ID GDI1_YEAST STANDARD; PRT; 451 AA. AC P39958; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 30-MAY-2006, entry version 44. DE Rab GDP-dissociation inhibitor (Rab GDI) (Secretory pathway GDP DE dissociation inhibitor). GN Name=GDI1; Synonyms=SEC19; OrderedLocusNames=YER136W; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC 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=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. 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. 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 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 P36017:YPT51; NbExp=1; IntAct=EBI-7517, EBI-29399; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- MISCELLANEOUS: Present with 7280 molecules/cell. 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 PDB; 1UKV; X-ray; G=1-451. DR PDB; 2BCG; X-ray; G=1-451. DR IntAct; P39958; -. DR GermOnline; 139215; -. DR Ensembl; YER136W; Saccharomyces cerevisiae. DR GenomeReviews; U00092_GR; YER136W. DR SGD; S000000938; GDI1. DR BioCyc; SCER-S28-01:SCER-S28-01-001808-MONOMER; -. DR LinkHub; P39958; -. DR GO; GO:0005624; C:membrane fraction; IDA. DR GO; GO:0005625; C:soluble fraction; IDA. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0005093; F:Rab GDP-dissociation inhibitor activity; IDA. DR GO; GO:0016192; P:vesicle-mediated transport; IMP. 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. KW 3D-structure; Complete proteome; GTPase activation; Protein transport; KW 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 9 9 FT STRAND 11 15 FT STRAND 18 18 FT HELIX 19 30 FT TURN 31 32 FT STRAND 35 38 FT STRAND 40 44 FT HELIX 46 48 FT STRAND 50 51 FT HELIX 53 60 FT STRAND 62 63 FT HELIX 67 74 FT HELIX 77 79 FT STRAND 82 85 FT STRAND 88 90 FT TURN 91 92 FT STRAND 93 93 FT HELIX 94 101 FT TURN 102 103 FT HELIX 104 106 FT TURN 107 107 FT STRAND 110 112 FT STRAND 116 120 FT TURN 121 122 FT STRAND 123 126 FT STRAND 129 130 FT HELIX 131 136 FT TURN 138 139 FT STRAND 140 140 FT HELIX 142 157 FT TURN 160 161 FT HELIX 163 165 FT STRAND 166 166 FT TURN 167 168 FT TURN 171 173 FT STRAND 174 175 FT HELIX 176 182 FT TURN 183 184 FT HELIX 187 196 FT TURN 197 197 FT STRAND 198 198 FT STRAND 201 203 FT HELIX 204 207 FT STRAND 208 210 FT HELIX 211 227 FT STRAND 228 229 FT STRAND 231 235 FT TURN 236 237 FT TURN 239 240 FT HELIX 241 252 FT TURN 253 254 FT STRAND 256 258 FT STRAND 260 260 FT STRAND 264 268 FT TURN 270 272 FT STRAND 275 280 FT TURN 281 282 FT STRAND 283 286 FT STRAND 288 288 FT STRAND 290 292 FT HELIX 294 296 FT HELIX 298 300 FT STRAND 301 317 FT TURN 320 321 FT STRAND 322 322 FT TURN 323 324 FT STRAND 326 332 FT HELIX 334 336 FT TURN 337 338 FT STRAND 340 341 FT STRAND 343 349 FT HELIX 350 352 FT TURN 353 353 FT STRAND 354 355 FT TURN 357 358 FT STRAND 360 367 FT STRAND 370 371 FT HELIX 373 376 FT TURN 377 377 FT HELIX 378 382 FT TURN 383 384 FT STRAND 386 386 FT STRAND 388 402 FT STRAND 404 404 FT TURN 405 407 FT STRAND 408 411 FT STRAND 417 417 FT STRAND 419 420 FT TURN 421 421 FT HELIX 422 436 FT STRAND 437 438 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 //