RAEP_YEAST
ID RAEP_YEAST Reviewed; 603 AA.
AC P32864; D6W363; Q06761;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Rab proteins geranylgeranyltransferase component A;
DE AltName: Full=Rab escort protein;
DE Short=REP;
GN Name=MRS6; Synonyms=MSI4; OrderedLocusNames=YOR370C;
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=8132658; DOI=10.1016/s0021-9258(17)37095-3;
RA Fujimura K., Tanaka K., Nakano A., Toh-e A.;
RT "The Saccharomyces cerevisiae MSI4 gene encodes the yeast counterpart of
RT component A of Rab geranylgeranyltransferase.";
RL J. Biol. Chem. 269:9205-9212(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7882424; DOI=10.1007/bf00310494;
RA Ragnini A., Teply R., Waldherr M., Voskova A., Schweyen R.J.;
RT "The yeast protein Mrs6p, a homologue of the rabGDI and human
RT choroideraemia proteins, affects cytoplasmic and mitochondrial functions.";
RL Curr. Genet. 26:308-314(1994).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 132-594.
RA Waldherr M., Voskova A., Schweyen R.J.;
RL Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP SIMILARITY TO CHOROIDEREMIA PROTEIN.
RX PubMed=8387377; DOI=10.1038/ng0393-193;
RA Waldherr M., Ragnini R.J., Schweyen R.J., Boguski M.S.;
RT "MRS6 -- yeast homologue of the choroideraemia gene.";
RL Nat. Genet. 3:193-194(1993).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470, 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 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: Substrate-binding subunit (component A) of the Rab
CC geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab
CC proteins and presents the substrate peptide to the catalytic component
CC B. The component A is thought to be regenerated by transferring its
CC prenylated Rab back to the donor membrane.
CC -!- INTERACTION:
CC P32864; P32432: SFP1; NbExp=5; IntAct=EBI-14799, EBI-17035;
CC P32864; P36017: VPS21; NbExp=3; IntAct=EBI-14799, EBI-29399;
CC P32864; P38146: YPT10; NbExp=3; IntAct=EBI-14799, EBI-29357;
CC P32864; P36018: YPT52; NbExp=3; IntAct=EBI-14799, EBI-29407;
CC -!- MISCELLANEOUS: Present with 23800 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the Rab GDI family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA49805.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D26441; BAA05460.1; -; Genomic_DNA.
DR EMBL; X70339; CAA49804.1; -; Genomic_DNA.
DR EMBL; X70339; CAA49805.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z75278; CAA99701.1; -; Genomic_DNA.
DR EMBL; M90844; AAA34796.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11129.1; -; Genomic_DNA.
DR PIR; S47917; S47917.
DR RefSeq; NP_015015.1; NM_001183790.1.
DR AlphaFoldDB; P32864; -.
DR SMR; P32864; -.
DR BioGRID; 34753; 385.
DR ComplexPortal; CPX-1636; Protein geranylgeranyltransferase type II complex.
DR DIP; DIP-2246N; -.
DR IntAct; P32864; 18.
DR MINT; P32864; -.
DR STRING; 4932.YOR370C; -.
DR iPTMnet; P32864; -.
DR MaxQB; P32864; -.
DR PaxDb; P32864; -.
DR PRIDE; P32864; -.
DR EnsemblFungi; YOR370C_mRNA; YOR370C; YOR370C.
DR GeneID; 854552; -.
DR KEGG; sce:YOR370C; -.
DR SGD; S000005897; MRS6.
DR VEuPathDB; FungiDB:YOR370C; -.
DR eggNOG; KOG1439; Eukaryota.
DR GeneTree; ENSGT00950000182994; -.
DR HOGENOM; CLU_021695_3_1_1; -.
DR InParanoid; P32864; -.
DR OMA; TPWDVTI; -.
DR BioCyc; YEAST:G3O-33838-MON; -.
DR Reactome; R-SCE-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
DR Reactome; R-SCE-8873719; RAB geranylgeranylation.
DR Reactome; R-SCE-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR PRO; PR:P32864; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P32864; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0016020; C:membrane; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; IDA:SGD.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IMP:SGD.
DR GO; GO:0090630; P:activation of GTPase activity; IMP:SGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:SGD.
DR GO; GO:0018344; P:protein geranylgeranylation; IMP:SGD.
DR GO; GO:0006612; P:protein targeting to membrane; IMP:SGD.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR018203; GDP_dissociation_inhibitor.
DR InterPro; IPR017230; Mrs6.
DR PANTHER; PTHR11787; PTHR11787; 1.
DR Pfam; PF00996; GDI; 1.
DR PIRSF; PIRSF037514; Rab_ger_ger_transf_A_fun; 1.
DR PRINTS; PR00891; RABGDIREP.
DR PRINTS; PR00894; YEASTMRS6P.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW GTPase activation; Phosphoprotein; Reference proteome.
FT CHAIN 1..603
FT /note="Rab proteins geranylgeranyltransferase component A"
FT /id="PRO_0000056693"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950"
FT CONFLICT 132..137
FT /note="DLSPKI -> MIFPRV (in Ref. 5; AAA34796)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="A -> P (in Ref. 2; CAA49804/CAA49805 and 5;
FT AAA34796)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 603 AA; 67374 MW; 30BB7FFF8D712FFD CRC64;
MLSPERRPSM AERRPSFFSF TQNPSPLVVP HLAGIEDPLP ATTPDKVDVL IAGTGMVESV
LAAALAWQGS NVLHIDKNDY YGDTSATLTV DQIKRWVNEV NEGSVSCYKN AKLYVSTLIG
SGKYSSRDFG IDLSPKILFA KSDLLSILIK SRVHQYLEFQ SLSNFHTYEN DCFEKLTNTK
QEIFTDQNLP LMTKRNLMKF IKFVLNWEAQ TEIWQPYAER TMSDFLGEKF KLEKPQVFEL
IFSIGLCYDL NVKVPEALQR IRRYLTSFDV YGPFPALCSK YGGPGELSQG FCRSAAVGGA
TYKLNEKLVS FNPTTKVATF QDGSKVEVSE KVIISPTQAP KDSKHVPQQQ YQVHRLTCIV
ENPCTEWFNE GESAAMVVFP PGSLKSGNKE VVQAFILGAG SEICPEGTIV WYLSTTEQGP
RAEMDIDAAL EAMEMALLRE SSSGLENDEE IVQLTGNGHT IVNSVKLGQS FKEYVPRERL
QFLFKLYYTQ YTSTPPFGVV NSSFFDVNQD LEKKYIPGAS DNGVIYTTMP SAEISYDEVV
TAAKVLYEKI VGSDDDFFDL DFEDEDEIQA SGVANAEQFE NAIDDDDDVN MEGSGEFVGE
MEI
