 CRC64;
TSNEPNKIKY IIFGNRTIDC PTNVCCDCGQ SNPCWASINL GILLCIECSG IHRYDIIHYC
S
//
