ID RGA1_SCHPO Reviewed; 1150 AA.
AC O43052;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 27-MAR-2024, entry version 146.
DE RecName: Full=Rho-type GTPase-activating protein 1;
GN Name=rga1; ORFNames=SPBC3F6.05;
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 FUNCTION, AND SUBCELLULAR LOCATION.
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-690, 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 Rho1. Involved in the F-actin
CC patch localization, cell morphogenesis, regulation of septation, and
CC cell wall synthesis. {ECO:0000269|PubMed:11737264}.
CC -!- SUBCELLULAR LOCATION: Cell tip {ECO:0000269|PubMed:11737264}. Nucleus
CC {ECO:0000269|PubMed:11737264}. Note=Cell poles and cell division site.
CC {ECO:0000269|PubMed:11737264}.
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DR EMBL; CU329671; CAA17694.1; -; Genomic_DNA.
DR PIR; T40395; T40395.
DR RefSeq; NP_596743.1; NM_001023763.2.
DR AlphaFoldDB; O43052; -.
DR SMR; O43052; -.
DR BioGRID; 277537; 7.
DR STRING; 284812.O43052; -.
DR iPTMnet; O43052; -.
DR MaxQB; O43052; -.
DR PaxDb; 4896-SPBC3F6-05-1; -.
DR EnsemblFungi; SPBC3F6.05.1; SPBC3F6.05.1:pep; SPBC3F6.05.
DR GeneID; 2541022; -.
DR KEGG; spo:SPBC3F6.05; -.
DR PomBase; SPBC3F6.05; rga1.
DR VEuPathDB; FungiDB:SPBC3F6.05; -.
DR eggNOG; KOG1703; Eukaryota.
DR eggNOG; KOG2710; Eukaryota.
DR HOGENOM; CLU_001321_1_0_1; -.
DR InParanoid; O43052; -.
DR OMA; WQMQSSV; -.
DR PhylomeDB; O43052; -.
DR PRO; PR:O43052; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
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; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000935; C:division septum; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005096; F:GTPase activator activity; IGI:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:PomBase.
DR GO; GO:1903338; P:regulation of cell wall organization or biogenesis; IMP:PomBase.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd09391; LIM1_Lrg1p_like; 1.
DR CDD; cd09392; LIM2_Lrg1p_like; 1.
DR CDD; cd04397; RhoGAP_fLRG1; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 2.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR14963; RHO GTPASE ACTIVATING PROTEIN 18,19-RELATED; 1.
DR PANTHER; PTHR14963:SF1; RHO GTPASE-ACTIVATING PROTEIN CONUNDRUM; 1.
DR Pfam; PF00412; LIM; 2.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00132; LIM; 2.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 3.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW GTPase activation; LIM domain; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Zinc.
FT CHAIN 1..1150
FT /note="Rho-type GTPase-activating protein 1"
FT /id="PRO_0000075898"
FT DOMAIN 114..177
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 178..238
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 483..546
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 837..1038
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1104..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 690
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1150 AA; 130602 MW; 72F29A63A456EDAF CRC64;
MSQRDAKKDG LLYTTNGVSP TPPKRIPVPS RQNKIEENST TKNFPHSRHT STVAGTEGGS
SLSRRHTSAE SRKALPNQQQ LAQSGLLNKE EQQSLKRSDT SVFPKAVRKV SSSKICASCG
QVISGQYVRA LGNIYHLECF RCHDCNSLVA SKFFPIDDPT LNKQVPLCET DYFRRLDLLC
ASCGMALRGY YITALNKKFH IEHFTCSLCY TVFGPNDSYY EYEGKVYCHY HYSTLFAARC
CGCDGPILRQ FVEVYRNGVS QNWHVPCHMI YKFWNVKLCQ KTSIETSKKK DSELSQSQLR
KREKHLEQKI FHIWHALSYF EEYTASCISD MLLLVSNGEF TKSVICAQKF IRYIEILFKG
IDSLETILSS FHAKSMPYVR EAKLLCKKLV SIFALLAKCH NSDIRDVAIV QDFLSLFTGL
AHYLKLLIRI SLTGGLRLEQ DHACKHALPQ FLQTVEEARF VDQEGYDSSS FDMPLNLANA
SSDLCYVCHS ALEEDCVLLG EIRCHIGCLS CTKCKYNNRE NYDWARWNNQ TKQIECYLCY
TESSNVSNDE PHPSFEYVSR LSQYIYLLRI ALVRLYTILM ENNDSSQRKP LSVDPKQENV
SSTVETAKQA ETTASSDSFR KYANTLNDLR HLKSSRNRKA TSNETQSSSN STETSKLSKN
VSESGKDKSP HWHSHGGSIT GKSIVEQASS PLERRMDAFD ENRAFTLDDI PKVISEQRNR
EHRPNAFRHM PSYTDPSYRK NSGAIYDKND GTQKGLTPKS EDAPIRYLSD LSNLELLFTK
HVAVLILHPL VRDYYSLDEL MEMSDLRKGG FWEKFGKAFK GKDAEKKNVK KKGTFGVPLE
ILVERNNAQS TVGTGVGVKH IPAFIGNTLA AMKRKDMSVV GVFRKNGNIR RLKELSDMLD
VSPDSIDYEQ ETPIQLAALL KKFLRELPDP LLTFKLFGLF ITSSKLESEE ERMRVLHLTI
CLLPKGHRDT MEVIFGFLYW VASFSHIDDE VGSKMDIHNL ATVITPNILY SKSNDPVDES
FLAIEAVHLL IENFEKFCEV PREISLLLDD PTLFYNNAAW TSKELYKRCE EIISQMSLDE
RNTPKHTAST KRKRQPIRRV TTNLTSDVPS GSEVADTNSL SSTTKDEASP NSDAQPKPQV
KPQHAVIRDS
//
