MGR3_YEAST
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 03-AUG-2022, entry version 136.
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; 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 205.
DR ComplexPortal; CPX-1655; i-AAA complex.
DR DIP; DIP-7624N; -.
DR IntAct; Q04472; 2.
DR STRING; 4932.YMR115W; -.
DR MaxQB; Q04472; -.
DR PaxDb; Q04472; -.
DR PRIDE; Q04472; -.
DR EnsemblFungi; YMR115W_mRNA; YMR115W; YMR115W.
DR GeneID; 855142; -.
DR KEGG; sce:YMR115W; -.
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 BioCyc; YEAST:G3O-32810-MON; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IC: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; PTHR28142; 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
