ID YPT32_YEAST Reviewed; 222 AA. AC P51996; D6VTU5; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 197. DE RecName: Full=GTP-binding protein YPT32/YPT11; DE AltName: Full=Rab GTPase YPT32; GN Name=YPT32; Synonyms=YPT11; OrderedLocusNames=YGL210W; 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. RC STRAIN=DUR; RX PubMed=8978673; DOI=10.1002/j.1460-2075.1996.tb01037.x; RA Benli M., Doering F., Robinson D.G., Yang X., Gallwitz D.; RT "Two GTPase isoforms, Ypt31p and Ypt32p, are essential for Golgi function RT in yeast."; RL EMBO J. 15:6460-6475(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8813766; RX DOI=10.1002/(sici)1097-0061(19960630)12:8<799::aid-yea965>3.0.co;2-u; RA Kail M., Juettner E., Vaux D.; RT "Lambda clone B22 contains a 7676 bp genomic fragment of Saccharomyces RT cerevisiae chromosome VII spanning the VAM7-SPM2 intergenic region and RT containing three novel transcribed open reading frames."; RL Yeast 12:799-807(1996). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9153757; RX DOI=10.1002/(sici)1097-0061(199704)13:5<475::aid-yea101>3.0.co;2-0; RA Feuermann M., Simeonava L., Souciet J.-L., Potier S.; RT "Analysis of 21.7 kb DNA sequence from the left arm of chromosome VII RT reveals 11 open reading frames: two correspond to new genes."; RL Yeast 13:475-477(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169869; RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H., RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."; RL Nature 387:81-84(1997). RN [5] 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 [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [7] RP FUNCTION, MUTAGENESIS OF ALA-141, AND SUBCELLULAR LOCATION. RX PubMed=9151665; DOI=10.1083/jcb.137.3.563; RA Jedd G., Mulholland J., Segev N.; RT "Two new Ypt GTPases are required for exit from the yeast trans-Golgi RT compartment."; RL J. Cell Biol. 137:563-580(1997). RN [8] RP ACTIVITY REGULATION. RX PubMed=10559187; DOI=10.1074/jbc.274.47.33186; RA Albert S., Gallwitz D.; RT "Two new members of a family of Ypt/Rab GTPase activating proteins. RT Promiscuity of substrate recognition."; RL J. Biol. Chem. 274:33186-33189(1999). RN [9] RP ACTIVITY REGULATION. RX PubMed=11102533; DOI=10.1091/mbc.11.12.4403; RA Jones S., Newman C., Liu F., Segev N.; RT "The TRAPP complex is a nucleotide exchanger for Ypt1 and Ypt31/32."; RL Mol. Biol. Cell 11:4403-4411(2000). RN [10] RP INTERACTION WITH YIP3. RX PubMed=11785952; DOI=10.1006/bbrc.2001.6242; RA Calero M., Collins R.N.; RT "Saccharomyces cerevisiae Pra1p/Yip3p interacts with Yip1p and Rab RT proteins."; RL Biochem. Biophys. Res. Commun. 290:676-681(2002). RN [11] RP FUNCTION, AND INTERACTION WITH TRS130. RX PubMed=12478387; DOI=10.1007/s00294-002-0336-5; RA Yamamoto K., Jigami Y.; RT "Mutation of TRS130, which encodes a component of the TRAPP II complex, RT activates transcription of OCH1 in Saccharomyces cerevisiae."; RL Curr. Genet. 42:85-93(2002). RN [12] RP INTERACTION WITH YIF1; YIP4 AND YIP5. RX PubMed=11943201; DOI=10.1016/s0014-5793(02)02442-0; RA Calero M., Winand N.J., Collins R.N.; RT "Identification of the novel proteins Yip4p and Yip5p as Rab GTPase RT interacting factors."; RL FEBS Lett. 515:89-98(2002). RN [13] RP FUNCTION, INTERACTION WITH SEC2, AND MUTAGENESIS OF SER-27; GLU-49; GLN-72 RP AND ASN-126. RX PubMed=12045183; DOI=10.1083/jcb.200201003; RA Ortiz D., Medkova M., Walch-Solimena C., Novick P.J.; RT "Ypt32 recruits the Sec4p guanine nucleotide exchange factor, Sec2p, to RT secretory vesicles; evidence for a Rab cascade in yeast."; RL J. Cell Biol. 157:1005-1015(2002). RN [14] 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 [15] RP FUNCTION. RX PubMed=23078654; DOI=10.1111/tra.12024; RA Zou S., Chen Y., Liu Y., Segev N., Yu S., Liu Y., Min G., Ye M., Zeng Y., RA Zhu X., Hong B., Bjorn L.O., Liang Y., Li S., Xie Z.; RT "Trs130 participates in autophagy through GTPases Ypt31/32 in Saccharomyces RT cerevisiae."; RL Traffic 14:233-246(2013). CC -!- FUNCTION: Required for protein transport through the secretory pathway. CC Probably involved in regulation of secretory vesicle formation at the CC trans-Golgi compartment. Mediates the proper polarized localization of CC SEC2, a GEF for SEC4, but does not alter the exchange activity of SEC2 CC on SEC4. Plays a role in autophagy. {ECO:0000269|PubMed:12045183, CC ECO:0000269|PubMed:12478387, ECO:0000269|PubMed:23078654, CC ECO:0000269|PubMed:8978673, ECO:0000269|PubMed:9151665}. CC -!- ACTIVITY REGULATION: Alternates between an inactive form bound to GDP CC and an active form bound to GTP. Activated by the guanine nucleotide- CC exchange factor (GEF) TRAPP complex, and inactivated by GTPase- CC activating protein (GAP) GYP3. {ECO:0000269|PubMed:10559187, CC ECO:0000269|PubMed:11102533}. CC -!- SUBUNIT: Interacts with YIF1, YIP3, YIP4 and YIP5. Interacts with the CC GEF SEC2. Interacts with TRS130. {ECO:0000269|PubMed:11785952, CC ECO:0000269|PubMed:11943201, ECO:0000269|PubMed:12045183, CC ECO:0000269|PubMed:12478387}. CC -!- INTERACTION: CC P51996; P39958: GDI1; NbExp=3; IntAct=EBI-29384, EBI-7517; CC P51996; Q08484: GYP1; NbExp=3; IntAct=EBI-29384, EBI-8005; CC P51996; P53845: YIF1; NbExp=2; IntAct=EBI-29384, EBI-28230; CC P51996; P53633: YIP3; NbExp=2; IntAct=EBI-29384, EBI-25301; CC P51996; P53093: YIP4; NbExp=2; IntAct=EBI-29384, EBI-24124; CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000269|PubMed:9151665}; Lipid-anchor CC {ECO:0000269|PubMed:9151665}. CC -!- MISCELLANEOUS: Present with 4298 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family. CC {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; X72834; CAA51355.1; -; Genomic_DNA. DR EMBL; U33754; AAC49495.1; -; Genomic_DNA. DR EMBL; Z72732; CAA96926.1; -; Genomic_DNA. DR EMBL; AY558506; AAS56832.1; -; Genomic_DNA. DR EMBL; BK006941; DAA07906.1; -; Genomic_DNA. DR PIR; S58514; S58514. DR RefSeq; NP_011305.1; NM_001181075.1. DR PDB; 3RWM; X-ray; 2.00 A; B=7-188. DR PDB; 3RWO; X-ray; 1.70 A; A/B=7-188. DR PDB; 7E8T; EM; 3.80 A; L=1-222. DR PDB; 7EA3; EM; 4.31 A; L/Y=1-222. DR PDB; 7U05; EM; 3.70 A; L/l=1-220. DR PDB; 7U06; EM; 4.20 A; l=1-220. DR PDBsum; 3RWM; -. DR PDBsum; 3RWO; -. DR PDBsum; 7E8T; -. DR PDBsum; 7EA3; -. DR PDBsum; 7U05; -. DR PDBsum; 7U06; -. DR AlphaFoldDB; P51996; -. DR EMDB; EMD-26254; -. DR EMDB; EMD-26255; -. DR EMDB; EMD-31022; -. DR EMDB; EMD-31038; -. DR SMR; P51996; -. DR BioGRID; 33046; 134. DR DIP; DIP-6597N; -. DR IntAct; P51996; 7. DR MINT; P51996; -. DR STRING; 4932.YGL210W; -. DR iPTMnet; P51996; -. DR MaxQB; P51996; -. DR PaxDb; 4932-YGL210W; -. DR PeptideAtlas; P51996; -. DR EnsemblFungi; YGL210W_mRNA; YGL210W; YGL210W. DR GeneID; 852662; -. DR KEGG; sce:YGL210W; -. DR AGR; SGD:S000003178; -. DR SGD; S000003178; YPT32. DR VEuPathDB; FungiDB:YGL210W; -. DR eggNOG; KOG0087; Eukaryota. DR GeneTree; ENSGT00940000171249; -. DR HOGENOM; CLU_041217_23_0_1; -. DR InParanoid; P51996; -. DR OMA; ITAIYQM; -. DR OrthoDB; 3487147at2759; -. DR BioCyc; YEAST:G3O-30687-MONOMER; -. DR Reactome; R-SCE-5620912; Anchoring of the basal body to the plasma membrane. DR Reactome; R-SCE-8873719; RAB geranylgeranylation. DR BioGRID-ORCS; 852662; 0 hits in 10 CRISPR screens. DR PRO; PR:P51996; -. DR Proteomes; UP000002311; Chromosome VII. DR RNAct; P51996; Protein. DR GO; GO:0005935; C:cellular bud neck; HDA:SGD. DR GO; GO:0005829; C:cytosol; IEA:GOC. DR GO; GO:0005768; C:endosome; IDA:SGD. DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD. DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IBA:GO_Central. DR GO; GO:0003924; F:GTPase activity; IDA:SGD. DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW. DR GO; GO:0034498; P:early endosome to Golgi transport; IGI:SGD. DR GO; GO:0006887; P:exocytosis; IMP:SGD. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0016192; P:vesicle-mediated transport; IMP:SGD. DR CDD; cd01868; Rab11_like; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR001806; Small_GTPase. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR47979:SF33; DRAB11; 1. DR PANTHER; PTHR47979; DRAB11-RELATED; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00175; RAB; 1. DR SMART; SM00176; RAN; 1. DR SMART; SM00173; RAS; 1. DR SMART; SM00174; RHO; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51419; RAB; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Autophagy; Exocytosis; Golgi apparatus; KW GTP-binding; Lipoprotein; Membrane; Nucleotide-binding; Prenylation; KW Protein transport; Reference proteome; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P38555" FT CHAIN 2..222 FT /note="GTP-binding protein YPT32/YPT11" FT /id="PRO_0000121324" FT REGION 186..222 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 42..50 FT /note="Effector region" FT /evidence="ECO:0000305" FT COMPBIAS 186..202 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 20..27 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 68..72 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 126..129 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000250|UniProtKB:P38555" FT LIPID 221 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000250" FT LIPID 222 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000250" FT MUTAGEN 27 FT /note="S->N: Binds preferentially GDP." FT /evidence="ECO:0000269|PubMed:12045183" FT MUTAGEN 49 FT /note="E->Q: Cold sensitive." FT /evidence="ECO:0000269|PubMed:12045183" FT MUTAGEN 72 FT /note="Q->L: Reduces GTPase activity." FT /evidence="ECO:0000269|PubMed:12045183" FT MUTAGEN 126 FT /note="N->I: Blocks nucleotide binding." FT /evidence="ECO:0000269|PubMed:12045183" FT MUTAGEN 141 FT /note="A->D: Loss of function at 37 degrees Celsius." FT /evidence="ECO:0000269|PubMed:9151665" FT STRAND 11..19 FT /evidence="ECO:0007829|PDB:3RWO" FT HELIX 26..35 FT /evidence="ECO:0007829|PDB:3RWO" FT STRAND 47..57 FT /evidence="ECO:0007829|PDB:3RWO" FT STRAND 60..71 FT /evidence="ECO:0007829|PDB:3RWO" FT HELIX 76..83 FT /evidence="ECO:0007829|PDB:3RWO" FT STRAND 88..94 FT /evidence="ECO:0007829|PDB:3RWO" FT HELIX 98..102 FT /evidence="ECO:0007829|PDB:3RWO" FT HELIX 104..114 FT /evidence="ECO:0007829|PDB:3RWO" FT STRAND 120..126 FT /evidence="ECO:0007829|PDB:3RWO" FT HELIX 128..133 FT /evidence="ECO:0007829|PDB:3RWO" FT HELIX 138..147 FT /evidence="ECO:0007829|PDB:3RWO" FT STRAND 151..154 FT /evidence="ECO:0007829|PDB:3RWO" FT TURN 157..159 FT /evidence="ECO:0007829|PDB:3RWO" FT HELIX 163..177 FT /evidence="ECO:0007829|PDB:3RWO" SQ SEQUENCE 222 AA; 24520 MW; 621217A296161964 CRC64; MSNEDYGYDY DYLFKIVLIG DSGVGKSNLL SRFTTDEFNI ESKSTIGVEF ATRTIEVENK KIKAQIWDTA GQERYRAITS AYYRGAVGAL IVYDISKSSS YENCNHWLTE LRENADDNVA VGLIGNKSDL AHLRAVPTDE AKNFAMENQM LFTETSALNS DNVDKAFREL IVAIFQMVSK HQVDLSGSGT NNMGSNGAPK GPTISLTPAP KEDKKKKSSN CC //