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RGA1_SCHPO
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   25-MAY-2022, entry version 141.
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 septum {ECO:0000269|PubMed:11737264}.
CC       Note=Cell poles and septum.
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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; 4896.SPBC3F6.05.1; -.
DR   iPTMnet; O43052; -.
DR   MaxQB; O43052; -.
DR   PaxDb; O43052; -.
DR   PRIDE; O43052; -.
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:0008360; P:regulation of cell shape; 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   Gene3D; 1.10.555.10; -; 1.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR001781; Znf_LIM.
DR   Pfam; PF00412; LIM; 2.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00132; LIM; 2.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; SSF48350; 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; 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
 
 
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