YPT32_YEAST
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 03-AUG-2022, entry version 191.
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}.
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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 PDBsum; 3RWM; -.
DR PDBsum; 3RWO; -.
DR PDBsum; 7E8T; -.
DR PDBsum; 7EA3; -.
DR AlphaFoldDB; P51996; -.
DR SMR; P51996; -.
DR BioGRID; 33046; 110.
DR DIP; DIP-6597N; -.
DR IntAct; P51996; 7.
DR MINT; P51996; -.
DR STRING; 4932.YGL210W; -.
DR iPTMnet; P51996; -.
DR MaxQB; P51996; -.
DR PaxDb; P51996; -.
DR PRIDE; P51996; -.
DR EnsemblFungi; YGL210W_mRNA; YGL210W; YGL210W.
DR GeneID; 852662; -.
DR KEGG; sce:YGL210W; -.
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; PSSYENC; -.
DR BioCyc; YEAST:G3O-30687-MON; -.
DR Reactome; R-SCE-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-SCE-8873719; RAB geranylgeranylation.
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 Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 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
