MIC10_YEAST
ID MIC10_YEAST Reviewed; 97 AA.
AC Q96VH5; D6VQV9;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=MICOS complex subunit MIC10;
DE AltName: Full=Mitochondrial contact site complex 10 kDa subunit;
DE AltName: Full=Mitochondrial inner membrane organization component of 10 kDa;
DE AltName: Full=Mitochondrial organizing structure protein 1;
DE Short=MitOS1;
GN Name=MIC10; Synonyms=MCS10, MIO10, MOS1; OrderedLocusNames=YCL057C-A;
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=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 [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], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
RN [4]
RP FUNCTION, IDENTIFICATION IN 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 [5]
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 [6]
RP FUNCTION, IDENTIFICATION IN THE MICOS COMPLEX, INTERACTION WITH OM45 AND
RP POR1, 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 [7]
RP FUNCTION, IDENTIFICATION IN THE MICOS COMPLEX, SUBCELLULAR LOCATION, AND
RP TOPOLOGY.
RX PubMed=22114354; DOI=10.1091/mbc.e11-09-0774;
RA Alkhaja A.K., Jans D.C., Nikolov M., Vukotic M., Lytovchenko O.,
RA Ludewig F., Schliebs W., Riedel D., Urlaub H., Jakobs S., Deckers M.;
RT "MINOS1 is a conserved component of mitofilin complexes and required for
RT mitochondrial function and cristae organization.";
RL Mol. Biol. Cell 23:247-257(2012).
RN [8]
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 ECO:0000269|PubMed:22114354}.
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:21944719, ECO:0000269|PubMed:21987634,
CC ECO:0000269|PubMed:22009199, ECO:0000269|PubMed:22114354}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:21944719,
CC ECO:0000269|PubMed:21987634, ECO:0000269|PubMed:22009199,
CC ECO:0000269|PubMed:22114354}; Single-pass membrane protein
CC {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:21944719,
CC ECO:0000269|PubMed:21987634, ECO:0000269|PubMed:22009199,
CC ECO:0000269|PubMed:22114354}. Note=The C-terminus is located in the
CC intermembrane space, while the location of the N-terminus has not been
CC determined yet. As some programs predict the presence of 2 closely
CC apposed membrane domains, it has been proposed that the protein may
CC cross the membrane twice and that both termini may face the
CC intermembrane space (PubMed:22114354). Enriched at crista junctions.
CC {ECO:0000269|PubMed:22114354}.
CC -!- DISRUPTION PHENOTYPE: Partially altered shape of the mitochondrial
CC network with condensed, fragmented mitochondria accumulating at the
CC periphery of cells. 60-70% of mitochondria exhibit an increased inner
CC membrane surface and stacks of lamellar cristae disconnected from the
CC inner boundary membrane. {ECO:0000269|PubMed:21944719,
CC ECO:0000269|PubMed:21987634}.
CC -!- SIMILARITY: Belongs to the MICOS complex subunit Mic10 family.
CC {ECO:0000305}.
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DR EMBL; X59720; CAC42954.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07428.1; -; Genomic_DNA.
DR PIR; S78709; S78709.
DR RefSeq; NP_065435.1; NM_001184448.1.
DR AlphaFoldDB; Q96VH5; -.
DR BioGRID; 30928; 122.
DR ComplexPortal; CPX-140; MICOS mitochondrial contact site and cristae organizing system complex.
DR IntAct; Q96VH5; 9.
DR MINT; Q96VH5; -.
DR STRING; 4932.YCL057C-A; -.
DR TCDB; 8.A.156.1.1; the micos complex (micos-c) family.
DR iPTMnet; Q96VH5; -.
DR MaxQB; Q96VH5; -.
DR PaxDb; Q96VH5; -.
DR PRIDE; Q96VH5; -.
DR EnsemblFungi; YCL057C-A_mRNA; YCL057C-A; YCL057C-A.
DR GeneID; 850300; -.
DR KEGG; sce:YCL057C-A; -.
DR SGD; S000007547; MIC10.
DR VEuPathDB; FungiDB:YCL057C-A; -.
DR eggNOG; KOG4604; Eukaryota.
DR HOGENOM; CLU_068905_3_0_1; -.
DR InParanoid; Q96VH5; -.
DR OMA; DAIFRTN; -.
DR BioCyc; YEAST:G3O-29419-MON; -.
DR PRO; PR:Q96VH5; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; Q96VH5; 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:0061024; P:membrane organization; IDA:SGD.
DR InterPro; IPR007512; Mic10.
DR PANTHER; PTHR21304; PTHR21304; 1.
DR Pfam; PF04418; DUF543; 1.
PE 1: Evidence at protein level;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..97
FT /note="MICOS complex subunit MIC10"
FT /id="PRO_0000221640"
FT TOPO_DOM 1..35
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..97
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 97 AA; 10408 MW; D6C214612BD35E26 CRC64;
MSEQAQTQQP AKSTPSKDSN KNGSSVSTIL DTKWDIVLSN MLVKTAMGFG VGVFTSVLFF
KRRAFPVWLG IGFGVGRGYA EGDAIFRSSA GLRSSKV
