ID   MIC27_YEAST             Reviewed;         234 AA.
AC   P50945; D6W179; Q45U03;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-NOV-2023, entry version 133.
DE   RecName: Full=MICOS complex subunit MIC27;
DE   AltName: Full=Altered inheritance of mitochondria protein 37;
DE   AltName: Full=Mitochondrial contact site complex 27 kDa subunit;
GN   Name=MIC27; Synonyms=AIM37, MCS27; OrderedLocusNames=YNL100W;
GN   ORFNames=N2190;
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=SK1;
RX   PubMed=16273108; DOI=10.1038/ng1674;
RA   Deutschbauer A.M., Davis R.W.;
RT   "Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
RL   Nat. Genet. 37:1333-1340(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8701612;
RX   DOI=10.1002/(sici)1097-0061(19960330)12:4<403::aid-yea923>3.0.co;2-h;
RA   Saiz J.E., Buitrago M.J., Soler A., del Rey F., Revuelta J.L.;
RT   "The sequence of a 21.3 kb DNA fragment from the left arm of yeast
RT   chromosome XIV reveals LEU4, MET4, POL1, RAS2, and six new open reading
RT   frames.";
RL   Yeast 12:403-409(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [4]
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   [5]
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   [6]
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   [7]
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   [8]
RP   PREDICTION OF FUNCTION.
RX   PubMed=17005538; DOI=10.1093/bioinformatics/btl492;
RA   Huttenhower C., Hibbs M., Myers C., Troyanskaya O.G.;
RT   "A scalable method for integration and functional analysis of multiple
RT   microarray datasets.";
RL   Bioinformatics 22:2890-2897(2006).
RN   [9]
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   [10]
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   [11]
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   [12]
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   [13]
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: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   -!- SIMILARITY: Belongs to the apolipoprotein O/MICOS complex subunit Mic27
CC       family. {ECO:0000305}.
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DR   EMBL; DQ115393; AAZ22507.1; -; Genomic_DNA.
DR   EMBL; Z50161; CAA90526.1; -; Genomic_DNA.
DR   EMBL; Z71376; CAA95976.1; -; Genomic_DNA.
DR   EMBL; AY692704; AAT92723.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10445.1; -; Genomic_DNA.
DR   PIR; S58252; S58252.
DR   RefSeq; NP_014299.1; NM_001182938.1.
DR   AlphaFoldDB; P50945; -.
DR   SMR; P50945; -.
DR   BioGRID; 35723; 161.
DR   ComplexPortal; CPX-140; MICOS mitochondrial contact site and cristae organizing system complex.
DR   DIP; DIP-2042N; -.
DR   IntAct; P50945; 9.
DR   MINT; P50945; -.
DR   STRING; 4932.YNL100W; -.
DR   MaxQB; P50945; -.
DR   PaxDb; 4932-YNL100W; -.
DR   PeptideAtlas; P50945; -.
DR   EnsemblFungi; YNL100W_mRNA; YNL100W; YNL100W.
DR   GeneID; 855623; -.
DR   KEGG; sce:YNL100W; -.
DR   AGR; SGD:S000005044; -.
DR   SGD; S000005044; MIC27.
DR   VEuPathDB; FungiDB:YNL100W; -.
DR   eggNOG; ENOG502S31N; Eukaryota.
DR   HOGENOM; CLU_093584_0_0_1; -.
DR   InParanoid; P50945; -.
DR   OMA; KYKVCKG; -.
DR   OrthoDB; 2017057at2759; -.
DR   BioCyc; YEAST:G3O-33128-MONOMER; -.
DR   BioGRID-ORCS; 855623; 3 hits in 10 CRISPR screens.
DR   PRO; PR:P50945; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P50945; 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:0043933; P:protein-containing complex organization; IMP:SGD.
PE   1: Evidence at protein level;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..234
FT                   /note="MICOS complex subunit MIC27"
FT                   /id="PRO_0000203438"
FT   TOPO_DOM        1..100
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        101..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        121..141
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        162..234
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   234 AA;  26960 MW;  8DFD8FD42E71B8DB CRC64;
     MVNFYDDVDE SKSHGEFPLI PVVLQNSSEL SVRTIPTGNE IIESVHLTKW LRKYRNALAS
     QLDRYEKGWQ SKIANFRLQV QHVINYSRKN IFNVDSENKH TVVPGSLIAL GAFFAGSIAV
     NRSNWGAKRL IFGHKSSILE KLCTSLPSRI LLPWVLAAAT FKYWAPQTSQ NLVNATENDL
     LPADFVKSYH NTWKRIYEEG YVAKKCDLKR QIDQTLQKNI RYAREQLYEK LEQA
//