MIC60_YEAST
ID MIC60_YEAST Reviewed; 540 AA.
AC P36112; D6VX81;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=MICOS complex subunit MIC60;
DE AltName: Full=Altered inheritance of mitochondria protein 28;
DE AltName: Full=Formation of crista junctions protein 1;
DE AltName: Full=Found in mitochondrial proteome protein 13;
DE AltName: Full=Mitofilin;
DE Flags: Precursor;
GN Name=MIC60; Synonyms=AIM28, FCJ1, FMP13; OrderedLocusNames=YKR016W;
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=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=19528297; DOI=10.1083/jcb.200811099;
RA Rabl R., Soubannier V., Scholz R., Vogel F., Mendl N.,
RA Vasiljev-Neumeyer A., Korner C., Jagasia R., Keil T., Baumeister W.,
RA Cyrklaff M., Neupert W., Reichert A.S.;
RT "Formation of cristae and crista junctions in mitochondria depends on
RT antagonism between Fcj1 and Su e/g.";
RL J. Cell Biol. 185:1047-1063(2009).
RN [6]
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 [7]
RP FUNCTION, INTERACTION WITH MIA40; TOM22 AND TOM40, COMPOSITION OF THE MICOS
RP COMPLEX, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21944719; DOI=10.1016/j.devcel.2011.08.026;
RA von der Malsburg K., Muller J.M., Bohnert M., Oeljeklaus S.,
RA Kwiatkowska P., Becker T., Loniewska-Lwowska A., Wiese S., Rao S.,
RA Milenkovic D., Hutu D.P., Zerbes R.M., Schulze-Specking A., Meyer H.E.,
RA Martinou J.C., Rospert S., Rehling P., Meisinger C., Veenhuis M.,
RA Warscheid B., van der Klei I.J., Pfanner N., Chacinska A., van der Laan M.;
RT "Dual role of mitofilin in mitochondrial membrane organization and protein
RT biogenesis.";
RL Dev. Cell 21:694-707(2011).
RN [8]
RP IDENTIFICATION IN THE MICOS COMPLEX, AND MASS SPECTROMETRY.
RX PubMed=22009199; DOI=10.1038/emboj.2011.379;
RA Harner M., Korner C., Walther D., Mokranjac D., Kaesmacher J., Welsch U.,
RA Griffith J., Mann M., Reggiori F., Neupert W.;
RT "The mitochondrial contact site complex, a determinant of mitochondrial
RT architecture.";
RL EMBO J. 30:4356-4370(2011).
RN [9]
RP FUNCTION, COMPOSITION OF THE MICOS COMPLEX, INTERACTION WITH OM45 AND POR1,
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21987634; DOI=10.1083/jcb.201107053;
RA Hoppins S., Collins S.R., Cassidy-Stone A., Hummel E., Devay R.M.,
RA Lackner L.L., Westermann B., Schuldiner M., Weissman J.S., Nunnari J.;
RT "A mitochondrial-focused genetic interaction map reveals a scaffold-like
RT complex required for inner membrane organization in mitochondria.";
RL J. Cell Biol. 195:323-340(2011).
RN [10]
RP NOMENCLATURE.
RX PubMed=24687277; DOI=10.1083/jcb.201401006;
RA Pfanner N., van der Laan M., Amati P., Capaldi R.A., Caudy A.A.,
RA Chacinska A., Darshi M., Deckers M., Hoppins S., Icho T., Jakobs S., Ji J.,
RA Kozjak-Pavlovic V., Meisinger C., Odgren P.R., Park S.K., Rehling P.,
RA Reichert A.S., Sheikh M.S., Taylor S.S., Tsuchida N., van der Bliek A.M.,
RA van der Klei I.J., Weissman J.S., Westermann B., Zha J., Neupert W.,
RA Nunnari J.;
RT "Uniform nomenclature for the mitochondrial contact site and cristae
RT organizing system.";
RL J. Cell Biol. 204:1083-1086(2014).
CC -!- FUNCTION: Component of the MICOS complex, a large protein complex of
CC the mitochondrial inner membrane that plays crucial roles in the
CC maintenance of crista junctions, inner membrane architecture, and
CC formation of contact sites to the outer membrane. Plays a role in
CC keeping cristae membranes connected to the inner boundary membrane.
CC Also promotes protein import via the mitochondrial intermembrane space
CC assembly (MIA) pathway. {ECO:0000269|PubMed:19528297,
CC ECO:0000269|PubMed:21944719, ECO:0000269|PubMed:21987634}.
CC -!- SUBUNIT: Component of the mitochondrial contact site and cristae
CC organizing system (MICOS) complex, composed of at least MIC10, MIC12,
CC MIC19, MIC26, MIC27 and MIC60. This complex was also known under the
CC names MINOS or MitOS complex. Interacts with TOM22 and TOM40 in a
CC MICOS-independent manner, resulting in coupling with the outer
CC membrane. Interacts with MIA40, OM45 and POR1.
CC {ECO:0000269|PubMed:21944719, ECO:0000269|PubMed:21987634,
CC ECO:0000269|PubMed:22009199}.
CC -!- INTERACTION:
CC P36112; P43594: MIC19; NbExp=5; IntAct=EBI-27078, EBI-22936;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:19528297,
CC ECO:0000269|PubMed:21944719, ECO:0000269|PubMed:21987634}; Single-pass
CC membrane protein {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:19528297, ECO:0000269|PubMed:21944719,
CC ECO:0000269|PubMed:21987634}. Note=Enriched at crista junctions.
CC -!- DISRUPTION PHENOTYPE: Increases frequency of mitochondrial genome loss
CC and leads to altered mitochondrial morphology. Moderately reduces
CC mitochondrial membrane potential and import efficiency of preproteins
CC that are transported into or across the inner membrane via TIM23
CC complex. Impairs precursor protein import via the MIA pathway. 60-70%
CC of mitochondria exhibit an increased inner membrane surface and stacks
CC of lamellar cristae disconnected from the inner boundary membrane.
CC {ECO:0000269|PubMed:19300474, ECO:0000269|PubMed:21944719,
CC ECO:0000269|PubMed:21987634}.
CC -!- MISCELLANEOUS: Present with 5730 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MICOS complex subunit Mic60 family.
CC {ECO:0000305}.
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DR EMBL; Z28241; CAA82088.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09171.1; -; Genomic_DNA.
DR PIR; S38085; S38085.
DR RefSeq; NP_012941.1; NM_001179806.1.
DR AlphaFoldDB; P36112; -.
DR SMR; P36112; -.
DR BioGRID; 34148; 394.
DR ComplexPortal; CPX-140; MICOS mitochondrial contact site and cristae organizing system complex.
DR DIP; DIP-4644N; -.
DR IntAct; P36112; 6.
DR MINT; P36112; -.
DR STRING; 4932.YKR016W; -.
DR TCDB; 9.B.216.1.1; the micos complex component, mic60 (mic60) family.
DR MaxQB; P36112; -.
DR PaxDb; P36112; -.
DR PRIDE; P36112; -.
DR EnsemblFungi; YKR016W_mRNA; YKR016W; YKR016W.
DR GeneID; 853886; -.
DR KEGG; sce:YKR016W; -.
DR SGD; S000001724; MIC60.
DR VEuPathDB; FungiDB:YKR016W; -.
DR eggNOG; KOG1854; Eukaryota.
DR GeneTree; ENSGT00390000002313; -.
DR HOGENOM; CLU_008024_2_0_1; -.
DR InParanoid; P36112; -.
DR OMA; LQGWAKV; -.
DR BioCyc; YEAST:G3O-31992-MON; -.
DR PRO; PR:P36112; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36112; protein.
DR GO; GO:0061617; C:MICOS complex; IDA:SGD.
DR GO; GO:0030061; C:mitochondrial crista; IDA:SGD.
DR GO; GO:0044284; C:mitochondrial crista junction; IDA:SGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:ComplexPortal.
DR GO; GO:0042407; P:cristae formation; IMP:SGD.
DR GO; GO:0045041; P:protein import into mitochondrial intermembrane space; IMP:SGD.
DR InterPro; IPR019133; Mt-IM_prot_Mitofilin.
DR PANTHER; PTHR15415; PTHR15415; 2.
DR Pfam; PF09731; Mitofilin; 3.
PE 1: Evidence at protein level;
KW Coiled coil; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix.
FT TRANSIT 1..17
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 18..540
FT /note="MICOS complex subunit MIC60"
FT /id="PRO_0000203197"
FT TOPO_DOM 18..37
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..540
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT COILED 173..268
FT /evidence="ECO:0000255"
SQ SEQUENCE 540 AA; 61082 MW; FD8715B29DB52507 CRC64;
MMLRTTASRK IVLRRGLASI NTGTTVASKK ASHKFRNTLW TIALSATAFY AGGIIYSQKN
DKFGDFFSNN VPFAEDLLET YEHYHDRPTL FLEDSWDGLK AKSNDLLSGL TGSSQTRRSN
RENIEVKKIL SLEPLNIETE NSDPQLKEII GSLNDLINSL NDSNLSIPES EFNSIKKSNQ
NMLTNLSQLN ETLKEALSNY MIQRTSEVIT ELNTQYENSK REFEKNLQKN LLQEVDEFKE
NLTKQKDKEL EEKLKANEEL LQAKHANEVG LLSITQVKEF NKIIKDKIEK ERNGRLAHLE
EINSEVNDLS KSIDRSSKIL SKNEALVQLT FQVDEIKSRI NNNNLPDVNI DKELSRLKLL
SNLLSTFNKK SCCDDGDCCS CKKGNKNEGK EGKISCKCKP KTNPPSLLSV ALDELESTCS
GKKILSNEQI YNRWNLLADD FKTASLLPPN SGILGQLTAK VFSLFLFTKT GNPSNATDFD
SVYARVGDNL RVSNLNDAVE EVVSLKGWPH KVCESWIEDA RRKLEVQRLV EILDCEIRTL
