MGR1_YEAST
ID MGR1_YEAST Reviewed; 417 AA.
AC P25573; D6VQX2;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Mitochondrial inner membrane i-AAA protease supercomplex subunit MGR1;
DE AltName: Full=Mitochondrial genome-required protein 1;
GN Name=MGR1; OrderedLocusNames=YCL044C; ORFNames=YCL314, YCL44C;
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=1523890; DOI=10.1002/yea.320080709;
RA Scherens B., Messenguy F., Gigot D., Dubois E.;
RT "The complete sequence of a 9,543 bp segment on the left arm of chromosome
RT III reveals five open reading frames including glucokinase and the protein
RT disulfide isomerase.";
RL Yeast 8:577-586(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
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 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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH YME1, AND
RP IDENTIFICATION IN THE I-AAA COMPLEX.
RX PubMed=16267274; DOI=10.1091/mbc.e05-06-0585;
RA Dunn C.D., Lee M.S., Spencer F.A., Jensen R.E.;
RT "A genomewide screen for petite-negative yeast strains yields a new subunit
RT of the i-AAA protease complex.";
RL Mol. Biol. Cell 17:213-226(2006).
RN [8]
RP FUNCTION, AND SUBUNIT.
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 required for mitochondrial inner membrane protein
CC turnover. Together with MGR3, functions in an adapter complex that
CC targets substrates to the i-AAA protease for degradation. Required for
CC growth of cells lacking the mitochondrial genome.
CC {ECO:0000269|PubMed:16267274, ECO:0000269|PubMed:18843051}.
CC -!- SUBUNIT: Component of the mitochondrial inner membrane i-AAA protease
CC supercomplex composed of MGR1, MGR3 and YME1. With MGR3, forms a
CC subcomplex that binds to YME1 and to substrates to facilitate
CC proteolysis. Interacts directly with YME1.
CC {ECO:0000269|PubMed:16267274, ECO:0000269|PubMed:18843051}.
CC -!- INTERACTION:
CC P25573; P32795: YME1; NbExp=3; IntAct=EBI-21740, EBI-27785;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278,
CC ECO:0000269|PubMed:16267274}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278,
CC ECO:0000269|PubMed:16267274}.
CC -!- MISCELLANEOUS: Present with 3410 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MGR1 family. {ECO:0000305}.
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DR EMBL; X59720; CAA42372.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07441.1; -; Genomic_DNA.
DR PIR; S19373; S19373.
DR RefSeq; NP_009886.1; NM_001178689.1.
DR AlphaFoldDB; P25573; -.
DR BioGRID; 30940; 357.
DR ComplexPortal; CPX-1655; i-AAA complex.
DR DIP; DIP-5031N; -.
DR IntAct; P25573; 2.
DR MINT; P25573; -.
DR STRING; 4932.YCL044C; -.
DR MaxQB; P25573; -.
DR PaxDb; P25573; -.
DR PRIDE; P25573; -.
DR EnsemblFungi; YCL044C_mRNA; YCL044C; YCL044C.
DR GeneID; 850313; -.
DR KEGG; sce:YCL044C; -.
DR SGD; S000000549; MGR1.
DR VEuPathDB; FungiDB:YCL044C; -.
DR eggNOG; ENOG502QR67; Eukaryota.
DR HOGENOM; CLU_039216_0_0_1; -.
DR InParanoid; P25573; -.
DR OMA; FYHEGID; -.
DR BioCyc; YEAST:G3O-29300-MON; -.
DR PRO; PR:P25573; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25573; 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; IC:ComplexPortal.
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; IPR013911; i-AAA_Mgr1.
DR Pfam; PF08602; Mgr1; 2.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..417
FT /note="Mitochondrial inner membrane i-AAA protease
FT supercomplex subunit MGR1"
FT /id="PRO_0000202546"
FT TOPO_DOM 1..56
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:16267274"
FT TRANSMEM 57..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..151
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:16267274"
FT TRANSMEM 152..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..417
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:16267274"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 417 AA; 47156 MW; 39055E8ECF6C3B9B CRC64;
MAVFTPPSGN SNSTDHTHTQ DDHDKDDNDI KKFYIRPSLG LKLWGPLVPA PDNLPGLYTL
ITIQSAVGFF ALWRLRRLYK LPPPRRIATG THSDLSFGEL PSEMIVNGKT KIKKDIADFP
TLNRFSTTHG DIVLAPPPII PRQSRFVSVR KLLWGLFGSL LLSQSLLELT RLNFLKYDPW
CDEMKSVRDK KFFNNIVKYY HEGIDPTKIK VKDAMNGTPL STNIPEVKQS VALARAQVEA
QNPIIKWFGP LEYKPMSFNE YLNRMEFHLD MFEFFQNKRN IRENSIELIN SISHNPQSSS
TGLEGLSESK KLHLQNVEKR LHFLASSGDS ISAPVKKRSS TTLSRGVILP HDTKGPQDID
LDTIRSLYDP WMTLALETSL SIKFIPTTMP SHTKTPTSTD QPLPGPTPKA LTNEKTH
