ID A0A3B3DUZ3_ORYME Unreviewed; 720 AA.
AC A0A3B3DUZ3;
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 Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000033264.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000033264.1}
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; A0A3B3DUZ3; -.
DR STRING; 30732.ENSOMEP00000033264; -.
DR PaxDb; 30732-ENSOMEP00000033264; -.
DR Ensembl; ENSOMET00000026210.1; ENSOMEP00000033264.1; ENSOMEG00000019171.1.
DR GeneTree; ENSGT00940000156389; -.
DR OMA; DEFVCER; -.
DR OrthoDB; 1449795at2759; -.
DR Proteomes; UP000261560; 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; cd07603; BAR_ACAPs; 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:SF402; ARF-GAP WITH COILED-COIL, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN; 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}; Endosome {ECO:0000256|RuleBase:RU369028};
KW GTPase activation {ECO:0000256|RuleBase:RU369028};
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 263..358
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 395..517
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REPEAT 559..591
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 592..624
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 681..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..702
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 720 AA; 80267 MW; 6E7D2A1C06B4B644 CRC64;
MDTLLDFEEC VRDSPEFRLA LDQFEADVSL VEAQLQKVMK LSGKMVEAGQ TYKAANQLFL
SGLAELSTNH RREGVVTSCL DQFQQGLQEA LSFHSMLLDQ TQRAIGQQLS SLCSQFLPQL
AETRKEFVRI GENLETAVLK NAQVSRHKAS DAERTSHLLL ATRKCYQHFA LDYCLQLNTF
RIQHKVDILN SVFSFVQAQF TFFHQGFDLL RDLEPTMKTM AMQLSQLSAD CSTKKKELEN
QHLLVQQRDA SGEPMVSPRP DSDHVLQGYL FKRSRRRPKT WKRCWFTIRD NQLIYRRSHK
EEPAVLFEDL RLCAVKPLEH ADRRFCFELL SVQRCCALQA DSEQLKRAWL AALQGSIDLA
YRRGGGDVAP TQQVKEAPPL LWGGDASPAP PPLRQAVLGV ALEGPGNKQC CDCREAEPRW
ASVNLGVTMC IECSGIHRSL GVHLSKVRSL TLDSWEAEQL KLLCILGNEV MNRIYEARCS
EQQSLRPGPG SPRSEKEAWI REKYVEKRFV LHGGSDGAET QRDEAGRRLY RASVEGDLVA
MATALAQGAE VNGSISEEEG RTPLIGAAVG GSLLACEFLL QNGANVNHRD LRGRGALHTA
ATAGHTGQVC LLLKRGANQY AVDERGQDPL AIAVETAHAD IVTLLRMARM NEEMRDSEGV
FGAAGDDETF QDIIRDFSDM ASHDPERLSR RHLSRGGEEE AEQEGGGGAN CKLSVQKSFD
//
