YPT52_YEAST
ID YPT52_YEAST Reviewed; 234 AA.
AC P36018; D6VX79;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=GTP-binding protein YPT52;
GN Name=YPT52; OrderedLocusNames=YKR014C; ORFNames=YK112;
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=8163546; DOI=10.1083/jcb.125.2.283;
RA Singer-Krueger B., Stenmark H., Duesterhoeft A., Philippsen P., Yoo J.-S.,
RA Gallwitz D., Zerial M.;
RT "Role of three rab5-like GTPases, Ypt51p, Ypt52p, and Ypt53p, in the
RT endocytic and vacuolar protein sorting pathways of yeast.";
RL J. Cell Biol. 125:283-298(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(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 PROTEIN SEQUENCE OF 1-8, AND ASSOCIATION WITH SED5 VESICLES.
RX PubMed=10713261; DOI=10.1016/s0014-5793(00)01268-0;
RA Cho J.-H., Noda Y., Yoda K.;
RT "Proteins in the early Golgi compartment of Saccharomyces cerevisiae
RT immunoisolated by Sed5p.";
RL FEBS Lett. 469:151-154(2000).
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 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 AND SER-142, AND
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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ROY1.
RX PubMed=21389113; DOI=10.1091/mbc.e10-08-0716;
RA Liu Y., Nakatsukasa K., Kotera M., Kanada A., Nishimura T., Kishi T.,
RA Mimura S., Kamura T.;
RT "Non-SCF-type F-box protein Roy1/Ymr258c interacts with a Rab5-like GTPase
RT Ypt52 and inhibits Ypt52 function.";
RL Mol. Biol. Cell 22:1575-1584(2011).
RN [10]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-151, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Required for transport in the endocytic pathway and for
CC correct sorting of the vacuolar hydrolases suggesting a possible
CC intersection of the endocytic with the vacuolar sorting pathway.
CC {ECO:0000269|PubMed:21389113}.
CC -!- SUBUNIT: Interacts with ROY1, YIF1, YIP3, YIP4 and YIP5.
CC {ECO:0000269|PubMed:11785952, ECO:0000269|PubMed:11943201,
CC ECO:0000269|PubMed:21389113}.
CC -!- INTERACTION:
CC P36018; P39958: GDI1; NbExp=3; IntAct=EBI-29407, EBI-7517;
CC P36018; P32864: MRS6; NbExp=3; IntAct=EBI-29407, EBI-14799;
CC P36018; Q04847: ROY1; NbExp=3; IntAct=EBI-29407, EBI-27556;
CC P36018; P53633: YIP3; NbExp=2; IntAct=EBI-29407, EBI-25301;
CC P36018; P53093: YIP4; NbExp=2; IntAct=EBI-29407, EBI-24124;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:21389113}. Note=Also found in association with
CC endoplasmic reticulum vesicles having SED5 on their surface.
CC -!- MISCELLANEOUS: Present with 9380 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; X76174; CAA53770.1; -; Genomic_DNA.
DR EMBL; Z28239; CAA82086.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09169.1; -; Genomic_DNA.
DR PIR; S38083; S38083.
DR RefSeq; NP_012939.1; NM_001179804.1.
DR AlphaFoldDB; P36018; -.
DR SMR; P36018; -.
DR BioGRID; 34146; 119.
DR DIP; DIP-2121N; -.
DR IntAct; P36018; 18.
DR MINT; P36018; -.
DR STRING; 4932.YKR014C; -.
DR iPTMnet; P36018; -.
DR MaxQB; P36018; -.
DR PaxDb; P36018; -.
DR PRIDE; P36018; -.
DR EnsemblFungi; YKR014C_mRNA; YKR014C; YKR014C.
DR GeneID; 853884; -.
DR KEGG; sce:YKR014C; -.
DR SGD; S000001722; YPT52.
DR VEuPathDB; FungiDB:YKR014C; -.
DR eggNOG; KOG0092; Eukaryota.
DR GeneTree; ENSGT00940000176536; -.
DR HOGENOM; CLU_041217_10_2_1; -.
DR InParanoid; P36018; -.
DR OMA; AVHFDIW; -.
DR BioCyc; YEAST:G3O-31990-MON; -.
DR PRO; PR:P36018; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36018; protein.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR GO; GO:0005770; C:late endosome; IMP: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; IDA:SGD.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:0006895; P:Golgi to endosome transport; IMP:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IGI:SGD.
DR GO; GO:0036258; P:multivesicular body assembly; IGI:SGD.
DR GO; GO:0036010; P:protein localization to endosome; IGI:SGD.
DR GO; GO:0006623; P:protein targeting to vacuole; 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 Cell membrane; Direct protein sequencing; Endoplasmic reticulum;
KW GTP-binding; Isopeptide bond; Lipoprotein; Membrane; Nucleotide-binding;
KW Phosphoprotein; Prenylation; Protein transport; Reference proteome;
KW Transport; Ubl conjugation.
FT CHAIN 1..234
FT /note="GTP-binding protein YPT52"
FT /id="PRO_0000121326"
FT REGION 131..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 66..70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 111..114
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT LIPID 232
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 233
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT CROSSLNK 151
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 234 AA; 26132 MW; 34AB2FFE38697261 CRC64;
MLQFKLVLLG DSSVGKSSIV HRFVKDTFDE LRESTIGAAF LSQSITIHPN DGNETKDVVI
KFEIWDTAGQ ERYKSLAPMY YRNANAALVV YDITQEDSLQ KARNWVDELK NKVGDDDLVI
YLLGNKVDLC QETPSTETSP DSNEGGDEEQ KVRAISTEEA KQYAQEQGLL FREVSAKTGE
GVKEIFQDIG EKLYDLKKDE ILSKQNRQIG GGNNGQVDIN LQRPSTNDPT SCCS
