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YPT10_YEAST
ID   YPT10_YEAST             Reviewed;         199 AA.
AC   P38146; D6VQR1;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 2.
DT   03-AUG-2022, entry version 181.
DE   RecName: Full=GTP-binding protein YPT10;
GN   Name=YPT10; OrderedLocusNames=YBR264C; ORFNames=YBR1733;
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].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8465606; DOI=10.1002/yea.320090210;
RA   Doignon F., Biteau N., Crouzet M., Aigle M.;
RT   "The complete sequence of a 19,482 bp segment located on the right arm of
RT   chromosome II from Saccharomyces cerevisiae.";
RL   Yeast 9:189-199(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [3]
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   [4]
RP   FUNCTION, AND INTERACTION WITH GDI1.
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, which
RT   encodes a new yeast Ypt that is degraded by a proteasome-dependent
RT   mechanism.";
RL   Mol. Gen. Genet. 261:589-600(1999).
RN   [5]
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   [6]
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   [7]
RP   IDENTIFICATION OF PROBABLE INITIATION SITE.
RX   PubMed=12748633; DOI=10.1038/nature01644;
RA   Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT   "Sequencing and comparison of yeast species to identify genes and
RT   regulatory elements.";
RL   Nature 423:241-254(2003).
RN   [8]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   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   [9]
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   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: Protein transport. Probably involved in vesicular traffic (By
CC       similarity). Specifically binds guanine nucleotides. {ECO:0000250,
CC       ECO:0000269|PubMed:10394895}.
CC   -!- SUBUNIT: Via its C-terminal end interacts with the Rab GDP dissociation
CC       inhibitor (RabGDI). Interacts with YIF1, YIP3, YIP4 and YIP5.
CC       {ECO:0000269|PubMed:10394895, ECO:0000269|PubMed:11785952,
CC       ECO:0000269|PubMed:11943201}.
CC   -!- INTERACTION:
CC       P38146; P39958: GDI1; NbExp=6; IntAct=EBI-29357, EBI-7517;
CC       P38146; P32864: MRS6; NbExp=3; IntAct=EBI-29357, EBI-14799;
CC       P38146; P53845: YIF1; NbExp=2; IntAct=EBI-29357, EBI-28230;
CC       P38146; P53633: YIP3; NbExp=2; IntAct=EBI-29357, EBI-25301;
CC       P38146; P53093: YIP4; NbExp=2; IntAct=EBI-29357, EBI-24124;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 1360 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   -!- SEQUENCE CAUTION:
CC       Sequence=CAA49929.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAA85227.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X70529; CAA49929.1; ALT_INIT; Genomic_DNA.
DR   EMBL; Z36133; CAA85227.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BK006936; DAA07381.1; -; Genomic_DNA.
DR   PIR; S32965; S32965.
DR   RefSeq; NP_009823.2; NM_001178612.1.
DR   AlphaFoldDB; P38146; -.
DR   SMR; P38146; -.
DR   BioGRID; 32960; 61.
DR   DIP; DIP-4954N; -.
DR   IntAct; P38146; 14.
DR   MINT; P38146; -.
DR   STRING; 4932.YBR264C; -.
DR   iPTMnet; P38146; -.
DR   MaxQB; P38146; -.
DR   PaxDb; P38146; -.
DR   PRIDE; P38146; -.
DR   EnsemblFungi; YBR264C_mRNA; YBR264C; YBR264C.
DR   GeneID; 852567; -.
DR   KEGG; sce:YBR264C; -.
DR   SGD; S000000468; YPT10.
DR   VEuPathDB; FungiDB:YBR264C; -.
DR   eggNOG; KOG0092; Eukaryota.
DR   GeneTree; ENSGT00940000176536; -.
DR   HOGENOM; CLU_041217_10_2_1; -.
DR   InParanoid; P38146; -.
DR   OMA; MYYRDAN; -.
DR   BioCyc; YEAST:G3O-29187-MON; -.
DR   PRO; PR:P38146; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P38146; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR   GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR   GO; GO:0005768; C:endosome; IBA:GO_Central.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0019001; F:guanyl nucleotide binding; IDA:SGD.
DR   GO; GO:0007030; P:Golgi organization; IMP:SGD.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
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   Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..199
FT                   /note="GTP-binding protein YPT10"
FT                   /id="PRO_0000121321"
FT   BINDING         11..18
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         65..69
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         122..125
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         199
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250|UniProtKB:P36586"
FT   LIPID           197
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P36586"
FT   LIPID           199
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P36586"
SQ   SEQUENCE   199 AA;  21834 MW;  EE66719A8C65AA54 CRC64;
     MEATIKVVLL GDSSVGKTSI VTRLKSGKFL AKHAATIGAA FITKTIEVPS NDSSTEKRIH
     MEIWDTAGQE RYKSLVPMYY RDANIALIVF ELGDVSSLQC AKTWFQDLQD RAQGTQVIIV
     GNKYDLVCEE HSGEVTIPAE LQGLPYVAVS AKTGYNFDTL NKIIISLVPE SQFKTLSKNN
     EQGNILEINK KKSGSGCIC
 
 
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