ID   MIC19_YEAST             Reviewed;         170 AA.
AC   P43594; D6VTP1;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 154.
DE   RecName: Full=MICOS complex subunit MIC19;
DE   AltName: Full=Altered inheritance of mitochondria protein 13, mitochondrial;
DE   AltName: Full=Mitochondrial contact site complex 19 kDa subunit;
GN   Name=MIC19; Synonyms=AIM13, MCS19; OrderedLocusNames=YFR011C;
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=7670463; DOI=10.1038/ng0795-261;
RA   Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA   Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA   Eki T.;
RT   "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT   cerevisiae.";
RL   Nat. Genet. 10:261-268(1995).
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   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   [4]
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   [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   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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(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, AND SUBCELLULAR
RP   LOCATION.
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, 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   [11]
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   -!- INTERACTION:
CC       P43594; P36112: MIC60; NbExp=5; IntAct=EBI-22936, EBI-27078;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:21944719,
CC       ECO:0000269|PubMed:21987634, ECO:0000269|PubMed:22009199}; Peripheral
CC       membrane protein {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:21944719, ECO:0000269|PubMed:21987634,
CC       ECO:0000269|PubMed:22009199}; Intermembrane side
CC       {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:21944719,
CC       ECO:0000269|PubMed:21987634, ECO:0000269|PubMed:22009199}.
CC       Note=Enriched at crista junctions.
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 3550 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the MICOS complex subunit Mic19 family.
CC       {ECO:0000305}.
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DR   EMBL; D50617; BAA09250.1; -; Genomic_DNA.
DR   EMBL; AY692683; AAT92702.1; -; Genomic_DNA.
DR   EMBL; BK006940; DAA12451.1; -; Genomic_DNA.
DR   PIR; S56266; S56266.
DR   RefSeq; NP_116666.1; NM_001179976.1.
DR   AlphaFoldDB; P43594; -.
DR   SMR; P43594; -.
DR   BioGRID; 31161; 194.
DR   ComplexPortal; CPX-140; MICOS mitochondrial contact site and cristae organizing system complex.
DR   DIP; DIP-1570N; -.
DR   IntAct; P43594; 8.
DR   MINT; P43594; -.
DR   STRING; 4932.YFR011C; -.
DR   MaxQB; P43594; -.
DR   PaxDb; 4932-YFR011C; -.
DR   PeptideAtlas; P43594; -.
DR   EnsemblFungi; YFR011C_mRNA; YFR011C; YFR011C.
DR   GeneID; 850563; -.
DR   KEGG; sce:YFR011C; -.
DR   AGR; SGD:S000001907; -.
DR   SGD; S000001907; MIC19.
DR   VEuPathDB; FungiDB:YFR011C; -.
DR   eggNOG; ENOG502SDJV; Eukaryota.
DR   HOGENOM; CLU_093897_3_0_1; -.
DR   InParanoid; P43594; -.
DR   OMA; TDFTRQQ; -.
DR   OrthoDB; 2055598at2759; -.
DR   BioCyc; YEAST:G3O-30464-MONOMER; -.
DR   BioGRID-ORCS; 850563; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P43594; -.
DR   Proteomes; UP000002311; Chromosome VI.
DR   RNAct; P43594; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
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; IPR012471; DUF1690.
DR   Pfam; PF07956; DUF1690; 1.
PE   1: Evidence at protein level;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome.
FT   CHAIN           1..170
FT                   /note="MICOS complex subunit MIC19"
FT                   /id="PRO_0000202684"
SQ   SEQUENCE   170 AA;  18855 MW;  0E6670669D3AD0AA CRC64;
     MGSNTSKVGA GAEKQQVYTP LTQIDFSQSL VSQLDSSKES DYVTKQNAEK FIEKKVSQRL
     SNLEVETLKK FEDTLNNSLL SDDDKDAVDG ISSSSLNNQI ESLNKKLTLF DQLELQKLEK
     YGGAKGKSDK KTDNGSISIK AKLTECLLAN KGKPLNCYEE MEEFKKLVMG
//