ID A0A3B3VMR6_9TELE Unreviewed; 240 AA.
AC A0A3B3VMR6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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 Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000026129.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000026129.1}
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; A0A3B3VMR6; -.
DR STRING; 48699.ENSPLAP00000026129; -.
DR Ensembl; ENSPLAT00000028921.1; ENSPLAP00000026129.1; ENSPLAG00000013685.1.
DR GeneTree; ENSGT00940000156199; -.
DR Proteomes; UP000261500; 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; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR InterPro; IPR045258; ACAP1/2/3-like.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR PANTHER; PTHR23180:SF407; ARF-GAP WITH COILED-COIL, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 3; 1.
DR PANTHER; PTHR23180; CENTAURIN/ARF; 1.
DR Pfam; PF16746; BAR_3; 2.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 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|RuleBase:RU369028}.
FT DOMAIN 26..76
FT /note="BAR"
FT /evidence="ECO:0000259|Pfam:PF16746"
FT DOMAIN 77..220
FT /note="BAR"
FT /evidence="ECO:0000259|Pfam:PF16746"
SQ SEQUENCE 240 AA; 27758 MW; EF3D2C90C4DA48EB CRC64;
RKTGPCVCYC LAGQYLFFAT RISQIRSSVK ALQLIPNLVK LCSGMIEAGK AYISANKLFV
NGIRDLSQQC KKDEMISILF DQAQRSVKQQ LHNFVKEDVR KFKETKKHFD RVREDMEIAQ
VKNAQAPRNK PHEVEEATSA LSITRKCFRH LALDYVLQIN VLQAKKKFEI LDAMLSFMNA
QFSLFQQGYN LLDELDPYMK KLAAELDQLV IHSAMEKREM EHKHATIQQR VSCCFILFSF
//
