ID   MGR3_YEAST              Reviewed;         501 AA.
AC   Q04472; D6VZT8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=Mitochondrial inner membrane i-AAA protease supercomplex subunit MGR3;
DE   AltName: Full=Mitochondrial genome-required protein 3;
GN   Name=MGR3; Synonyms=FMP24; OrderedLocusNames=YMR115W;
GN   ORFNames=YM9718.14;
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=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(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   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   [4]
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   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 76625 / YPH499;
RX   PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA   Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA   Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA   Pfanner N., Meisinger C.;
RT   "The proteome of Saccharomyces cerevisiae mitochondria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN   [6]
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
RP   TOPOLOGY.
RX   PubMed=18843051; DOI=10.1091/mbc.e08-01-0103;
RA   Dunn C.D., Tamura Y., Sesaki H., Jensen R.E.;
RT   "Mgr3p and Mgr1p are adaptors for the mitochondrial i-AAA protease
RT   complex.";
RL   Mol. Biol. Cell 19:5387-5397(2008).
CC   -!- FUNCTION: Component of the mitochondrial inner membrane i-AAA protease
CC       supercomplex, which degrades misfolded mitochondrial proteins. Together
CC       with MGR1, functions in an adapter complex that targets substrates to
CC       the i-AAA protease for degradation. Required for growth of cells
CC       lacking the mitochondrial genome. {ECO:0000269|PubMed:18843051}.
CC   -!- SUBUNIT: Component of the mitochondrial inner membrane i-AAA protease
CC       supercomplex composed of MGR1, MGR3 and YME1. With MGR1, forms a
CC       subcomplex that binds to YME1 and to substrates to facilitate
CC       proteolysis. {ECO:0000269|PubMed:18843051}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305};
CC       Single-pass membrane protein {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Reduces proteolysis by YME1.
CC       {ECO:0000269|PubMed:18843051}.
CC   -!- MISCELLANEOUS: Present with 8970 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the MGR3 family. {ECO:0000305}.
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DR   EMBL; Z49702; CAA89752.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10012.1; -; Genomic_DNA.
DR   PIR; S54576; S54576.
DR   RefSeq; NP_013833.1; NM_001182615.1.
DR   AlphaFoldDB; Q04472; -.
DR   SMR; Q04472; -.
DR   BioGRID; 35291; 210.
DR   ComplexPortal; CPX-1655; i-AAA complex.
DR   DIP; DIP-7624N; -.
DR   IntAct; Q04472; 2.
DR   STRING; 4932.YMR115W; -.
DR   MaxQB; Q04472; -.
DR   PaxDb; 4932-YMR115W; -.
DR   PeptideAtlas; Q04472; -.
DR   EnsemblFungi; YMR115W_mRNA; YMR115W; YMR115W.
DR   GeneID; 855142; -.
DR   KEGG; sce:YMR115W; -.
DR   AGR; SGD:S000004721; -.
DR   SGD; S000004721; MGR3.
DR   VEuPathDB; FungiDB:YMR115W; -.
DR   eggNOG; ENOG502QU02; Eukaryota.
DR   GeneTree; ENSGT00940000176771; -.
DR   HOGENOM; CLU_039436_0_0_1; -.
DR   InParanoid; Q04472; -.
DR   OMA; CKMTTVE; -.
DR   OrthoDB; 1981313at2759; -.
DR   BioCyc; YEAST:G3O-32810-MONOMER; -.
DR   BioGRID-ORCS; 855142; 3 hits in 10 CRISPR screens.
DR   PRO; PR:Q04472; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q04472; Protein.
DR   GO; GO:0031942; C:i-AAA complex; IDA:SGD.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0051787; F:misfolded protein binding; IDA:SGD.
DR   GO; GO:0030163; P:protein catabolic process; IMP:ComplexPortal.
DR   GO; GO:0045041; P:protein import into mitochondrial intermembrane space; NAS:ComplexPortal.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IMP:SGD.
DR   InterPro; IPR040201; Mrg3-like.
DR   PANTHER; PTHR28142; MITOCHONDRIAL INNER MEMBRANE I-AAA PROTEASE SUPERCOMPLEX SUBUNIT MGR3-RELATED; 1.
DR   PANTHER; PTHR28142:SF1; MITOCHONDRIAL INNER MEMBRANE I-AAA PROTEASE SUPERCOMPLEX SUBUNIT MGR3-RELATED; 1.
PE   1: Evidence at protein level;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Repeat; TPR repeat; Transmembrane; Transmembrane helix.
FT   CHAIN           1..501
FT                   /note="Mitochondrial inner membrane i-AAA protease
FT                   supercomplex subunit MGR3"
FT                   /id="PRO_0000203293"
FT   TOPO_DOM        1..77
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000269|PubMed:18843051"
FT   TRANSMEM        78..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        96..501
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000269|PubMed:18843051"
FT   REPEAT          109..144
FT                   /note="TPR 1"
FT   REPEAT          154..187
FT                   /note="TPR 2"
FT   REPEAT          386..420
FT                   /note="TPR 3"
FT   REPEAT          440..473
FT                   /note="TPR 4"
FT   REGION          38..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   501 AA;  58004 MW;  994613B288C8DB7C CRC64;
     MLLQGMRLSQ RLHKRHLFAS KILTWTTNPA HIRHLHDIRP PASNFNTQES APIPESPANS
     PTRPQMAPKP NLKKKNRSLM YSIIGVSIVG LYFWFKSNSR KQKLPLSAQK VWKEAIWQES
     DKMDFNYKEA LRRYIEALDE CDRSHVDLLS DDYTRIELKI AEMYEKLNML EEAQNLYQEL
     LSRFFEALNV PGKVDESERG EVLRKDLRIL IKSLEINKDI ESGKRKLLQH LLLAQEEILS
     KSPELKEFFE NRKKKLSMVK DINRDPNDDF KTFVSEENIK FDEQGYMILD LEKNSSAWEP
     FKEEFFTARD LYTAYCLSSK DIAAALSCKI TSVEWMVMAD MPPGQILLSQ ANLGSLFYLQ
     AEKLEADLNQ LEQKKSKESN QELDMGTYIK AVRFVRKNRD LCLERAQKCY DSVIAFAKRN
     RKIRFHVKDQ LDPSIAQSIA LSTYGMGVLS LHEGVLAKAE KLFKDSITMA KETEFNELLA
     EAEKELEKTT VLKAAKKEGL N
//