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Database: UniProt
Entry: A0A2K5ZRG3_MANLE
LinkDB: A0A2K5ZRG3_MANLE
Original site: A0A2K5ZRG3_MANLE 
ID   A0A2K5ZRG3_MANLE        Unreviewed;       705 AA.
AC   A0A2K5ZRG3;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=ACAP3 {ECO:0000313|Ensembl:ENSMLEP00000030405.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000030405.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000030405.1}
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; A0A2K5ZRG3; -.
DR   Ensembl; ENSMLET00000053969.1; ENSMLEP00000030405.1; ENSMLEG00000039298.1.
DR   GeneTree; ENSGT00940000156199; -.
DR   Proteomes; UP000233140; 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; cd07637; BAR_ACAP3; 1.
DR   CDD; cd13250; PH_ACAP; 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; IPR042695; ACAP3_BAR.
DR   InterPro; IPR027267; AH/BAR_dom_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: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; PF16746; BAR_3; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00105; ArfGap; 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; PS50115; ARFGAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, 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:UP000233140};
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          267..333
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          381..509
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50115"
FT   REGION          353..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..371
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   705 AA;  78619 MW;  B683BC08D7442E7E CRC64;
     SILCPEQCVG DSQPRSCFRA TIDEVETDVV EIEAKLDKLV KLCSGMVEAG KAYVSTSRLF
     VSGVRDLSQQ CQGDTVISEC LQRFADSLQE VVNYHMILFD QAQRSVRQQL HNFVKEDVRK
     FKETKKQFDK VREDLELSLV RNAQAPRHRP HEVEEATGAL TLTRKCFRHL ALDYVLQINV
     LQAKKKFEIL DSMLSFMHAQ SSFFQQGYSL LHQLDPYMKK LAAELDQLVI DSAVEKREME
     RKHAAIQQRD FSYDESKVEF DVDAPSGVVM EGYLFKRASN AFKTWNRRWF SIQNSQLVYQ
     KKLKDALTVV VDDLRLCSVK PCEDIERRFC FEVAGGVAAH RRAACCRPTP RSCGRLDRTA
     SPSTSSVDSA TDPRERGVKG ESVLQRVQSV AGNSQCGDCG QSDPRWASIN LGVLLCIECS
     GIHRSLGVHC SKVRSLTLDS WEPELLKLMC ELGNRAVNQI YEAQCEGPGS RKPTASSPRQ
     DKEAWIKDKY VEKKFLRKAP MVPALEAPRR WRAHKCPRPH SSPRVPTARR KVRLEPVLPC
     VAALSSVGTL DRKFRRDSLF CPDELDSLFS YFDAGAAGAG PRSKCGMGPA RWQGRAKEAG
     LEGAQVWMAL AGEWSSIWRG GGLLATELEA EALTVGVSCA NVCVGCVHPG VCVERMARGA
     RAAEGTASWP SAWDPSEAML PIRWVETFLP GPATDRDGGP LQGCR
//
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