UPS3_YEAST
ID UPS3_YEAST Reviewed; 179 AA.
AC Q04006; D6VSG9;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Protein UPS3, mitochondrial;
DE AltName: Full=Genetic interactor of prohibitins protein 2;
DE AltName: Full=Unprocessed MGM1 protein 3;
GN Name=UPS3; Synonyms=GEP2; OrderedLocusNames=YDR185C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
RP FUNCTION.
RX PubMed=19221197; DOI=10.1083/jcb.200810189;
RA Osman C., Haag M., Potting C., Rodenfels J., Dip P.V., Wieland F.T.,
RA Brugger B., Westermann B., Langer T.;
RT "The genetic interactome of prohibitins: coordinated control of cardiolipin
RT and phosphatidylethanolamine by conserved regulators in mitochondria.";
RL J. Cell Biol. 184:583-596(2009).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19506038; DOI=10.1083/jcb.200812018;
RA Tamura Y., Endo T., Iijima M., Sesaki H.;
RT "Ups1p and Ups2p antagonistically regulate cardiolipin metabolism in
RT mitochondria.";
RL J. Cell Biol. 185:1029-1045(2009).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION MDM35.
RX PubMed=20622808; DOI=10.1038/emboj.2010.149;
RA Tamura Y., Iijima M., Sesaki H.;
RT "Mdm35p imports Ups proteins into the mitochondrial intermembrane space by
RT functional complex formation.";
RL EMBO J. 29:2875-2887(2010).
CC -!- FUNCTION: Required for mitochondrial morphology. With UPS1 and UPS2,
CC controls phospholipid metabolism in the mitochondrial intermembrane
CC space. {ECO:0000269|PubMed:19221197, ECO:0000269|PubMed:19506038}.
CC -!- SUBUNIT: Interacts with MDM35. {ECO:0000269|PubMed:20622808}.
CC -!- INTERACTION:
CC Q04006; O60200: MDM35; NbExp=3; IntAct=EBI-3830982, EBI-2080774;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral membrane
CC protein; Intermembrane side. Mitochondrion intermembrane space.
CC Note=Lacks the two major intermembrane space-targeting signals,
CC bipartite presequences and cysteine motifs, and import is mediated by
CC another IMS protein, MDM35.
CC -!- MISCELLANEOUS: Present with 672 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the slowmo family. {ECO:0000305}.
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DR EMBL; Z46727; CAA86692.1; -; Genomic_DNA.
DR EMBL; AY557670; AAS55996.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12029.1; -; Genomic_DNA.
DR PIR; S49782; S49782.
DR RefSeq; NP_010471.1; NM_001180493.1.
DR AlphaFoldDB; Q04006; -.
DR SMR; Q04006; -.
DR BioGRID; 32239; 20.
DR IntAct; Q04006; 1.
DR MINT; Q04006; -.
DR STRING; 4932.YDR185C; -.
DR PaxDb; Q04006; -.
DR PRIDE; Q04006; -.
DR EnsemblFungi; YDR185C_mRNA; YDR185C; YDR185C.
DR GeneID; 851766; -.
DR KEGG; sce:YDR185C; -.
DR SGD; S000002593; UPS3.
DR VEuPathDB; FungiDB:YDR185C; -.
DR eggNOG; KOG3336; Eukaryota.
DR GeneTree; ENSGT00950000182810; -.
DR HOGENOM; CLU_067902_1_1_1; -.
DR InParanoid; Q04006; -.
DR OMA; DPAEKKM; -.
DR BioCyc; YEAST:G3O-29774-MON; -.
DR Reactome; R-SCE-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
DR PRO; PR:Q04006; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04006; protein.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:1990050; F:phosphatidic acid transfer activity; IBA:GO_Central.
DR GO; GO:0070584; P:mitochondrion morphogenesis; IMP:SGD.
DR GO; GO:0015914; P:phospholipid transport; IBA:GO_Central.
DR InterPro; IPR006797; PRELI/MSF1_dom.
DR InterPro; IPR037365; Slowmo/Ups.
DR PANTHER; PTHR11158; PTHR11158; 1.
DR Pfam; PF04707; PRELI; 1.
DR PROSITE; PS50904; PRELI_MSF1; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome.
FT CHAIN 1..179
FT /note="Protein UPS3, mitochondrial"
FT /id="PRO_0000253834"
FT DOMAIN 1..175
FT /note="PRELI/MSF1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00158"
SQ SEQUENCE 179 AA; 20921 MW; CD21C3B53E76808B CRC64;
MKSFQKSYEF DYPWEKVTTA NWMKYPNKIS THVIAVDVLR RELKEHGDVL LTERLITIRQ
NTPHWMSILV GNTNLAYVRE VSTVDRRDRS LTMRSCNMTF PHILKCYETV RYVPHPKNPS
NVTLFKQDAK FLSGVPTKTF SEKVENWGVK RFSDNAVKGK VGFDSILAMF NDIWKNANE
