RGA1_YEAST
ID RGA1_YEAST Reviewed; 1007 AA.
AC P39083; D6W2I5; P39934;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Rho-type GTPase-activating protein 1;
GN Name=RGA1; Synonyms=DBM1, THE1; OrderedLocusNames=YOR127W;
GN ORFNames=O3290, YOR3290W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8657111; DOI=10.1128/mcb.16.4.1376;
RA Chen G.-C., Zheng L., Chan C.S.M.;
RT "The LIM domain-containing Dbm1 GTPase-activating protein is required for
RT normal cellular morphogenesis in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 16:1376-1390(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7498791; DOI=10.1101/gad.9.23.2949;
RA Stevenson B.J., Ferguson B., de Virgilio C., Bi E., Pringle J.R.,
RA Ammerer G., Sprague G.F. Jr.;
RT "Mutation of RGA1, which encodes a putative GTPase-activating protein for
RT the polarity-establishment protein Cdc42p, activates the pheromone-response
RT pathway in the yeast Saccharomyces cerevisiae.";
RL Genes Dev. 9:2949-2963(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8904341;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<281::aid-yea904>3.0.co;2-o;
RA Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C.,
RA Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.;
RT "Sequencing and analysis of 51 kb on the right arm of chromosome XV from
RT Saccharomyces cerevisiae reveals 30 open reading frames.";
RL Yeast 12:281-288(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 570-639.
RC STRAIN=S288c / SNY243;
RX PubMed=1454852; DOI=10.1073/pnas.89.23.11589;
RA Ramer S.W., Elledge S.J., Davis R.W.;
RT "Dominant genetics using a yeast genomic library under the control of a
RT strong inducible promoter.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:11589-11593(1992).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-278, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-278, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-278; SER-291 AND THR-532, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: GTPase-activating protein (GAP) for CDC42 and/or RHO1.
CC Negative regulator of the pheromone-response pathway through the STE20
CC protein kinase; acts at a step between the G-protein and the MAP kinase
CC module. Dominant suppressor of bud emergence defect caused by deletion
CC of IPL2/BEM2. Involved in the control of polarized cell growth and
CC proper bud site selection.
CC -!- INTERACTION:
CC P39083; Q12518: ENT1; NbExp=3; IntAct=EBI-15044, EBI-31494;
CC P39083; Q05785: ENT2; NbExp=2; IntAct=EBI-15044, EBI-35928;
CC P39083; P40073: SHO1; NbExp=2; IntAct=EBI-15044, EBI-18140;
CC P39083; O88339: Epn1; Xeno; NbExp=2; IntAct=EBI-15044, EBI-7066728;
CC -!- MISCELLANEOUS: Present with 396 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U07421; AAA16875.1; -; mRNA.
DR EMBL; X90950; CAA62445.1; -; Genomic_DNA.
DR EMBL; X90518; CAA62108.1; -; Genomic_DNA.
DR EMBL; X94335; CAA64046.1; -; Genomic_DNA.
DR EMBL; Z75035; CAA99326.1; -; Genomic_DNA.
DR EMBL; L02617; AAA35153.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10901.1; -; Genomic_DNA.
DR PIR; S48535; S48535.
DR RefSeq; NP_014770.1; NM_001183546.1.
DR AlphaFoldDB; P39083; -.
DR SMR; P39083; -.
DR BioGRID; 34522; 142.
DR DIP; DIP-1559N; -.
DR IntAct; P39083; 14.
DR MINT; P39083; -.
DR STRING; 4932.YOR127W; -.
DR iPTMnet; P39083; -.
DR MaxQB; P39083; -.
DR PaxDb; P39083; -.
DR PRIDE; P39083; -.
DR EnsemblFungi; YOR127W_mRNA; YOR127W; YOR127W.
DR GeneID; 854294; -.
DR KEGG; sce:YOR127W; -.
DR SGD; S000005653; RGA1.
DR VEuPathDB; FungiDB:YOR127W; -.
DR eggNOG; KOG1453; Eukaryota.
DR eggNOG; KOG1704; Eukaryota.
DR GeneTree; ENSGT01030000234635; -.
DR HOGENOM; CLU_003874_1_0_1; -.
DR InParanoid; P39083; -.
DR OMA; TGHAYEL; -.
DR BioCyc; YEAST:G3O-33652-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-8980692; RHOA GTPase cycle.
DR Reactome; R-SCE-9013148; CDC42 GTPase cycle.
DR Reactome; R-SCE-9013405; RHOD GTPase cycle.
DR Reactome; R-SCE-9013423; RAC3 GTPase cycle.
DR Reactome; R-SCE-9013424; RHOV GTPase cycle.
DR Reactome; R-SCE-9035034; RHOF GTPase cycle.
DR PRO; PR:P39083; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P39083; protein.
DR GO; GO:0071597; C:cellular birth scar; IDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0032177; C:cellular bud neck split septin rings; IDA:SGD.
DR GO; GO:0005621; C:cellular bud scar; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005096; F:GTPase activator activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007015; P:actin filament organization; IMP:SGD.
DR GO; GO:0007120; P:axial cellular bud site selection; IMP:SGD.
DR GO; GO:0007118; P:budding cell apical bud growth; IPI:SGD.
DR GO; GO:0007119; P:budding cell isotropic bud growth; IPI:SGD.
DR GO; GO:0030010; P:establishment of cell polarity; IMP:SGD.
DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IPI:SGD.
DR GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IGI:SGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:SGD.
DR GO; GO:2000222; P:positive regulation of pseudohyphal growth; IPI:SGD.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0031106; P:septin ring organization; IGI:SGD.
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; 1.
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; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 2.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW GTPase activation; LIM domain; Metal-binding; Pheromone response;
KW Phosphoprotein; Reference proteome; Repeat; Zinc.
FT CHAIN 1..1007
FT /note="Rho-type GTPase-activating protein 1"
FT /id="PRO_0000075899"
FT DOMAIN 13..66
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 70..122
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 791..1006
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 203..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 278
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 532
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT VARIANT 866
FT /note="V -> A"
FT VARIANT 898
FT /note="K -> R"
FT VARIANT 926
FT /note="S -> G"
FT MUTAGEN 37
FT /note="C->S: Bipolar budding."
FT /evidence="ECO:0000269|PubMed:8657111"
FT MUTAGEN 40
FT /note="C->S: Bipolar budding."
FT /evidence="ECO:0000269|PubMed:8657111"
FT MUTAGEN 98
FT /note="C->S: Bipolar budding."
FT /evidence="ECO:0000269|PubMed:8657111"
FT MUTAGEN 101
FT /note="C->S: Bipolar budding."
FT /evidence="ECO:0000269|PubMed:8657111"
FT CONFLICT 457
FT /note="D -> E (in Ref. 2; CAA62445)"
FT /evidence="ECO:0000305"
FT CONFLICT 507
FT /note="T -> P (in Ref. 2; CAA62445)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1007 AA; 112832 MW; C805411B57553791 CRC64;
MASTAPNEQF PSCVRCKEFI TTGHAYELGC DRWHTHCFAC YKCEKPLSCE SDFLVLGTGA
LICFDCSDSC KNCGKKIDDL AIILSSSNEA YCSDCFKCCK CGENIADLRY AKTKRGLFCL
SCHEKLLAKR KYYEEKKRRL KKNLPSLPTP VIDNGHTDEV SASAVLPEKT FSRPASLVNE
IPSGSEPSKD IETNSSDIVP HFITGYNDSD DNSGSSKFGS NVSIDVIGPE ENSTEHVNDD
VKEEAEAPSA NMSLNVATDP TLSCKEPPSH SRNLLNKTPL RNSSGQYLAK SPSSYRQGII
VNDSLEESDQ IDPPNNSSRN ASELLTSVLH SPVSVNMKNP KGSNTDIFNT GEISQMDPSL
SRKVLNNIVE ETNALQRPVV EVVKEDRSVP DLAGVQQEQA EKYSYSNNSG KGRKISRSLS
RRSKDLMINL KSRATGKQDS NVKLSPASKV TSRRSQDLMR DNDSHTGLDT PNSNSTSLDI
LVNNQKSLNY KRFTDNGTLR VTSGKETALE EQKNHSFKSP SPIDHLLQSP ATPSNVSMYR
TPPLDSSLTF DRRNGSSYSN QNYSIPSWQK TPKTQLENSD NFEEQKETLY ENSESRNDPS
LDKEIVTAEH YLKQLKINLK ELESQREELM KEITEMKSMK EALRRHIESY NSEKNKLYLD
SNELSNNPPM INEISLGESP PVKHVATASS VARSSVKPKF WKFFSSAKPQ TEQSIQGVST
NNTNSIVKSA PVLLSAPSSG SNSGRLEISP PVLQNPNEFS DVRLVPIEND ANMGQSKDGE
EYLDGSNLYG SSLVARCNYE NNEIPMILSV CIDFIESDEE NMRSEGIYRK SGSQLVIEEI
EKQFSAWKVQ QNTETPNILT EQDLNVVTGV LKRYLRKLPN PIFTFQIYEP LMRLVKSKKM
MENLPFVGGK LSLEAKNSDT YMSSKSALKN ILEDLPREHY RVLRVLSEHI EKVTRYSHWN
RMTLYNLALV FAPGLIRDFS GEKDIIDMKE RNYIVAFIFG NYKDILT
