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Database: UniProt
Entry: H0XKG1_OTOGA
LinkDB: H0XKG1_OTOGA
Original site: H0XKG1_OTOGA 
ID   H0XKG1_OTOGA            Unreviewed;      1533 AA.
AC   H0XKG1;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=ArfGAP with RhoGAP domain, ankyrin repeat and PH domain 3 {ECO:0000313|Ensembl:ENSOGAP00000016601.1};
GN   Name=ARAP3 {ECO:0000313|Ensembl:ENSOGAP00000016601.1};
OS   Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC   Galagidae; Otolemur.
OX   NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000016601.1, ECO:0000313|Proteomes:UP000005225};
RN   [1] {ECO:0000313|Proteomes:UP000005225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA   Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA   Walker B.J., Sharpe T., Hall G.;
RT   "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSOGAP00000016601.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AAQR03009001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAQR03009002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 30611.ENSOGAP00000016601; -.
DR   Ensembl; ENSOGAT00000029476.1; ENSOGAP00000016601.1; ENSOGAG00000030775.1.
DR   eggNOG; KOG1117; Eukaryota.
DR   GeneTree; ENSGT00940000158869; -.
DR   HOGENOM; CLU_002900_1_0_1; -.
DR   InParanoid; H0XKG1; -.
DR   OMA; CETVFQS; -.
DR   TreeFam; TF105769; -.
DR   Proteomes; UP000005225; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IEA:Ensembl.
DR   GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd17902; ArfGap_ARAP3; 1.
DR   CDD; cd13253; PH1_ARAP; 1.
DR   CDD; cd04385; RhoGAP_ARAP; 1.
DR   CDD; cd09490; SAM_Arap1_2_3; 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); 3.
DR   Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
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   InterPro; IPR000159; RA_dom.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR037858; RhoGAP_ARAP.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR45899:SF4; ARF-GAP WITH RHO-GAP DOMAIN, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 3; 1.
DR   PANTHER; PTHR45899; RHO GTPASE ACTIVATING PROTEIN AT 15B, ISOFORM C; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   Pfam; PF00169; PH; 2.
DR   Pfam; PF00788; RA; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00105; ArfGap; 1.
DR   SMART; SM00233; PH; 5.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR   SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR   SUPFAM; SSF50729; PH domain-like; 5.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 3.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   4: Predicted;
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00288};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005225};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00288};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00288}.
FT   DOMAIN          8..63
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   DOMAIN          275..367
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          382..471
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          468..599
FT                   /note="Arf-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50115"
FT   DOMAIN          895..1076
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50238"
FT   DOMAIN          1105..1198
FT                   /note="Ras-associating"
FT                   /evidence="ECO:0000259|PROSITE:PS50200"
FT   DOMAIN          1211..1313
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          72..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1402..1533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..231
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1404..1445
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1490..1533
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1533 AA;  168742 MW;  0BCAFD062F152DA3 CRC64;
     MAAPQDLDIA VWLATVHLEQ YADTFRRHGL ATAGAARALG HEELRQLGIS ATGHRKRILR
     LLQIGTVEGS LDLKSNSTME PSPSPAPPAH LSKPVPKPRT VFGLNSPATT QRPGLSLESR
     PRSPPFPTSS SKQTSTLNTM EMMPNAIYFG LDLRGGAQAA QDMAPDSSQT AAPIPALRPT
     TGTVHIMDPG CLYYGVQPVG IPGTPDRREG RGVGQDRIEH SLSRQDPEAR EDVGYASLEL
     PGDSTLSLPT LDTEETGDDL ISPYASFSST ADRPTPLLSG WLDKLSPQGN YVFQRRFVQF
     NGRSLMYFGS DKDPFPKGVI PLTAIEMTRG SKDNKFQVIT SQRVFMFRTE SEAQRDMWCS
     TLQSCLKEQR LLGHPRPPQP PRPLRTGVLE LRGHKAKVFA ALSPGELALY KSEQAFTLGI
     GICFIELQGC SVRETKSRSF DLLTPHRCFS FTAESGGARQ SWAAALQEAV TETLSDYEVA
     EKIWSNRANR HCADCGASRP DWAAVNLGVV ICKQCAGQHR ALGSGISKVQ SLKLDTSVWS
     NEIVQLFIVL GNDRANRFWA GTLPPGEGLY PDSNPGPRGE FISRKYKLGL FRKPHPQYPD
     HSQLLQALCA AVAGPNLLKN MAQLLCVEAS EDEEPWSPAA PDGSFPGHLP ADPSPGVYNE
     VVVPATYSGF LYCGPISNKA GPPPPRRGRD VPPRLWCVLG AALEMFASES SPEPVSLIQP
     QDVVCLGVSP PPTDPGDLFP FSFELILTGG KIQHFSTDGA DSLEAWTSAM GKWFSPLSCH
     QLLGPGLLRL GRLWLRSPSH TALAPGLWLS AFGLLRGDHL FLCPAPGPGP PAPEDMVHLR
     RLQEISVVPA ADTPDKKEHL VLVETGRTLY LQGEGRLDFS AWNTAIGGAA GGGGTGLQEQ
     QMSRGDIPII VDACISFVTQ HGLRLEGVYR KGGARARSLK LLAEFRRDAR SVKLRPGEHF
     VEDVTDTLKR FFRELDDPVT SARLLPRWRE AAELPQKDQR LEKYKEVIGS LPRVNRRTLA
     TLIGHLYRVQ KCAALNQMCT RNLALLFAPS VFQTDGRGEH EVRVLQELID GYVSVFDIDS
     DQVAQIDLEV NLITTWKDVQ LSQAGDLIME VYIEQQLPDN CVTLKVSPTL TAEELTNQVL
     EIRGTAAGTD LWVTFEIREH GELERPLHPK EKVLEQALQW CQLPEPCSAS LLLKKVSLAQ
     ASCLFTGIRR ESPRVGLLRC REEPPRLLGS RFQERFFLLR GRCLLLLKEK KSSKPEREWP
     LEGAKVYLGI RKKLKPPTLW GFTLILEKMQ LYLSCTDEDE MWDWTTSILK AQHDDQQPLV
     LRRRSSSDLA RQKFGTMPLL PIHGDDSGAT LLSANQTLRR LHNRRTLSMF FPMKSSQGSV
     EEQEELEEPV YEEPVYEEVG AFPELTQDTS TSSAIQERTD KTEIPLTSQK SFDQPLLSKA
     STLNQEERPP EPPPGPPSKS NPQAQGSLEE QLLQELSSLI LRKGETIGGP GSPSQPSSPQ
     TPSSSSTGLP TRTPSFPTQS SCTSSPPSSQ PLT
//
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