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 20-JAN-2016, entry version 128. 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; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. RX PubMed=8157010; RA Garrett M.D., Zahner J.E., Cheney C.M., Novick P.J.; RT "GDI1 encodes a GDP dissociation inhibitor that plays an essential RT role in 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., RA Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., RA Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., RA Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., RA Smith V., Taylor P., Wei Y., 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., RA Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and RT 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, RT which encodes a new yeast Ypt that is degraded by a proteasome- RT dependent mechanism."; RL Mol. Gen. Genet. 261:589-600(1999). RN [5] 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 [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., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [7] 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 RT insights into evolution."; RL Science 325:1682-1686(2009). RN [8] 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 RT prenylated YPT1 GTPase."; RL Science 302:646-650(2003). CC -!- FUNCTION: Regulates the GDP/GTP exchange reaction of SEC4 by CC inhibiting the dissociation of GDP from it, and the subsequent CC binding of GTP to SEC4. Plays an essential role in the yeast CC secretory pathway. {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 P01123:YPT1; NbExp=5; IntAct=EBI-7517, EBI-29496; CC P38146:YPT10; NbExp=4; IntAct=EBI-7517, EBI-29357; CC P38555:YPT31; NbExp=6; IntAct=EBI-7517, EBI-29379; CC P36018:YPT52; NbExp=3; IntAct=EBI-7517, EBI-29407; CC Q99260:YPT6; NbExp=3; IntAct=EBI-7517, EBI-29503; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. CC -!- MISCELLANEOUS: Present with 7280 molecules/cell in log phase SD CC medium. {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 ProteinModelPortal; P39958; -. DR SMR; P39958; 5-446. DR BioGrid; 36882; 37. DR DIP; DIP-785N; -. DR IntAct; P39958; 16. DR MINT; MINT-502785; -. DR iPTMnet; P39958; -. DR UCD-2DPAGE; P39958; -. DR MaxQB; P39958; -. DR PeptideAtlas; P39958; -. DR EnsemblFungi; YER136W; YER136W; YER136W. DR GeneID; 856876; -. DR KEGG; sce:YER136W; -. DR EuPathDB; FungiDB:YER136W; -. DR SGD; S000000938; GDI1. DR GeneTree; ENSGT00530000063044; -. DR HOGENOM; HOG000163825; -. DR InParanoid; P39958; -. DR KO; K17255; -. DR OMA; ITECILS; -. DR OrthoDB; EOG72C58R; -. DR BioCyc; YEAST:G3O-30297-MONOMER; -. DR Reactome; R-SCE-194840; Rho GTPase cycle. DR EvolutionaryTrace; P39958; -. DR NextBio; 983252; -. DR PRO; PR:P39958; -. DR Proteomes; UP000002311; Chromosome V. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. 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:0050790; P:regulation of catalytic activity; IDA:GOC. DR GO; GO:0016192; P:vesicle-mediated transport; IMP:SGD. DR Gene3D; 3.50.50.60; -; 2. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR018203; GDP_dissociation_inhibitor. DR InterPro; IPR000806; RabGDI. 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; Complete proteome; Cytoplasm; GTPase activation; KW Protein transport; Reference proteome; Transport. FT CHAIN 1 451 Rab GDP-dissociation inhibitor. FT /FTId=PRO_0000056684. FT REGION 106 112 Interaction with YPT1. FT REGION 234 259 Interaction with YPT1. FT STRAND 11 15 {ECO:0000244|PDB:2BCG}. FT HELIX 19 30 {ECO:0000244|PDB:2BCG}. FT STRAND 35 38 {ECO:0000244|PDB:2BCG}. FT STRAND 40 44 {ECO:0000244|PDB:2BCG}. FT HELIX 46 48 {ECO:0000244|PDB:2BCG}. FT HELIX 53 60 {ECO:0000244|PDB:2BCG}. FT HELIX 67 74 {ECO:0000244|PDB:2BCG}. FT HELIX 77 79 {ECO:0000244|PDB:2BCG}. FT STRAND 82 85 {ECO:0000244|PDB:2BCG}. FT STRAND 88 90 {ECO:0000244|PDB:2BCG}. FT HELIX 94 101 {ECO:0000244|PDB:2BCG}. FT HELIX 104 106 {ECO:0000244|PDB:2BCG}. FT STRAND 110 112 {ECO:0000244|PDB:2BCG}. FT STRAND 116 120 {ECO:0000244|PDB:2BCG}. FT STRAND 123 126 {ECO:0000244|PDB:2BCG}. FT HELIX 131 136 {ECO:0000244|PDB:2BCG}. FT STRAND 138 140 {ECO:0000244|PDB:3CPJ}. FT HELIX 142 157 {ECO:0000244|PDB:2BCG}. FT HELIX 163 165 {ECO:0000244|PDB:2BCG}. FT TURN 171 173 {ECO:0000244|PDB:2BCG}. FT HELIX 176 182 {ECO:0000244|PDB:2BCG}. FT HELIX 187 196 {ECO:0000244|PDB:2BCG}. FT STRAND 201 203 {ECO:0000244|PDB:2BCG}. FT HELIX 204 207 {ECO:0000244|PDB:2BCG}. FT STRAND 208 210 {ECO:0000244|PDB:2BCG}. FT HELIX 211 227 {ECO:0000244|PDB:2BCG}. FT STRAND 231 235 {ECO:0000244|PDB:2BCG}. FT HELIX 241 252 {ECO:0000244|PDB:2BCG}. FT STRAND 256 258 {ECO:0000244|PDB:2BCG}. FT STRAND 265 268 {ECO:0000244|PDB:2BCG}. FT TURN 270 272 {ECO:0000244|PDB:2BCG}. FT STRAND 275 280 {ECO:0000244|PDB:2BCG}. FT STRAND 283 286 {ECO:0000244|PDB:2BCG}. FT STRAND 290 292 {ECO:0000244|PDB:2BCG}. FT HELIX 294 296 {ECO:0000244|PDB:2BCG}. FT HELIX 298 300 {ECO:0000244|PDB:2BCG}. FT STRAND 301 317 {ECO:0000244|PDB:2BCG}. FT STRAND 322 324 {ECO:0000244|PDB:3CPI}. FT STRAND 326 332 {ECO:0000244|PDB:2BCG}. FT HELIX 334 336 {ECO:0000244|PDB:2BCG}. FT STRAND 343 349 {ECO:0000244|PDB:2BCG}. FT HELIX 350 352 {ECO:0000244|PDB:2BCG}. FT STRAND 360 367 {ECO:0000244|PDB:2BCG}. FT HELIX 373 376 {ECO:0000244|PDB:2BCG}. FT HELIX 378 381 {ECO:0000244|PDB:2BCG}. FT HELIX 382 384 {ECO:0000244|PDB:2BCG}. FT STRAND 388 402 {ECO:0000244|PDB:2BCG}. FT TURN 405 407 {ECO:0000244|PDB:2BCG}. FT STRAND 408 411 {ECO:0000244|PDB:2BCG}. FT STRAND 419 421 {ECO:0000244|PDB:2BCG}. FT HELIX 422 436 {ECO:0000244|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 //