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MIC26_YEAST
ID   MIC26_YEAST             Reviewed;         233 AA.
AC   P50087; D6VV15;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=MICOS subunit MIC26;
DE   AltName: Full=Mitochondrial contact site complex 29 kDa subunit;
DE   AltName: Full=Mitochondrial inner membrane organization component of 27 kDa;
DE   AltName: Full=Mitochondrial organizing structure protein 2;
DE            Short=MitOS2;
GN   Name=MIC26; Synonyms=MCS29, MIO27, MOS2; OrderedLocusNames=YGR235C;
GN   ORFNames=G8575;
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=8701610;
RX   DOI=10.1002/(sici)1097-0061(19960330)12:4<385::aid-yea910>3.0.co;2-g;
RA   van der Aart Q.J.M., Kleine K., Steensma H.Y.;
RT   "Sequence analysis of the 43 kb CRM1-YLM9-PET54-DIE2-SMI1-PHO81-YHB4-PFK1
RT   region from the right arm of Saccharomyces cerevisiae chromosome VII.";
RL   Yeast 12:385-390(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
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   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   FUNCTION, COMPOSITION OF THE MICOS COMPLEX, AND SUBCELLULAR LOCATION.
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   [7]
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   [8]
RP   FUNCTION, COMPOSITION OF THE MICOS COMPLEX, SUBCELLULAR LOCATION, AND
RP   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   [9]
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. {ECO:0000269|PubMed:22009199}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305};
CC       Multi-pass membrane protein {ECO:0000305}. Note=Enriched at crista
CC       junctions. {ECO:0000269|PubMed:21944719, ECO:0000269|PubMed:21987634,
CC       ECO:0000269|PubMed:22009199}.
CC   -!- DISRUPTION PHENOTYPE: Moderate changes in the mitochondrial morphology.
CC       {ECO:0000269|PubMed:21987634}.
CC   -!- MISCELLANEOUS: Present with 5220 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the apolipoprotein O/MICOS complex subunit Mic27
CC       family. Yeast Mic26 subfamily. {ECO:0000305}.
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DR   EMBL; X87941; CAA61185.1; -; Genomic_DNA.
DR   EMBL; Z73020; CAA97263.1; -; Genomic_DNA.
DR   EMBL; AY558276; AAS56602.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08326.1; -; Genomic_DNA.
DR   PIR; S57700; S57700.
DR   RefSeq; NP_011751.1; NM_001181364.1.
DR   AlphaFoldDB; P50087; -.
DR   BioGRID; 33487; 40.
DR   ComplexPortal; CPX-140; MICOS mitochondrial contact site and cristae organizing system complex.
DR   DIP; DIP-4903N; -.
DR   IntAct; P50087; 6.
DR   MINT; P50087; -.
DR   STRING; 4932.YGR235C; -.
DR   TCDB; 8.A.156.2.1; the micos complex (micos-c) family.
DR   iPTMnet; P50087; -.
DR   MaxQB; P50087; -.
DR   PaxDb; P50087; -.
DR   PRIDE; P50087; -.
DR   EnsemblFungi; YGR235C_mRNA; YGR235C; YGR235C.
DR   GeneID; 853150; -.
DR   KEGG; sce:YGR235C; -.
DR   SGD; S000003467; MIC26.
DR   VEuPathDB; FungiDB:YGR235C; -.
DR   eggNOG; ENOG502S70K; Eukaryota.
DR   HOGENOM; CLU_086433_1_0_1; -.
DR   InParanoid; P50087; -.
DR   OMA; KEWTGLN; -.
DR   BioCyc; YEAST:G3O-30913-MON; -.
DR   PRO; PR:P50087; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P50087; 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   InterPro; IPR019166; MIC26/MIC27.
DR   InterPro; IPR033181; Mic26_fungi.
DR   PANTHER; PTHR28268; PTHR28268; 1.
DR   Pfam; PF09769; ApoO; 1.
PE   1: Evidence at protein level;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..233
FT                   /note="MICOS subunit MIC26"
FT                   /id="PRO_0000202852"
FT   TOPO_DOM        1..119
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        138..141
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        165..233
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   233 AA;  26912 MW;  D72E346FE810DF99 CRC64;
     MTKDFYRQLD PVEEKIVPPE NAIVISSEAK EATVNEKEAK QGVLSQRVMK YIGENELVDG
     ISVRDPDYLK RFFNERRKQF SAKWDKVTNK IDDIAGRYYA REESFTSTIA SLHTDPNERL
     IPGLLSILVA SMTGSVLARR RTWLLRATMP IILGSCCFAY AMPTTFRNTM GLIHNLEMNT
     FPHFTERQDR VWKETKRLST ASVQYYYDAK KWLNKDVEKT GNAIKNWTGV NVK
 
 
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