RGA2_SCHPO
ID RGA2_SCHPO Reviewed; 1275 AA.
AC Q10164; Q9USA5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Probable Rho-type GTPase-activating protein 2;
GN Name=rga2; ORFNames=SPAC26A3.09c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 69-301, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP GENE NAME.
RX PubMed=11737264; DOI=10.1046/j.1365-2443.2001.00485.x;
RA Nakano K., Mutoh T., Mabuchi I.;
RT "Characterization of GTPase-activating proteins for the function of the
RT Rho-family small GTPases in the fission yeast Schizosaccharomyces pombe.";
RL Genes Cells 6:1031-1042(2001).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: GTPase-activating protein for Rho-type proteins.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889}.
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DR EMBL; CU329670; CAA93232.1; -; Genomic_DNA.
DR EMBL; AB027912; BAA87216.1; -; Genomic_DNA.
DR PIR; T38397; T38397.
DR RefSeq; NP_594152.1; NM_001019576.2.
DR AlphaFoldDB; Q10164; -.
DR SMR; Q10164; -.
DR BioGRID; 279135; 63.
DR STRING; 4896.SPAC26A3.09c.1; -.
DR iPTMnet; Q10164; -.
DR MaxQB; Q10164; -.
DR PaxDb; Q10164; -.
DR PRIDE; Q10164; -.
DR EnsemblFungi; SPAC26A3.09c.1; SPAC26A3.09c.1:pep; SPAC26A3.09c.
DR GeneID; 2542682; -.
DR KEGG; spo:SPAC26A3.09c; -.
DR PomBase; SPAC26A3.09c; rga2.
DR VEuPathDB; FungiDB:SPAC26A3.09c; -.
DR eggNOG; KOG4269; Eukaryota.
DR HOGENOM; CLU_283724_0_0_1; -.
DR InParanoid; Q10164; -.
DR PRO; PR:Q10164; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0051286; C:cell tip; HDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0035838; C:growing cell tip; IDA:PomBase.
DR GO; GO:0110085; C:mitotic actomyosin contractile ring; IDA:PomBase.
DR GO; GO:0120105; C:mitotic actomyosin contractile ring, intermediate layer; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IDA:PomBase.
DR GO; GO:0008289; F:lipid binding; ISM:PomBase.
DR GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IC:GOC-OWL.
DR GO; GO:0070610; P:regulation of fungal-type cell wall (1->3)-alpha-glucan biosynthetic process; IMP:PomBase.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW GTPase activation; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1275
FT /note="Probable Rho-type GTPase-activating protein 2"
FT /id="PRO_0000097312"
FT DOMAIN 719..836
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1065..1275
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 118..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 957..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1254..1275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..438
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1275 AA; 143588 MW; 136DA1A26B4A1BBE CRC64;
MVKMDVVRTT GFFLRSEPTT CRITTFAYSA EIIYFHAETT FLFEKIMKEG NELEKYSKIE
LNSEIWEDEE EEDNSGIVSQ NERLMKLVNK QREIIYELHK DLEKVKKDNT SLRMRLSKYE
STDSFPSSQP SRANSPQSDS YSSPYEKGKL FPKISLKSSK DVPTASAHIS SSDHEKSSSV
SLSALNNYNK TTDIKARSLD RLSDMTRPKL LLNTKRSHRS SEEPGASSPV TSPILKDSQK
ERIQALRNKA IKTYSVSTES AERIDSIRSD NLSPLSLNTS SFRRPITKPT PFNSDSNISI
DPKDNNSNKQ DHFAEIEDEL RQQFLDIKVG RANASSPRRK SISIVKPHGI SSPKHSTNNL
SSKSGKFHSD FRVVSENVLL QARSETNSPI IENKEANNFL APTSNVPAYS TPARPTESPP
PPPISSSSTT PRPDDKPSLP PRGLSEDNDS LSLQKTGSSD TRRSSFSTLK IPDSDICFTR
RRSDSNRTWT VIDPHHSQSF DNDILAEIPT SKLDNSSQKS PGKLSSKGLL NSFSPISPFS
KSKSHNHHPS SQVEKSTSNS KGSMLPLDTL YNNKLSFRLD ESLVRYLRFE LMKTSLASLS
PDFDCIGLQF VVGVSASSHL ASQWKDEVWS FTRSIGECRS FATSFVLDIG APPFPTLDWF
TNDSSVIQNE LLRRSVDTYF RYIFQTDLKL EQRIKLLEFL SSDTLREYLH DVFFLPPEHA
QKEGVLLKYI ENSGLVSRYF YLKDNILYFA ENRNSPVLGT IHLKDAQVNR YNANLPIFSI
IDPPHEFLTG ENYQSAFVIQ EKQTETRTGT ATVHVLLARD VEDQKSWLRA ILRQVPGSTS
PLNASPFSVL SSDFPGSSRY RDQSSPIRFY GKADSRPVSQ EAILSQDISS SPSPVLPPSE
NVASYADDSL VSNLTMSPKL RDSMEQVPLE NHREFEISDR VSELSFDSST GSVLEIADTR
RNQDAPEKHV PVIEIQSSRP SLEKTDQSTP VELLIDSHSQ NSQNEEKRSR MKFWAFPHHK
AENYEQISDT NIPVIETNVM LSPSSTTSAE PLQKHIVRKS GIFGLPLNEA VNISTQFNDS
GLPIVVYRCI EYLESCRAEK EEGIYRLSGS ASTIKHLKEQ FNEGVDYDLL SSDEEFDVHV
IAGLLKLYLR NLPTNLLDTS MHKLFELLPN VPNDSAALGE LCDVISKLPP ENFALLDSLL
HHLRRIIAFE KVNKMNIRNV CIVFSPTLNI PSDIFMMLIL NYDHIFTDIS RQTNGAQNES
DSDVSDDNGE DNEFF
