UPS2_YEAST
ID UPS2_YEAST Reviewed; 230 AA.
AC P35200; D6VYH4;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Protein UPS2, mitochondrial;
DE AltName: Full=Altered inheritance rate of mitochondrion protein 30;
DE AltName: Full=Genetic interactor of prohibitins protein 1;
DE AltName: Full=Unprocessed MGM1 protein 2;
GN Name=UPS2; Synonyms=AIM30, GEP1, MSF1; OrderedLocusNames=YLR168C;
GN ORFNames=L9470.15;
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=SP1;
RX PubMed=8373805; DOI=10.1016/0167-4781(93)90198-m;
RA Nakai M., Takada T., Endo T.;
RT "Cloning of the YAP19 gene encoding a putative yeast homolog of AP19, the
RT mammalian small chain of the clathrin-assembly proteins.";
RL Biochim. Biophys. Acta 1174:282-284(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
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 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, AND SUBCELLULAR LOCATION.
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 DISRUPTION PHENOTYPE.
RX PubMed=19300474; DOI=10.1371/journal.pgen.1000407;
RA Hess D.C., Myers C.L., Huttenhower C., Hibbs M.A., Hayes A.P., Paw J.,
RA Clore J.J., Mendoza R.M., Luis B.S., Nislow C., Giaever G., Costanzo M.,
RA Troyanskaya O.G., Caudy A.A.;
RT "Computationally driven, quantitative experiments discover genes required
RT for mitochondrial biogenesis.";
RL PLoS Genet. 5:E1000407-E1000407(2009).
RN [9]
RP SUBCELLULAR LOCATION, FUNCTION, 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).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH MDM35.
RX PubMed=20657548; DOI=10.1038/emboj.2010.169;
RA Potting C., Wilmes C., Engmann T., Osman C., Langer T.;
RT "Regulation of mitochondrial phospholipids by Ups1/PRELI-like proteins
RT depends on proteolysis and Mdm35.";
RL EMBO J. 29:2888-2898(2010).
CC -!- FUNCTION: Required for mitochondrial cristae morphogenesis and MGM1-
CC processing. Controls the stability of mitochondrial
CC phosphatidylethanolamine (PE). With UPS1, controls the level of
CC cardiolipin in mitochondria. Cardiolipin is a unique phospholipid with
CC four fatty acid chains and is present mainly in the mitochondrial inner
CC membrane where it stabilizes the electron transport chain supercomplex
CC between complexes III and IV through direct interaction of their
CC subunits. {ECO:0000269|PubMed:19221197, ECO:0000269|PubMed:19506038,
CC ECO:0000269|PubMed:20622808}.
CC -!- SUBUNIT: Interacts with MDM35. {ECO:0000269|PubMed:20622808,
CC ECO:0000269|PubMed:20657548}.
CC -!- INTERACTION:
CC P35200; O60200: MDM35; NbExp=5; IntAct=EBI-11337, 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 -!- DISRUPTION PHENOTYPE: Defects in mitochondrial morphology.
CC {ECO:0000269|PubMed:19300474}.
CC -!- MISCELLANEOUS: Present with 2910 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; X70279; CAA49766.1; -; Genomic_DNA.
DR EMBL; U17246; AAB67467.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09490.1; -; Genomic_DNA.
DR PIR; S37758; S37758.
DR RefSeq; NP_013269.1; NM_001182055.1.
DR AlphaFoldDB; P35200; -.
DR SMR; P35200; -.
DR BioGRID; 31441; 152.
DR DIP; DIP-4699N; -.
DR IntAct; P35200; 10.
DR MINT; P35200; -.
DR STRING; 4932.YLR168C; -.
DR PaxDb; P35200; -.
DR PRIDE; P35200; -.
DR DNASU; 850865; -.
DR EnsemblFungi; YLR168C_mRNA; YLR168C; YLR168C.
DR GeneID; 850865; -.
DR KEGG; sce:YLR168C; -.
DR SGD; S000004158; UPS2.
DR VEuPathDB; FungiDB:YLR168C; -.
DR eggNOG; KOG3336; Eukaryota.
DR GeneTree; ENSGT00950000182810; -.
DR HOGENOM; CLU_067902_1_0_1; -.
DR InParanoid; P35200; -.
DR OMA; AMSRRVF; -.
DR BioCyc; YEAST:G3O-32298-MON; -.
DR Reactome; R-SCE-6803204; TP53 Regulates Transcription of Genes Involved in Cytochrome C Release.
DR PRO; PR:P35200; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P35200; 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:0032048; P:cardiolipin metabolic process; IGI:SGD.
DR GO; GO:0042407; P:cristae formation; IMP:SGD.
DR GO; GO:2001246; P:negative regulation of phosphatidylcholine biosynthetic process; IMP:SGD.
DR GO; GO:0046337; P:phosphatidylethanolamine metabolic process; IMP:SGD.
DR GO; GO:0015914; P:phospholipid transport; IDA:SGD.
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..230
FT /note="Protein UPS2, mitochondrial"
FT /id="PRO_0000096596"
FT DOMAIN 1..175
FT /note="PRELI/MSF1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00158"
SQ SEQUENCE 230 AA; 26506 MW; D4A2A5015EFB6570 CRC64;
MKLFQNSYDF NYPWDQVTAA NWKKYPNEIS THVIAVDVLR RELKDQGKVL VTERLITVKQ
GVPKWIMMML GGTNMSHVRE VSVVDLNKKS LTMRSCNLTM CNLLKVYETV TYSPHPDDSA
NKTLFQQEAQ ITAYGSIRKL CNKMEDWSVQ RFCENAKKGK MGFDAVLQVF SENWEKHVDD
LSNQLVSKVN ETMEDVKISA GTLLKGTERS GRTILQQNID LFRDAYNHEN
