RGD1_YEAST
ID RGD1_YEAST Reviewed; 666 AA.
AC P38339; D6VQQ7;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=RHO GTPase-activating protein RGD1;
DE Short=RhoGAP;
DE AltName: Full=Related GAP domain protein 1;
GN Name=RGD1; OrderedLocusNames=YBR260C; ORFNames=YBR1728;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8465606; DOI=10.1002/yea.320090210;
RA Doignon F., Biteau N., Crouzet M., Aigle M.;
RT "The complete sequence of a 19,482 bp segment located on the right arm of
RT chromosome II from Saccharomyces cerevisiae.";
RL Yeast 9:189-199(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
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 [4]
RP IDENTIFICATION.
RX PubMed=9769859; DOI=10.1016/s0764-4469(98)80776-2;
RA Barthe C., de Bettignies G., Louvet O., Peypouquet M.-F., Morel C.,
RA Doignon F., Crouzet M.;
RT "First characterization of the gene RGD1 in the yeast Saccharomyces
RT cerevisiae.";
RL C. R. Acad. Sci. III, Sci. Vie 321:453-462(1998).
RN [5]
RP FUNCTION.
RX PubMed=10526184; DOI=10.1016/s0014-5793(99)01293-4;
RA Doignon F., Weinachter C., Roumanie O., Crouzet M.;
RT "The yeast Rgd1p is a GTPase activating protein of the Rho3 and rho4
RT proteins.";
RL FEBS Lett. 459:458-462(1999).
RN [6]
RP FUNCTION.
RX PubMed=10590461;
RX DOI=10.1002/(sici)1097-0061(199912)15:16<1719::aid-yea499>3.0.co;2-f;
RA de Bettignies G., Barthe C., Morel C., Peypouquet M.-F., Doignon F.,
RA Crouzet M.;
RT "RGD1 genetically interacts with MID2 and SLG1, encoding two putative
RT sensors for cell integrity signalling in Saccharomyces cerevisiae.";
RL Yeast 15:1719-1731(1999).
RN [7]
RP FUNCTION.
RX PubMed=11779787; DOI=10.1093/genetics/159.4.1435;
RA de Bettignies G., Thoraval D., Morel C., Peypouquet M.-F., Crouzet M.;
RT "Overactivation of the protein kinase C-signaling pathway suppresses the
RT defects of cells lacking the Rho3/Rho4-GAP Rgd1p in Saccharomyces
RT cerevisiae.";
RL Genetics 159:1435-1448(2001).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
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 [10]
RP FUNCTION.
RX PubMed=16087742; DOI=10.1128/ec.4.8.1375-1386.2005;
RA Claret S., Gatti X., Doignon F., Thoraval D., Crouzet M.;
RT "The Rgd1p Rho GTPase-activating protein and the Mid2p cell wall sensor are
RT required at low pH for protein kinase C pathway activation and cell
RT survival in Saccharomyces cerevisiae.";
RL Eukaryot. Cell 4:1375-1386(2005).
RN [11]
RP FUNCTION.
RX PubMed=15922872; DOI=10.1016/j.gene.2005.03.034;
RA Gatti X., de Bettignies G., Claret S., Doignon F., Crouzet M., Thoraval D.;
RT "RGD1, encoding a RhoGAP involved in low-pH survival, is an Msn2p/Msn4p
RT regulated gene in Saccharomyces cerevisiae.";
RL Gene 351:159-169(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-386, AND IDENTIFICATION BY
RP 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).
RN [13]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RC STRAIN=ATCC 201389 / BY4742;
RX PubMed=23454383; DOI=10.1016/j.bbrc.2013.02.081;
RA Vieillemard A., Prouzet-Mauleon V., Hugues M., Lefebvre F., Mitteau R.,
RA Claverol S., Bonneu M., Crouzet M., Doignon F., Thoraval D.;
RT "The Saccharomyces cerevisiae RhoGAP Rgd1 is phosphorylated by the Aurora B
RT like kinase Ipl1.";
RL Biochem. Biophys. Res. Commun. 433:1-5(2013).
CC -!- FUNCTION: GTPase activating protein of RHO3 and RHO4. Acts in concert
CC with MID2 in cell integrity, which is functionally linked to the PKC
CC pathway. Involved in various stress responses. Required at low pH for
CC activation of the PKC pathway. Important during mating response.
CC {ECO:0000269|PubMed:10526184, ECO:0000269|PubMed:10590461,
CC ECO:0000269|PubMed:11779787, ECO:0000269|PubMed:15922872,
CC ECO:0000269|PubMed:16087742}.
CC -!- INTERACTION:
CC P38339; P38339: RGD1; NbExp=2; IntAct=EBI-15065, EBI-15065;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:23454383}. Note=Bud and bud neck. During isotropic
CC bud growth in the G1 and S phases, detected at the bud tip. During
CC cytokinesis, undetectable at the bud tip and localized at the bud neck
CC only.
CC -!- INDUCTION: Induced by stress including low pH, heat shock and oxidative
CC shock. Basal and acid-stressed expression level is regulated by
CC transcription factors MSN2 and MSN4 as well as the HOG pathway.
CC -!- PTM: Phosphorylated in vivo. In vitro, phosphorylated by IPL1.
CC {ECO:0000269|PubMed:23454383}.
CC -!- MISCELLANEOUS: Present with 1500 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: Lack of RGD1 diminishes the PKC pathway activity.
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DR EMBL; X70529; CAA49924.1; -; Genomic_DNA.
DR EMBL; Z36129; CAA85223.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07377.1; -; Genomic_DNA.
DR PIR; S29349; S29349.
DR RefSeq; NP_009819.1; NM_001178608.1.
DR PDB; 4WPC; X-ray; 3.34 A; A/B=24-333.
DR PDB; 5MY3; X-ray; 2.19 A; A=450-666.
DR PDBsum; 4WPC; -.
DR PDBsum; 5MY3; -.
DR AlphaFoldDB; P38339; -.
DR SMR; P38339; -.
DR BioGRID; 32956; 256.
DR DIP; DIP-4950N; -.
DR IntAct; P38339; 27.
DR MINT; P38339; -.
DR STRING; 4932.YBR260C; -.
DR iPTMnet; P38339; -.
DR MaxQB; P38339; -.
DR PaxDb; P38339; -.
DR PRIDE; P38339; -.
DR EnsemblFungi; YBR260C_mRNA; YBR260C; YBR260C.
DR GeneID; 852563; -.
DR KEGG; sce:YBR260C; -.
DR SGD; S000000464; RGD1.
DR VEuPathDB; FungiDB:YBR260C; -.
DR eggNOG; KOG1450; Eukaryota.
DR GeneTree; ENSGT01030000234635; -.
DR HOGENOM; CLU_010730_2_0_1; -.
DR InParanoid; P38339; -.
DR OMA; IADSGWQ; -.
DR BioCyc; YEAST:G3O-29184-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:P38339; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38339; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:0005933; C:cellular bud; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0005628; C:prospore membrane; HDA:SGD.
DR GO; GO:0005096; F:GTPase activator activity; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:SGD.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:SGD.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:SGD.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:SGD.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IDA:SGD.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0010447; P:response to acidic pH; IMP:SGD.
DR GO; GO:0006970; P:response to osmotic stress; IGI:SGD.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; GTPase activation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..666
FT /note="RHO GTPase-activating protein RGD1"
FT /id="PRO_0000056736"
FT DOMAIN 33..295
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 472..663
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 139..226
FT /evidence="ECO:0000255"
FT COMPBIAS 349..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 386
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:4WPC"
FT HELIX 43..83
FT /evidence="ECO:0007829|PDB:4WPC"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:4WPC"
FT HELIX 97..179
FT /evidence="ECO:0007829|PDB:4WPC"
FT HELIX 195..231
FT /evidence="ECO:0007829|PDB:4WPC"
FT HELIX 233..274
FT /evidence="ECO:0007829|PDB:4WPC"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:4WPC"
FT HELIX 283..288
FT /evidence="ECO:0007829|PDB:4WPC"
FT HELIX 292..304
FT /evidence="ECO:0007829|PDB:4WPC"
FT HELIX 474..477
FT /evidence="ECO:0007829|PDB:5MY3"
FT HELIX 487..499
FT /evidence="ECO:0007829|PDB:5MY3"
FT TURN 500..502
FT /evidence="ECO:0007829|PDB:5MY3"
FT TURN 504..508
FT /evidence="ECO:0007829|PDB:5MY3"
FT HELIX 513..525
FT /evidence="ECO:0007829|PDB:5MY3"
FT HELIX 527..533
FT /evidence="ECO:0007829|PDB:5MY3"
FT HELIX 541..557
FT /evidence="ECO:0007829|PDB:5MY3"
FT STRAND 558..560
FT /evidence="ECO:0007829|PDB:5MY3"
FT HELIX 565..567
FT /evidence="ECO:0007829|PDB:5MY3"
FT HELIX 568..576
FT /evidence="ECO:0007829|PDB:5MY3"
FT HELIX 580..592
FT /evidence="ECO:0007829|PDB:5MY3"
FT HELIX 596..614
FT /evidence="ECO:0007829|PDB:5MY3"
FT HELIX 616..619
FT /evidence="ECO:0007829|PDB:5MY3"
FT HELIX 623..634
FT /evidence="ECO:0007829|PDB:5MY3"
FT HELIX 646..662
FT /evidence="ECO:0007829|PDB:5MY3"
SQ SEQUENCE 666 AA; 74619 MW; 711D9CC717E9111D CRC64;
MEETAKKPAS ATVSAKSSHD GGTDDLAHLF STPEIKKVLN SDVAINALLS RLKQSLLTCE
EFMKFIRKKY AFEEEHVQEL SKQYKHFFNI QGSTNSSLKK MIHEVLGFDG KMAQVKQSYI
TALQKMYSEI SSLLLTMTKL RKSVKENSKR LEKDVSDAIH SAEKAQSRYN SLCQDWDKLR
MTDPTKTKLT LRGSKTTKEQ EEELLRKIDN ADLEYKQKVD HSNSLRNTFI TKERPRIVQE
LKDLILEIDT AMTIQLQKYT IWTENLVLNT GVTISPLDST KSMKSFAGSV SNERDLYSFL
NKYNQTGKHS LLINKNLIPV SYKKHPSMNH GQKNKSPPKF AVDPSRNSIP KRMISTHNES
PFLSSSSNTA AVPNANLNSA TPSLNTNKQL PPTMASSISS TSNAAGAMSP SSSIVTSDTT
SSITKTLDPG NNSPQIPEEL INSLDSDRPI SHIQTNNNMP PGVQKNFKTF GVPLESLIEF
EQDMVPAIVR QCIYVIDKFG LDQEGIYRKS ANVLDVSKLK EEIDKDPANI SMILPSKPHS
DSDIYLVGSL LKTFFASLPD SVLPKALSSE IKVCLQIEDP TTRKNFMHGL IYNLPDAQYW
TLRALVFHLK RVLAHEAQNR MNLRALCIIW GPTIAPANPD DANDVNFQIM AMEVLLEVSD
QAFEPE
