ID A0A1D5Q2X4_MACMU Unreviewed; 1717 AA.
AC A0A1D5Q2X4;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=ArfGAP with RhoGAP domain, ankyrin repeat and PH domain 2 {ECO:0000313|Ensembl:ENSMMUP00000042386.2};
GN Name=ARAP2 {ECO:0000313|Ensembl:ENSMMUP00000042386.2,
GN ECO:0000313|VGNC:VGNC:69843};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000042386.2, ECO:0000313|Proteomes:UP000006718};
RN [1] {ECO:0000313|Proteomes:UP000006718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX PubMed=17431167; DOI=10.1126/science.1139247;
RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA Kuhn R.M., Smith K.E., Zwieg A.S.;
RT "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL Science 316:222-234(2007).
RN [2] {ECO:0000313|Ensembl:ENSMMUP00000042386.2}
RP IDENTIFICATION.
RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000042386.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR SMR; A0A1D5Q2X4; -.
DR STRING; 9544.ENSMMUP00000042386; -.
DR Ensembl; ENSMMUT00000062853.2; ENSMMUP00000042386.2; ENSMMUG00000006871.4.
DR VEuPathDB; HostDB:ENSMMUG00000006871; -.
DR VGNC; VGNC:69843; ARAP2.
DR eggNOG; KOG1117; Eukaryota.
DR GeneTree; ENSGT00940000160197; -.
DR InParanoid; A0A1D5Q2X4; -.
DR OMA; FAHSCET; -.
DR Proteomes; UP000006718; Chromosome 5.
DR Bgee; ENSMMUG00000006871; Expressed in dorsolateral prefrontal cortex and 20 other cell types or tissues.
DR ExpressionAtlas; A0A1D5Q2X4; baseline.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd08856; ArfGap_ARAP2; 1.
DR CDD; cd13253; PH1_ARAP; 1.
DR CDD; cd13254; PH2_ARAP; 1.
DR CDD; cd13256; PH3_ARAP; 1.
DR CDD; cd13257; PH4_ARAP; 1.
DR CDD; cd13259; PH5_ARAP; 1.
DR CDD; cd17227; RA_ARAP2; 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); 4.
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 PANTHER; PTHR45899:SF1; ARF-GAP WITH RHO-GAP DOMAIN, ANK REPEAT AND PH DOMAIN-CONTAINING PROTEIN 2; 1.
DR PANTHER; PTHR45899; RHO GTPASE ACTIVATING PROTEIN AT 15B, ISOFORM C; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00169; PH; 4.
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 PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50003; PH_DOMAIN; 4.
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:UP000006718};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00288};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00288}.
FT DOMAIN 10..70
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 481..587
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 600..692
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 689..824
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT DOMAIN 891..1016
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1129..1310
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT DOMAIN 1339..1433
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1447..1550
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 107..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1651..1687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1667..1687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1717 AA; 195197 MW; 2C63513299D71CC3 CRC64;
MSSVSEVNVD IKDFLMSINL EQYLLHFHES GFTTVKDCAV INDSLLQKIG ISPTGHRRRI
LKQLQIILSK MQDFPIYANV HKTKKNDDPS KDHNVPSSDQ NICIELSSSS SVQMPSPPQL
ETVTKKLEDD ASVERSQYPQ SDNKLSPPKR DFPTSEEPHL NLGSLNNSLF GSENIKIESL
ITKKTMGHTI EEQQTEKVKL ISENLNKLPN ADSECLSSVG CSTSETNSRN GTNGLLDGSP
PSPFFKFQGE MIVNDLYVPS SPILAPMRSR SKLVSRPSRS FLLRHRPVPE IPGSTKGISG
SYFRERRNVA TSTEKSVAWQ NSNEENSSSI FPYGETFLFQ RLENSKKRSI KNEFLTQEEA
LKGEATTATN SFIIKSSIYD NRKEKISEDK VEDIWIPRED KNNFLIDTAS ESEYSTVEEC
FQSLRRKNSK ASKSRTQKAL TLDSVNRHSY PLSSTSGNAD SSAVSSQAIS PYACFYGASV
KKVKSGWLDK LSPQGKRMFQ KRWVKFDGLS ISYYNNEKFA CTFECEDNSF PREMYSKGII
PLSAISTVRV QGDNKFEVVT TQRTFVFRVE KEEERNDWIS ILLNALKSQS LTSQSQGIVT
PEKCGYLELR GYKAKIFTVL SGNSVWLCKN EQDFKSGLGI TIIPMNVANV KQVDRTVKQS
FEIITPYRSF SFTAETEKEK QDWIEAVQQS IAETLSDYEV AEKIWFNESN RSCADCKAPD
PDWASINLCV VICKKCAGQH RSLGPKDSKV RSLKMDASIW SNELIELFIV IGNKRANDFW
AGNLQKDEEL HMDSPVEKRK NFITQKYKEG KFRKTLLASL TKEELNKALC AAVVKPDVLE
TMALLFSGAD VMCATGDPVH STPYLLAKKA GQSLQMEFLY HNKFSDFPQH DIHSEGVLSQ
ESSQCTFLCD FLYQAPAAAS KLSSEKKLLE ETNKKWCVLE GGFLSYYESD KSTTPNGTIN
INEVICLAIH KEDFYLNTGP IFIFEIYLPS ERVFLFGAET SQAQRKWTEA IAKHFVPLFA
ENLTEADYDL IGQLFYKDCH ALDQWRKGWF AMDKSSLHFC LQMQEVQGDR MHLRRLQELT
ISTMVQNGEK LDVLLLVEKG RTLYIHGHTK LDFTVWHTAI EKAAGTDGNA LQDQQLSKND
VPIIVNSCIA FVTQYGLGCK YIYQKNGDPL HISELLESFK KDARSFKLRA GKHQLEDVTG
VLKSFLSDID DALLTKELYP YWISALDAQD DKERIKKYGA FIRSLPGVNR ATLAAIIEHL
YRVQKCSEIN HMNAHNLALV FSSCLFQTEG QTSEEVNVIE DLINNYVEIF EVKEDQVKQM
DIENSFITKW KDTQVSQAGD LLIEVYVERK EPDCSIIIRI SPVMEAEELT NDILAIKNII
PTKGDIWATF EVIENEELER PLHYKENVLE QVLRWSSLAE PGSAYLVVKK FLTADTIKHC
SDRSTLGSIK EGILKIKEEP SKILSGNKFQ DRYFVLRDGF LFLYKDVKSS KHDKMFSVSS
VKFYRGVKKK MKPPTSWGLT AYSEKHHWHL CCDSSRAQME WMTSIFIAQH ENDIWPPAGK
ERKRSITKNP KIGGLPLIPI QHEGNATLAR KNIESARAEL ERLRLVEKCD RESVDSSLKE
RASMVAHCLE HKDDKLRNRT RKHRSFNCLE DTEPEAPLGQ PKGHKGLKTL RKTEDRNSKA
TLDSDHKLPS RVIEELNVVL QRSRTLPREL QDEQILK
//
