MIC12_YEAST
ID MIC12_YEAST Reviewed; 106 AA.
AC P38341; D6VQQ9;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=MICOS complex subunit MIC12;
DE AltName: Full=Altered inheritance of mitochondria protein 5, mitochondrial;
DE AltName: Full=Found in mitochondrial proteome protein 51;
DE AltName: Full=Mitochondrial contact site complex 12 kDa subunit;
GN Name=MIC12; Synonyms=AIM5, FMP51, MCS12; OrderedLocusNames=YBR262C;
GN ORFNames=YBR1731;
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=ATCC 204508 / S288c;
RX PubMed=8465606; DOI=10.1002/yea.320090210;
RA Doignon F., Biteau N., Crouzet M., Aigle M.;
RT "The complete sequence of a 19,482 bp segment located on the right arm of
RT chromosome II from Saccharomyces cerevisiae.";
RL Yeast 9:189-199(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
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 [6]
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 [7]
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 [8]
RP FUNCTION, COMPOSITION OF THE MICOS COMPLEX, SUBCELLULAR LOCATION, AND
RP 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 [9]
RP IDENTIFICATION IN THE MICOS COMPLEX, MASS SPECTROMETRY, SUBCELLULAR
RP LOCATION, AND TOPOLOGY.
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 [10]
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
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.
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 OM45 and POR1.
CC {ECO:0000269|PubMed:21987634, ECO:0000269|PubMed:22009199}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305};
CC Single-pass membrane protein {ECO:0000305}. Note=Enriched at crista
CC junctions. {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:21944719,
CC ECO:0000269|PubMed:21987634, ECO:0000269|PubMed:22009199}.
CC -!- DISRUPTION PHENOTYPE: Increases frequency of mitochondrial genome loss.
CC Partially altered shape of the mitochondrial network with condensed,
CC fragmented mitochondria accumulating at the periphery of cells. 20-40%
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 2550 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MICOS complex subunit Mic12 family.
CC {ECO:0000305}.
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DR EMBL; X70529; CAA49928.1; -; Genomic_DNA.
DR EMBL; Z36131; CAA85225.1; -; Genomic_DNA.
DR EMBL; AY558435; AAS56761.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07379.1; -; Genomic_DNA.
DR PIR; S32964; S32964.
DR RefSeq; NP_009821.3; NM_001178610.3.
DR AlphaFoldDB; P38341; -.
DR SMR; P38341; -.
DR BioGRID; 32959; 213.
DR ComplexPortal; CPX-140; MICOS mitochondrial contact site and cristae organizing system complex.
DR DIP; DIP-4886N; -.
DR IntAct; P38341; 5.
DR MINT; P38341; -.
DR STRING; 4932.YBR262C; -.
DR MaxQB; P38341; -.
DR PaxDb; P38341; -.
DR PRIDE; P38341; -.
DR EnsemblFungi; YBR262C_mRNA; YBR262C; YBR262C.
DR GeneID; 852566; -.
DR KEGG; sce:YBR262C; -.
DR SGD; S000000466; MIC12.
DR VEuPathDB; FungiDB:YBR262C; -.
DR HOGENOM; CLU_164154_0_0_1; -.
DR InParanoid; P38341; -.
DR OMA; MKDIWNE; -.
DR BioCyc; YEAST:G3O-29186-MON; -.
DR PRO; PR:P38341; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38341; protein.
DR GO; GO:0061617; C:MICOS complex; IDA:SGD.
DR GO; GO:0044284; C:mitochondrial crista junction; IDA:SGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:ComplexPortal.
DR GO; GO:0042407; P:cristae formation; IMP:SGD.
DR GO; GO:0065003; P:protein-containing complex assembly; IMP:SGD.
DR InterPro; IPR031463; Mic12.
DR Pfam; PF17050; AIM5; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..106
FT /note="MICOS complex subunit MIC12"
FT /id="PRO_0000202527"
FT TOPO_DOM 1..10
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..106
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
SQ SEQUENCE 106 AA; 12388 MW; 357863592C1E92CF CRC64;
MSKLGPLARS VKWTLSVGVI GSVFYLYRYS NNGYFYDHDA TWLKQDHQVQ DLVDRKEVVP
GETRNRKLVV TDDGTAWSRT MGESIKDIWN EQIRNSVDWI YSWGKN
