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Database: UniProt
Entry: A0A3L8RRV9_CHLGU
LinkDB: A0A3L8RRV9_CHLGU
Original site: A0A3L8RRV9_CHLGU 
ID   A0A3L8RRV9_CHLGU        Unreviewed;       348 AA.
AC   A0A3L8RRV9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
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};
DE   Flags: Fragment;
GN   ORFNames=DV515_00016659 {ECO:0000313|EMBL:RLV82427.1};
OS   Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC   Chloebia.
OX   NCBI_TaxID=44316 {ECO:0000313|EMBL:RLV82427.1, ECO:0000313|Proteomes:UP000276834};
RN   [1] {ECO:0000313|EMBL:RLV82427.1, ECO:0000313|Proteomes:UP000276834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Red01 {ECO:0000313|EMBL:RLV82427.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:RLV82427.1};
RX   PubMed=30282656;
RA   Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA   Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT   "A non-coding region near Follistatin controls head colour polymorphism in
RT   the Gouldian finch.";
RL   Proc. R. Soc. B 285:0-0(2018).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RLV82427.1}.
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DR   EMBL; QUSF01000391; RLV82427.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3L8RRV9; -.
DR   STRING; 44316.ENSEGOP00005021617; -.
DR   Proteomes; UP000276834; Unassembled WGS sequence.
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; cd13250; PH_ACAP; 1.
DR   Gene3D; 1.10.220.150; Arf GTPase activating protein; 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; IPR037278; ARFGAP/RecO.
DR   InterPro; IPR001164; ArfGAP_dom.
DR   InterPro; IPR038508; ArfGAP_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
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; PF01412; ArfGap; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00105; ArfGap; 1.
DR   SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 2.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 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   Reference proteome {ECO:0000313|Proteomes:UP000276834};
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          1..58
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          84..247
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50115"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:RLV82427.1"
SQ   SEQUENCE   348 AA;  38378 MW;  AE86894B0546BC1D CRC64;
     DVLTVVVEDL RLCTVKPCED IERRFCFEVV SPTKSCMLQA DSEKLRQAWI QAVQASIACA
     YRESPDCCYG ESAAEGRERG GRGEPLLRRL QSAPGNERCC DCGRPDPRWA SINLGVLLCI
     ECSGIHRSLG VHCSKVRSLT LDSWEPELLK VSAGRNAGNA GILWKRGNSS PEEFNSLRGF
     HFQLMCELGN STMNQIYEAQ CEELGLKKPT AGSSRQDKEA WIKVKYVEKK FLRKLPGGEV
     LAESERKPRR WSLKRCQRLH GGCRAPAARR KLRPEPAGAA AALASAAATL ERKFRRDSLF
     CPDELDSLFS YFDTGAGSGP RTFSLTSVRG AVARKGSGCS GMTLVKNL
//
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