YPT31_YEAST
ID YPT31_YEAST Reviewed; 223 AA.
AC P38555; D3DLT0;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=GTP-binding protein YPT31/YPT8;
DE AltName: Full=Rab GTPase YPT31;
GN Name=YPT31; Synonyms=YPT8; OrderedLocusNames=YER031C;
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].
RX PubMed=8017109; DOI=10.1002/yea.320100313;
RA Lai M.H., Bard M., Kirsch D.R.;
RT "Identification of a gene encoding a new Ypt/Rab-like monomeric G-protein
RT in Saccharomyces cerevisiae.";
RL Yeast 10:399-402(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
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 [3]
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., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [4]
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 [5]
RP PROTEIN SEQUENCE OF 2-32; 44-61; 77-134 AND 143-177, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (MAY-2005) to UniProtKB.
RN [6]
RP FUNCTION, 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 [7]
RP INTERACTION WITH YIP1.
RC STRAIN=HLR3;
RX PubMed=9724632; DOI=10.1093/emboj/17.17.4954;
RA Yang X., Matern H.T., Gallwitz D.;
RT "Specific binding to a novel and essential Golgi membrane protein (Yip1p)
RT functionally links the transport GTPases Ypt1p and Ypt31p.";
RL EMBO J. 17:4954-4963(1998).
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 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 [14]
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 insights
RT into evolution.";
RL Science 325:1682-1686(2009).
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 in the secretory pathway.
CC Probably involved in regulation of secretory vesicle formation at the
CC trans-Golgi compartment. Plays a role in autophagy.
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, YIP1, YIP3, YIP4 and YIP5. Interacts with
CC TRS130. {ECO:0000269|PubMed:11785952, ECO:0000269|PubMed:11943201,
CC ECO:0000269|PubMed:12478387, ECO:0000269|PubMed:9724632}.
CC -!- INTERACTION:
CC P38555; P39958: GDI1; NbExp=5; IntAct=EBI-29379, EBI-7517;
CC P38555; P53845: YIF1; NbExp=3; IntAct=EBI-29379, EBI-28230;
CC P38555; P53633: YIP3; NbExp=3; IntAct=EBI-29379, EBI-25301;
CC P38555; P53093: YIP4; NbExp=2; IntAct=EBI-29379, EBI-24124;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:9151665}; Lipid-anchor
CC {ECO:0000269|PubMed:9151665}.
CC -!- MISCELLANEOUS: Present with 5955 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; L17070; AAA83385.1; -; Genomic_DNA.
DR EMBL; X72833; CAA51354.1; -; Genomic_DNA.
DR EMBL; U18778; AAB64564.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07684.1; -; Genomic_DNA.
DR PIR; S42679; S42679.
DR RefSeq; NP_010948.1; NM_001178922.1.
DR PDB; 3CPJ; X-ray; 2.35 A; B=1-223.
DR PDBsum; 3CPJ; -.
DR AlphaFoldDB; P38555; -.
DR SMR; P38555; -.
DR BioGRID; 36766; 302.
DR DIP; DIP-2022N; -.
DR IntAct; P38555; 19.
DR MINT; P38555; -.
DR STRING; 4932.YER031C; -.
DR iPTMnet; P38555; -.
DR MaxQB; P38555; -.
DR PaxDb; P38555; -.
DR PRIDE; P38555; -.
DR EnsemblFungi; YER031C_mRNA; YER031C; YER031C.
DR GeneID; 856753; -.
DR KEGG; sce:YER031C; -.
DR SGD; S000000833; YPT31.
DR VEuPathDB; FungiDB:YER031C; -.
DR eggNOG; KOG0087; Eukaryota.
DR GeneTree; ENSGT00940000171249; -.
DR HOGENOM; CLU_041217_23_2_1; -.
DR InParanoid; P38555; -.
DR OMA; SMKEDYY; -.
DR BioCyc; YEAST:G3O-30212-MON; -.
DR Reactome; R-SCE-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-SCE-8873719; RAB geranylgeranylation.
DR EvolutionaryTrace; P38555; -.
DR PRO; PR:P38555; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P38555; protein.
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:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
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; Direct protein sequencing;
KW Golgi apparatus; GTP-binding; Lipoprotein; Membrane; Nucleotide-binding;
KW Prenylation; Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5"
FT CHAIN 2..223
FT /note="GTP-binding protein YPT31/YPT8"
FT /id="PRO_0000121323"
FT REGION 185..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 42..50
FT /note="Effector region"
FT /evidence="ECO:0000305"
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:0000269|Ref.5"
FT LIPID 222
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 223
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT STRAND 12..20
FT /evidence="ECO:0007829|PDB:3CPJ"
FT HELIX 26..35
FT /evidence="ECO:0007829|PDB:3CPJ"
FT STRAND 49..57
FT /evidence="ECO:0007829|PDB:3CPJ"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:3CPJ"
FT TURN 70..76
FT /evidence="ECO:0007829|PDB:3CPJ"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:3CPJ"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:3CPJ"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:3CPJ"
FT HELIX 98..114
FT /evidence="ECO:0007829|PDB:3CPJ"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:3CPJ"
FT HELIX 128..133
FT /evidence="ECO:0007829|PDB:3CPJ"
FT HELIX 138..147
FT /evidence="ECO:0007829|PDB:3CPJ"
FT STRAND 151..154
FT /evidence="ECO:0007829|PDB:3CPJ"
FT HELIX 163..174
FT /evidence="ECO:0007829|PDB:3CPJ"
SQ SEQUENCE 223 AA; 24469 MW; EC274E5873138D78 CRC64;
MSSEDYGYDY DLLFKIVLIG DSGVGKSNLL SRFTKNEFNM DSKSTIGVEF ATRTLEIDGK
RIKAQIWDTA GQERYRAITS AYYRGAVGAL IVYDISKSSS YENCNHWLSE LRENADDNVA
VGLIGNKSDL AHLRAVPTEE SKTFAQENQL LFTETSALNS ENVDKAFEEL INTIYQKVSK
HQMDLGDSSA NGNANGASAP NGPTISLTPT PNENKKANGN NCC
