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Database: UniProt
Entry: A0A2R9BF19_PANPA
LinkDB: A0A2R9BF19_PANPA
Original site: A0A2R9BF19_PANPA 
ID   A0A2R9BF19_PANPA        Unreviewed;       740 AA.
AC   A0A2R9BF19;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   24-JAN-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};
GN   Name=ACAP1 {ECO:0000313|Ensembl:ENSPPAP00000028240.1};
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:ENSPPAP00000028240.1, ECO:0000313|Proteomes:UP000240080};
RN   [1] {ECO:0000313|Ensembl:ENSPPAP00000028240.1, 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:ENSPPAP00000028240.1}
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   EMBL; AJFE02031390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02031391; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJFE02031392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003810142.1; XM_003810094.3.
DR   AlphaFoldDB; A0A2R9BF19; -.
DR   STRING; 9597.ENSPPAP00000028240; -.
DR   Ensembl; ENSPPAT00000051086.1; ENSPPAP00000028240.1; ENSPPAG00000037176.1.
DR   GeneID; 100983146; -.
DR   KEGG; pps:100983146; -.
DR   CTD; 9744; -.
DR   GeneTree; ENSGT00940000160289; -.
DR   OMA; CADHGDI; -.
DR   OrthoDB; 1449795at2759; -.
DR   Proteomes; UP000240080; Chromosome 17.
DR   Bgee; ENSPPAG00000037176; 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; cd08852; ArfGap_ACAP1; 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:SF197; ARF-GAP WITH COILED-COIL, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 1; 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.
DR   PROSITE; PS50007; PIPLC_X_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};
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          265..360
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          405..527
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50115"
FT   REPEAT          606..638
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          639..671
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          525..581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        536..550
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   740 AA;  81463 MW;  4EA57AD7294B16F7 CRC64;
     MTVKLDFEEC LKDSPRFRAS IELVEAEVSE LETRLEKLLK LGTGLLESGR HYLAASRAFV
     VGICDLARLG PPEPMMAECL EKFTVSLNHK LDSHAELLDA TQHTLQQQIQ TLVKEGLRGF
     REARRDFWRG AESLEAALTH NAEVPRRRAQ EAEEAGAALR TARAGYRGRA LDYALQINVI
     EDKRKFDIME FVLRLVEAQA THFQQGHEEL SRLSQYRKEL GAQLHQLVLN SAREKRDMEQ
     RHVLLKQKEL GGEEPEPSLR EGPGGLVMEG HLFKRASNAF KTWSRRWFTI QSNQLVYQKK
     YKDPVTVVVD DLRLCTVKLC PDSERRFCFE VVSTSKSCLL QADSERLLQL WVSAVQSSIA
     SAFSQARLDD SPRGPGQGSG HLAIGSAATL GSGGMARGRE PGGVGHVVAQ VQSVDGNAQC
     CDCREPAPEW ASINLGVTLC IQCSGIHRSL GVHFSKVRSL TLDSWEPELV KLMCELGNVV
     INQIYEARVE AMAVKKPGPS CSRQEKEAWI HAKYVEKKFL TKLPEIRGRR GGRGPPRGQP
     PVPPKPSIRP RPGSLRSKPE PPSEDLGSLH PGALLFRASG HPPSLPTMAD ALAHGADVNW
     VNGGQDNATP LIQATAANSL LACEFLLQNG ANVNQADSAG RGPLHHATIL GHTGLACLFL
     KRGADLGARD SEGRDPLTIA METANADIVT LLRLAKMREA EAAQGQAGDE TYLDIFRDFS
     LMASDDPEKL SRRSHDLHTL
//
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