ID A0A091TXH4_PHALP Unreviewed; 757 AA.
AC A0A091TXH4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=N335_02898 {ECO:0000313|EMBL:KFQ82250.1};
OS Phaethon lepturus (White-tailed tropicbird).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Eurypygimorphae; Phaethontiformes;
OC Phaethontidae; Phaethon.
OX NCBI_TaxID=97097 {ECO:0000313|EMBL:KFQ82250.1, ECO:0000313|Proteomes:UP000053638};
RN [1] {ECO:0000313|EMBL:KFQ82250.1, ECO:0000313|Proteomes:UP000053638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N335 {ECO:0000313|EMBL:KFQ82250.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KK466670; KFQ82250.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091TXH4; -.
DR PhylomeDB; A0A091TXH4; -.
DR Proteomes; UP000053638; 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; cd08851; ArfGap_ACAP2; 1.
DR CDD; cd07638; BAR_ACAP2; 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};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000053638};
KW 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 250..345
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 383..505
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REPEAT 619..651
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 652..684
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 349..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 101..131
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 349..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ82250.1"
FT NON_TER 757
FT /evidence="ECO:0000313|EMBL:KFQ82250.1"
SQ SEQUENCE 757 AA; 85728 MW; E9DBDAC16E670D3E CRC64;
FRAALEEVEG DVTELELKLD KLVKLCIAMI DTGKAFCTAN KQFMNGIRDL AQYSCKDALV
ETSLTKFSDT LQEMINYHNI LFDQTQRSIK AQLQSFVKED IRKFKDAKKQ FEKVSEEKEN
ALVKNAQVQR NKQHEVEEAT NILTATRKCF RHIALDYVLQ INVLQSKRRA EILKSMLSFM
YAHLAFFHQG YDLFSELEPY MKDLGAQLDQ LAVDAAKEKR DMEQKHSTIQ QKDYSSDDTK
LEYNVDAANG IVMEGYLFKR ASNAFKTWNR RWFSIQNNQL VYQKKFKDNP TVVVEDLRLC
TVKHCEDIER RFCFEVVSPT KSCMLQADSE KLRQAWIKAV QTSIATAYRE KGDESEKQEK
KSSPSTGSLE SGSETKEKLL KGESALQRVQ CIPGNAACCD CGLADPRWAS INLGITLCIE
CSGIHRSLGV HFSKVRSLTL DSWEPELLKL MCELGNDVIN RIYEAKLEKV GVKKPQPGSQ
RQEKEAYIRA KYVERKFVEK QPASVSLLES GTKVLPQSQE EKRHSGPREQ GVAFQKVQSS
DSGIQQSTDD SREHLASTMS ANSLYEPERD KRESSVFCDS KQPSPGLQLY RAAFEKNLPD
MAEALAHGAE VNWVNIEENK ATPLIQAVRG GSLVTCEFLL QNGANVNIRD MKGRGPLHHA
TVLGHTGQVC LFLKRGANQH ATDEDGKDPL SIAVEAANAD IVTLLRLARM NEEMRESEGL
YGQPGDEIYQ DIFRDFSQMA SNNPEKLNRF QQSDSQK
//
