ID GDI1_YEAST Reviewed; 451 AA. AC P39958; D3DM41; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 07-APR-2021, entry version 167. DE RecName: Full=Rab GDP-dissociation inhibitor; DE Short=Rab GDI; DE AltName: Full=Secretory pathway GDP dissociation inhibitor; GN Name=GDI1; Synonyms=SEC19; OrderedLocusNames=YER136W; 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], AND FUNCTION. RX PubMed=8157010; DOI=10.1002/j.1460-2075.1994.tb06436.x; RA Garrett M.D., Zahner J.E., Cheney C.M., Novick P.J.; RT "GDI1 encodes a GDP dissociation inhibitor that plays an essential role in RT the yeast secretory pathway."; RL EMBO J. 13:1718-1728(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169868; RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., RA Botstein D., Davis R.W.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V."; RL Nature 387:78-81(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 INTERACTION WITH YPT10. RX PubMed=10394895; DOI=10.1007/s004380050001; RA Louvet O., Roumanie O., Barthe C., Peypouquet M.-F., Schaeffer J., RA Doignon F., Crouzet M.; RT "Characterization of the ORF YBR264c in Saccharomyces cerevisiae, which RT encodes a new yeast Ypt that is degraded by a proteasome-dependent RT mechanism."; RL Mol. Gen. Genet. 261:589-600(1999). RN [5] RP FUNCTION. RX PubMed=11118206; DOI=10.1093/emboj/19.24.6713; RA Eitzen G., Will E., Gallwitz D., Haas A., Wickner W.; RT "Sequential action of two GTPases to promote vacuole docking and fusion."; RL EMBO J. 19:6713-6720(2000). RN [6] 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 [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 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). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH YPT1. RX PubMed=14576435; DOI=10.1126/science.1087761; RA Rak A., Pylypenko O., Durek T., Watzke A., Kushnir S., Brunsveld L., RA Waldmann H., Goody R.S., Alexandrov K.; RT "Structure of Rab GDP-dissociation inhibitor in complex with prenylated RT YPT1 GTPase."; RL Science 302:646-650(2003). RN [10] RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEX WITH YPT1. RX PubMed=16395334; DOI=10.1038/sj.emboj.7600921; RA Pylypenko O., Rak A., Durek T., Kushnir S., Dursina B.E., Thomae N.H., RA Constantinescu A.T., Brunsveld L., Watzke A., Waldmann H., Goody R.S., RA Alexandrov K.; RT "Structure of doubly prenylated Ypt1:GDI complex and the mechanism of GDI- RT mediated Rab recycling."; RL EMBO J. 25:13-23(2006). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS). RX PubMed=18426803; DOI=10.1074/jbc.m709718200; RA Ignatev A., Kravchenko S., Rak A., Goody R.S., Pylypenko O.; RT "A structural model of the GDP dissociation inhibitor rab membrane RT extraction mechanism."; RL J. Biol. Chem. 283:18377-18384(2008). CC -!- FUNCTION: Regulates the GDP/GTP exchange reaction of SEC4 by inhibiting CC the dissociation of GDP from it, and the subsequent binding of GTP to CC SEC4. Plays an essential role in the yeast secretory pathway CC (PubMed:8157010). Extracts GDP-bound YPT7 from vacuolar membranes, CC antagonizing vacuolar membrane fusion (PubMed:11118206). CC {ECO:0000269|PubMed:11118206, ECO:0000269|PubMed:8157010}. CC -!- SUBUNIT: Interacts with the GDP-bound form of Rab GTPase YPT1. CC Interacts with YPT10. {ECO:0000269|PubMed:10394895, CC ECO:0000269|PubMed:14576435}. CC -!- INTERACTION: CC P39958; P07560: SEC4; NbExp=3; IntAct=EBI-7517, EBI-16858; CC P39958; P36017: VPS21; NbExp=4; IntAct=EBI-7517, EBI-29399; CC P39958; P01123: YPT1; NbExp=6; IntAct=EBI-7517, EBI-29496; CC P39958; P38146: YPT10; NbExp=6; IntAct=EBI-7517, EBI-29357; CC P39958; P38555: YPT31; NbExp=5; IntAct=EBI-7517, EBI-29379; CC P39958; P51996: YPT32; NbExp=3; IntAct=EBI-7517, EBI-29384; CC P39958; P36018: YPT52; NbExp=3; IntAct=EBI-7517, EBI-29407; CC P39958; Q99260: YPT6; NbExp=5; IntAct=EBI-7517, EBI-29503; CC P39958; P32939: YPT7; NbExp=3; IntAct=EBI-7517, EBI-29509; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. CC -!- MISCELLANEOUS: Present with 7280 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the Rab GDI 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; S69371; AAB30540.1; -; Genomic_DNA. DR EMBL; U18916; AAC03234.1; -; Genomic_DNA. DR EMBL; BK006939; DAA07795.1; -; Genomic_DNA. DR PIR; S44446; S44446. DR RefSeq; NP_011062.1; NM_001179026.1. DR PDB; 1UKV; X-ray; 1.50 A; G=1-451. DR PDB; 2BCG; X-ray; 1.48 A; G=1-451. DR PDB; 3CPH; X-ray; 2.90 A; G/H=1-451. DR PDB; 3CPI; X-ray; 2.30 A; G/H=1-451. DR PDB; 3CPJ; X-ray; 2.35 A; G=1-451. DR PDBsum; 1UKV; -. DR PDBsum; 2BCG; -. DR PDBsum; 3CPH; -. DR PDBsum; 3CPI; -. DR PDBsum; 3CPJ; -. DR SMR; P39958; -. DR BioGRID; 36882; 268. DR DIP; DIP-785N; -. DR IntAct; P39958; 20. DR MINT; P39958; -. DR STRING; 4932.YER136W; -. DR iPTMnet; P39958; -. DR UCD-2DPAGE; P39958; -. DR MaxQB; P39958; -. DR PaxDb; P39958; -. DR PRIDE; P39958; -. DR EnsemblFungi; YER136W_mRNA; YER136W; YER136W. DR GeneID; 856876; -. DR KEGG; sce:YER136W; -. DR SGD; S000000938; GDI1. DR VEuPathDB; FungiDB:YER136W; -. DR eggNOG; KOG1439; Eukaryota. DR GeneTree; ENSGT00950000182994; -. DR HOGENOM; CLU_021695_0_0_1; -. DR InParanoid; P39958; -. DR OMA; DFLGHAV; -. DR Reactome; R-SCE-6798695; Neutrophil degranulation. DR Reactome; R-SCE-8876198; RAB GEFs exchange GTP for GDP on RABs. DR EvolutionaryTrace; P39958; -. DR PRO; PR:P39958; -. DR Proteomes; UP000002311; Chromosome V. DR RNAct; P39958; protein. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW. DR GO; GO:0005093; F:Rab GDP-dissociation inhibitor activity; IDA:SGD. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro. DR GO; GO:0016192; P:vesicle-mediated transport; IMP:SGD. DR Gene3D; 3.50.50.60; -; 1. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR018203; GDP_dissociation_inhibitor. DR InterPro; IPR000806; RabGDI. DR PANTHER; PTHR11787; PTHR11787; 1. DR Pfam; PF00996; GDI; 1. DR PRINTS; PR00892; RABGDI. DR PRINTS; PR00891; RABGDIREP. DR SUPFAM; SSF51905; SSF51905; 2. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; GTPase activation; Protein transport; KW Reference proteome; Transport. FT CHAIN 1..451 FT /note="Rab GDP-dissociation inhibitor" FT /id="PRO_0000056684" FT REGION 106..112 FT /note="Interaction with YPT1" FT /evidence="ECO:0000269|PubMed:14576435" FT REGION 234..259 FT /note="Interaction with YPT1" FT /evidence="ECO:0000269|PubMed:14576435" FT STRAND 11..15 FT /evidence="ECO:0007744|PDB:2BCG" FT HELIX 19..30 FT /evidence="ECO:0007744|PDB:2BCG" FT STRAND 35..38 FT /evidence="ECO:0007744|PDB:2BCG" FT STRAND 40..44 FT /evidence="ECO:0007744|PDB:2BCG" FT HELIX 46..48 FT /evidence="ECO:0007744|PDB:2BCG" FT HELIX 53..60 FT /evidence="ECO:0007744|PDB:2BCG" FT HELIX 67..74 FT /evidence="ECO:0007744|PDB:2BCG" FT HELIX 77..79 FT /evidence="ECO:0007744|PDB:2BCG" FT STRAND 82..85 FT /evidence="ECO:0007744|PDB:2BCG" FT STRAND 88..90 FT /evidence="ECO:0007744|PDB:2BCG" FT HELIX 94..101 FT /evidence="ECO:0007744|PDB:2BCG" FT HELIX 104..106 FT /evidence="ECO:0007744|PDB:2BCG" FT STRAND 110..112 FT /evidence="ECO:0007744|PDB:2BCG" FT STRAND 116..120 FT /evidence="ECO:0007744|PDB:2BCG" FT STRAND 123..126 FT /evidence="ECO:0007744|PDB:2BCG" FT HELIX 131..136 FT /evidence="ECO:0007744|PDB:2BCG" FT STRAND 138..140 FT /evidence="ECO:0007744|PDB:3CPJ" FT HELIX 142..157 FT /evidence="ECO:0007744|PDB:2BCG" FT HELIX 163..165 FT /evidence="ECO:0007744|PDB:2BCG" FT TURN 171..173 FT /evidence="ECO:0007744|PDB:2BCG" FT HELIX 176..182 FT /evidence="ECO:0007744|PDB:2BCG" FT HELIX 187..196 FT /evidence="ECO:0007744|PDB:2BCG" FT STRAND 201..203 FT /evidence="ECO:0007744|PDB:2BCG" FT HELIX 204..207 FT /evidence="ECO:0007744|PDB:2BCG" FT STRAND 208..210 FT /evidence="ECO:0007744|PDB:2BCG" FT HELIX 211..227 FT /evidence="ECO:0007744|PDB:2BCG" FT STRAND 231..235 FT /evidence="ECO:0007744|PDB:2BCG" FT HELIX 241..252 FT /evidence="ECO:0007744|PDB:2BCG" FT STRAND 256..258 FT /evidence="ECO:0007744|PDB:2BCG" FT STRAND 265..268 FT /evidence="ECO:0007744|PDB:2BCG" FT TURN 270..272 FT /evidence="ECO:0007744|PDB:2BCG" FT STRAND 275..280 FT /evidence="ECO:0007744|PDB:2BCG" FT STRAND 283..286 FT /evidence="ECO:0007744|PDB:2BCG" FT STRAND 290..292 FT /evidence="ECO:0007744|PDB:2BCG" FT HELIX 294..296 FT /evidence="ECO:0007744|PDB:2BCG" FT HELIX 298..300 FT /evidence="ECO:0007744|PDB:2BCG" FT STRAND 301..317 FT /evidence="ECO:0007744|PDB:2BCG" FT STRAND 322..324 FT /evidence="ECO:0007744|PDB:3CPI" FT STRAND 326..332 FT /evidence="ECO:0007744|PDB:2BCG" FT HELIX 334..336 FT /evidence="ECO:0007744|PDB:2BCG" FT STRAND 343..349 FT /evidence="ECO:0007744|PDB:2BCG" FT HELIX 350..352 FT /evidence="ECO:0007744|PDB:2BCG" FT STRAND 360..367 FT /evidence="ECO:0007744|PDB:2BCG" FT HELIX 373..376 FT /evidence="ECO:0007744|PDB:2BCG" FT HELIX 378..381 FT /evidence="ECO:0007744|PDB:2BCG" FT HELIX 382..384 FT /evidence="ECO:0007744|PDB:2BCG" FT STRAND 388..402 FT /evidence="ECO:0007744|PDB:2BCG" FT TURN 405..407 FT /evidence="ECO:0007744|PDB:2BCG" FT STRAND 408..411 FT /evidence="ECO:0007744|PDB:2BCG" FT STRAND 419..421 FT /evidence="ECO:0007744|PDB:2BCG" FT HELIX 422..436 FT /evidence="ECO:0007744|PDB:2BCG" SQ SEQUENCE 451 AA; 51206 MW; 48CF8D45FC031772 CRC64; MDQETIDTDY DVIVLGTGIT ECILSGLLSV DGKKVLHIDK QDHYGGEAAS VTLSQLYEKF KQNPISKEER ESKFGKDRDW NVDLIPKFLM ANGELTNILI HTDVTRYVDF KQVSGSYVFK QGKIYKVPAN EIEAISSPLM GIFEKRRMKK FLEWISSYKE DDLSTHQGLD LDKNTMDEVY YKFGLGNSTK EFIGHAMALW TNDDYLQQPA RPSFERILLY CQSVARYGKS PYLYPMYGLG ELPQGFARLS AIYGGTYMLD TPIDEVLYKK DTGKFEGVKT KLGTFKAPLV IADPTYFPEK CKSTGQRVIR AICILNHPVP NTSNADSLQI IIPQSQLGRK SDIYVAIVSD AHNVCSKGHY LAIISTIIET DKPHIELEPA FKLLGPIEEK FMGIAELFEP REDGSKDNIY LSRSYDASSH FESMTDDVKD IYFRVTGHPL VLKQRQEQEK Q //