RGP1_YEAST
ID RGP1_YEAST Reviewed; 663 AA.
AC P16664; D6VSC0; Q03915;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Guanine nucleotide exchange factor subunit RGP1 {ECO:0000305};
DE AltName: Full=Reduced growth phenotype protein 1 {ECO:0000312|SGD:S000002544};
DE Short=Rgp1p {ECO:0000303|PubMed:10990452};
GN Name=RGP1 {ECO:0000303|PubMed:2179863, ECO:0000312|SGD:S000002544};
GN OrderedLocusNames=YDR137W; ORFNames=YD9302.13;
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].
RX PubMed=2179863; DOI=10.1093/nar/18.4.1064;
RA Aguilera A., Moskowitz P., Klein H.L.;
RT "Molecular analysis of RGP1, a new yeast gene required for proper mitotic
RT growth.";
RL Nucleic Acids Res. 18:1064-1064(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RGP1.
RX PubMed=10990452; DOI=10.1093/emboj/19.18.4885;
RA Siniossoglou S., Peak-Chew S.Y., Pelham H.R.B.;
RT "Ric1p and Rgp1p form a complex that catalyses nucleotide exchange on
RT Ypt6p.";
RL EMBO J. 19:4885-4894(2000).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11689439; DOI=10.1093/emboj/20.21.5991;
RA Siniossoglou S., Pelham H.R.B.;
RT "An effector of Ypt6p binds the SNARE Tlg1p and mediates selective fusion
RT of vesicles with late Golgi membranes.";
RL EMBO J. 20:5991-5998(2001).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363 AND SER-364, AND
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351; SER-354; SER-357;
RP SER-363; SER-364 AND SER-370, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: The RIC1-RGP1 complex acts as a guanine nucleotide exchange
CC factor (GEF), which activates YPT6 by exchanging bound GDP for free
CC GTP. It is thereby required for efficient fusion of endosome-derived
CC vesicles with the Golgi. The RIC1-RGP1 participates in the recycling of
CC SNC1, presumably by mediating fusion of endosomal vesicles with the
CC Golgi compartment. {ECO:0000269|PubMed:10990452,
CC ECO:0000269|PubMed:11689439}.
CC -!- FUNCTION: Required for proper mitotic growth.
CC -!- SUBUNIT: Forms a complex with RIC1. {ECO:0000269|PubMed:10990452}.
CC -!- INTERACTION:
CC P16664; P40395: RIC1; NbExp=4; IntAct=EBI-15080, EBI-15183;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:10990452,
CC ECO:0000269|PubMed:11689439}.
CC -!- MISCELLANEOUS: Present with 589 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the RGP1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X52081; CAA36300.1; -; Genomic_DNA.
DR EMBL; Z48179; CAA88219.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11980.1; -; Genomic_DNA.
DR PIR; S51865; S51865.
DR RefSeq; NP_010421.1; NM_001180444.1.
DR AlphaFoldDB; P16664; -.
DR BioGRID; 32191; 523.
DR ComplexPortal; CPX-3078; Ric1-Rgp1 guanyl-nucleotide exchange factor complex.
DR DIP; DIP-6486N; -.
DR IntAct; P16664; 3.
DR MINT; P16664; -.
DR STRING; 4932.YDR137W; -.
DR iPTMnet; P16664; -.
DR MaxQB; P16664; -.
DR PaxDb; P16664; -.
DR PRIDE; P16664; -.
DR EnsemblFungi; YDR137W_mRNA; YDR137W; YDR137W.
DR GeneID; 851714; -.
DR KEGG; sce:YDR137W; -.
DR SGD; S000002544; RGP1.
DR VEuPathDB; FungiDB:YDR137W; -.
DR eggNOG; KOG4469; Eukaryota.
DR GeneTree; ENSGT00390000006136; -.
DR HOGENOM; CLU_030995_0_0_1; -.
DR InParanoid; P16664; -.
DR OMA; QFYEDKK; -.
DR BioCyc; YEAST:G3O-29734-MON; -.
DR Reactome; R-SCE-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-SCE-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR PRO; PR:P16664; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P16664; protein.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IPI:SGD.
DR GO; GO:0032045; C:guanyl-nucleotide exchange factor complex; IDA:SGD.
DR GO; GO:0034066; C:Ric1-Rgp1 guanyl-nucleotide exchange factor complex; IPI:SGD.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0043087; P:regulation of GTPase activity; IDA:ComplexPortal.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:SGD.
DR InterPro; IPR014848; Rgp1.
DR PANTHER; PTHR12507; PTHR12507; 1.
DR Pfam; PF08737; Rgp1; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Golgi apparatus;
KW Guanine-nucleotide releasing factor; Mitosis; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..663
FT /note="Guanine nucleotide exchange factor subunit RGP1"
FT /id="PRO_0000097319"
FT REGION 412..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 52..56
FT /note="EKLLT -> KAS (in Ref. 1; CAA36300)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 663 AA; 75317 MW; 4A3B311ED90ED14A CRC64;
MRAHRIDTFL IRENIKLEII HESNSYFGGE HISIAFRFKH LGSQHELFNY KEKLLTVDKA
VEEKLEQQAK VQDDGEGTME NQTWSLKSLL GAFKRTGEPE ESVDVDNMKM LNESKMLREK
IQKQMYFHQP VTLISGYVQI SGVFQYDSEV ISESKFKQDE VKMVGLDIVP GHTTNSVLAL
EDGEHFKGKR NLTNYLNSDY TNVTNGLLFS ESGSRGRTGT YNERTLMISN DTSIKTLPLL
LIPQTLLFSE ISLEPGEVRT FYFKSTKLPK DICPSYSSSK VASINYTLEV GADVLSDDNI
EKFSNRVPIT IAPYISSNAE QYTSRLDKPA IILKTGNIKE LKPRLFTRKV STASAVSFGR
RKSSIIDIDS PLEDNEFVKR VKKNFIELVE SNQNVSRDID ELIDLQMGVQ FGKDEDSSDP
EPNDSHFSNE MVTSAESSLR SDAVTKRRKS YSVRDNISNL EQKMWNDCSL VKSDENSNLL
PQLINLQNAY QINRNNETMA KVSLSAPFYK TTDDINLVIE LDPITTPLLK VTSLTVSLES
FEIINPKYKT EGKGIGSKPK GNSVYEKHFI CFDECKSVSV KLLPPRSPTN QITGQFKTDV
FQHKWMIGLK FVIIAKTESI TLDQFYEDKK GILFHSKENL EGEEFTCYVP IPILCTSEDF
MGW