ID A0A2R9BTL9_PANPA Unreviewed; 813 AA.
AC A0A2R9BTL9;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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};
GN Name=ACAP2 {ECO:0000313|Ensembl:ENSPPAP00000029926.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000029926.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000029926.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000029926.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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DR EMBL; AJFE02022450; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02022451; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02022452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02022453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02022454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02022455; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02022456; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02022457; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02022458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02022459; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_008958041.1; XM_008959793.2.
DR AlphaFoldDB; A0A2R9BTL9; -.
DR Ensembl; ENSPPAT00000052780.1; ENSPPAP00000029926.1; ENSPPAG00000037793.1.
DR GeneID; 100969566; -.
DR CTD; 23527; -.
DR GeneTree; ENSGT00940000156389; -.
DR OrthoDB; 1449795at2759; -.
DR Proteomes; UP000240080; Chromosome 3.
DR Bgee; ENSPPAG00000037793; Expressed in testis and 6 other cell types or tissues.
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:UP000240080};
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 266..361
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 399..520
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REPEAT 675..707
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 708..740
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 371..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 594..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 117..147
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 217..248
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 594..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 813 AA; 92023 MW; A79FE313B0B861A4 CRC64;
MKMTVDFEEC LKDSPRFRAA LEEVEGDVAE LELKLDKLVK LCIAMIDTGK AFCVANKQFM
NGIRDLAQYS SNDAVVETSL TKFSDSLQEM INFHTILFDQ TQRSIKAQLQ NFVKEDLRKF
KDAKKQFEKV SEEKENALVK NAQVQRNKQH EVEEATNILT ATRKCFRHIA LDYVLQINVL
QSKRRSEILK SMLSFMYAHL AFFHQGYDLF SELGPYMKDL GAQLDRLVVD AAKEKREMEQ
KHSTIQQKDF SSDDSKLEYN VDAANGIVME GYLFKRASNA FKTWNRRWFS IQNNQLVYQK
KFKDNPTVVV EDLRLCTVKH CEDIERRFCF EVVSPTKSCM LQADSEKLRQ AWIKAVQTSI
ATAYREKGDE SEKLDKKSSP STGSLDSGNE SKEKLLKGES ALQRVQCIPG NASCCDCGLA
DPRWASINLG ITLCIECSGI HRSLGVHFSK VRSLTLDTWE PELLKLMCEL GNDVINRVYE
ANVEKMGIKK PQPGQRQEKE AYIRAKYVER KFVDKYSISL SPPEQQKKFV SKSSEEKRLS
ISKFGPGDQV RASAQSSVIA VNSDEARRES LFCPDELDSL FSYFDTSSKL RSIRSNDSGI
QQSSDDGRES LPSTVSANSL YEPEGERQDS SMFLDSKHLN PGLQLYRASY EKNLPKMAEA
LAHGADVNWA NSEENKATPL IQAVLGGSLV TCEFLLQNGA NVNQRDVQGR GPLHHATVLG
HTGQVCLFLK RGANQHATDE EGKDPLSIAV EAANADIVTL LRLARMNEEM RESEGLYGQP
GDETYQDIFR DFSQMASNNP EKLNRFQQDS QKF
//
