ID GDI1_YEAST Reviewed; 451 AA. AC P39958; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 15-DEC-2009, entry version 81. 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 (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. RX MEDLINE=94208542; 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 204511 / S288c / AB972; RX MEDLINE=97313264; 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 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 [4] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923954; 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 [5] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923965; 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 [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND MASS RP SPECTROMETRY. RX PubMed=17563356; DOI=10.1073/pnas.0701622104; RA Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; RT "Proteome-wide identification of in vivo targets of DNA damage RT checkpoint kinases."; RL Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54, AND MASS RP SPECTROMETRY. 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 RT phosphoproteome analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). 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. CC -!- SUBUNIT: Interacts with the GDP-bound form of Rab GTPase YPT1. CC Interacts with YPT10. CC -!- INTERACTION: CC P38295:EHT1; NbExp=1; IntAct=EBI-7517, EBI-20890; CC P19807:HNM1; NbExp=1; IntAct=EBI-7517, EBI-8409; CC P07560:SEC4; NbExp=1; IntAct=EBI-7517, EBI-16858; CC P36017:VPS21; NbExp=2; IntAct=EBI-7517, EBI-29399; CC P01123:YPT1; NbExp=2; IntAct=EBI-7517, EBI-29496; CC P38146:YPT10; NbExp=3; IntAct=EBI-7517, EBI-29357; CC P38555:YPT31; NbExp=2; IntAct=EBI-7517, EBI-29379; CC P51996:YPT32; NbExp=1; IntAct=EBI-7517, EBI-29384; CC Q99260:YPT6; NbExp=1; IntAct=EBI-7517, EBI-29503; CC P32939:YPT7; NbExp=1; IntAct=EBI-7517, EBI-29509; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- MISCELLANEOUS: Present with 7280 molecules/cell in log phase SD CC medium. CC -!- SIMILARITY: Belongs to the Rab GDI family. 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 PIR; S44446; S44446. DR RefSeq; NP_011062.1; -. 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 DIP; DIP-785N; -. DR IntAct; P39958; 30. DR STRING; P39958; -. DR PeptideAtlas; P39958; -. DR PRIDE; P39958; -. DR Ensembl; YER136W; YER136W; YER136W; Saccharomyces cerevisiae. DR GeneID; 856876; -. DR KEGG; sce:YER136W; -. DR NMPDR; fig|4932.3.peg.2139; -. DR CYGD; YER136w; -. DR SGD; S000000938; GDI1. DR HOGENOM; HBG330736; -. DR OMA; NPQSELK; -. DR OrthoDB; EOG937SX7; -. DR NextBio; 983252; -. DR ArrayExpress; P39958; -. DR Genevestigator; P39958; -. DR GermOnline; YER136W; Saccharomyces cerevisiae. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005624; C:membrane fraction; IDA:SGD. DR GO; GO:0005625; C:soluble fraction; IDA:SGD. DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW. DR GO; GO:0005515; F:protein binding; IPI:IntAct. 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:0043087; P:regulation of GTPase activity; IEA:InterPro. DR GO; GO:0016192; P:vesicle-mediated transport; IMP:SGD. DR InterPro; IPR018203; GDP_dissociation_inhibitor. DR InterPro; IPR002005; Rab_GDI_REP. DR InterPro; IPR000806; RabGDI. DR PANTHER; PTHR11787; Rab_GDI_REP; 1. DR Pfam; PF00996; GDI; 1. DR PRINTS; PR00892; RABGDI. DR PRINTS; PR00891; RABGDIREP. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; GTPase activation; KW Phosphoprotein; Protein transport; 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 MOD_RES 54 54 Phosphoserine. FT MOD_RES 230 230 Phosphoserine. FT STRAND 11 15 FT HELIX 19 30 FT STRAND 35 38 FT STRAND 40 44 FT HELIX 46 48 FT HELIX 53 60 FT HELIX 67 74 FT HELIX 77 79 FT STRAND 82 85 FT STRAND 88 90 FT HELIX 94 101 FT HELIX 104 106 FT STRAND 110 112 FT STRAND 116 120 FT STRAND 123 126 FT HELIX 131 136 FT HELIX 142 157 FT HELIX 163 165 FT TURN 171 173 FT HELIX 176 182 FT HELIX 187 196 FT STRAND 201 203 FT HELIX 204 207 FT STRAND 208 210 FT HELIX 211 227 FT STRAND 231 235 FT HELIX 241 252 FT STRAND 256 258 FT STRAND 265 268 FT TURN 270 272 FT STRAND 275 280 FT STRAND 283 286 FT STRAND 290 292 FT HELIX 294 296 FT HELIX 298 300 FT STRAND 301 317 FT STRAND 326 332 FT HELIX 334 336 FT STRAND 343 349 FT HELIX 350 352 FT STRAND 360 367 FT HELIX 373 376 FT HELIX 378 381 FT HELIX 382 384 FT STRAND 388 402 FT TURN 405 407 FT STRAND 408 411 FT STRAND 419 421 FT HELIX 422 436 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 //