MIX23_YEAST
ID MIX23_YEAST Reviewed; 196 AA.
AC P38162; D6VPP6;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Mitochondrial intermembrane space cysteine motif-containing protein MIX23 {ECO:0000303|PubMed:32826315};
DE AltName: Full=Mitochondrial intermembrane space CX(n)C motif protein of 23 kDa {ECO:0000303|PubMed:32826315};
GN Name=MIX23 {ECO:0000312|SGD:S000000203};
GN Synonyms=MIC23 {ECO:0000303|PubMed:22984289};
GN OrderedLocusNames=YBL107C {ECO:0000303|PubMed:22984289}; ORFNames=YBL0805;
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=7502586; DOI=10.1002/yea.320111112;
RA Obermaier B., Gassenhuber J., Piravandi E., Domdey H.;
RT "Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces
RT cerevisiae chromosome II.";
RL Yeast 11:1103-1112(1995).
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 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS], AND DOMAIN.
RX PubMed=22984289; DOI=10.1074/mcp.m112.021105;
RA Voegtle F.N., Burkhart J.M., Rao S., Gerbeth C., Hinrichs J.,
RA Martinou J.C., Chacinska A., Sickmann A., Zahedi R.P., Meisinger C.;
RT "Intermembrane space proteome of yeast mitochondria.";
RL Mol. Cell. Proteomics 11:1840-1852(2012).
RN [6]
RP GENE NAME.
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).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY RPN4, AND MUTAGENESIS OF
RP CYS-38; CYS-77; CYS-99; CYS-114; CYS-178 AND CYS-192.
RX PubMed=32826315; DOI=10.1074/jbc.ra120.014247;
RA Zoeller E., Laborenz J., Kraemer L., Boos F., Raeschle M., Alexander R.T.,
RA Herrmann J.M.;
RT "The intermembrane space protein Mix23 is a novel stress-induced
RT mitochondrial import factor.";
RL J. Biol. Chem. 295:14686-14697(2020).
CC -!- FUNCTION: Regulator of the mitochondrial protein import machinery that
CC is localized in the mitochondrial intermembrane space (IMS) and
CC facilitates the transport of proteins from the cytosol into the
CC mitochondrial matrix (PubMed:32826315). Not essential for mitochondrial
CC protein import but induced and required when mitochondrial import is
CC compromised (PubMed:32826315). Stimulates or stabilizes the
CC translocation into the mitochondria of proteins such as OXA1, ATP1 and
CC COX12 (PubMed:32826315). {ECO:0000269|PubMed:32826315}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:22984289, ECO:0000269|PubMed:32826315}.
CC Note=Imported into the mitochondria via the mitochondrial MIA40-ERV1
CC machinery. {ECO:0000269|PubMed:22984289, ECO:0000269|PubMed:32826315}.
CC -!- INDUCTION: Up-regulated by RPN4 transcription factor upon mitochondrial
CC protein-induced stress conditions such as the accumulation in the
CC cytosol of non-imported mitochondrial precursors.
CC {ECO:0000269|PubMed:32826315}.
CC -!- DOMAIN: The Cx14C/Cx13C motifs are involved in the recognition by the
CC mitochondrial MIA40-ERV1 disulfide relay system and the subsequent
CC transfer of disulfide bonds by dithiol/disulfide exchange reactions to
CC the newly imported protein. {ECO:0000269|PubMed:22984289}.
CC -!- MISCELLANEOUS: Present with 768 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MIX23 family. {ECO:0000305}.
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DR EMBL; X79489; CAA55988.1; -; Genomic_DNA.
DR EMBL; Z35868; CAA84934.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07016.1; -; Genomic_DNA.
DR PIR; S45388; S45388.
DR RefSeq; NP_009443.1; NM_001178347.1.
DR AlphaFoldDB; P38162; -.
DR SMR; P38162; -.
DR BioGRID; 32596; 45.
DR DIP; DIP-3952N; -.
DR IntAct; P38162; 1.
DR STRING; 4932.YBL107C; -.
DR MaxQB; P38162; -.
DR PaxDb; P38162; -.
DR PRIDE; P38162; -.
DR EnsemblFungi; YBL107C_mRNA; YBL107C; YBL107C.
DR GeneID; 852167; -.
DR KEGG; sce:YBL107C; -.
DR SGD; S000000203; MIX23.
DR VEuPathDB; FungiDB:YBL107C; -.
DR eggNOG; ENOG502S17Q; Eukaryota.
DR HOGENOM; CLU_118733_0_0_1; -.
DR InParanoid; P38162; -.
DR OMA; WQTRSDV; -.
DR BioCyc; YEAST:G3O-28991-MON; -.
DR PRO; PR:P38162; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38162; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR019171; MIX23.
DR InterPro; IPR016805; MIX23_fungal.
DR PANTHER; PTHR31905; PTHR31905; 1.
DR Pfam; PF09774; Cid2; 1.
DR PIRSF; PIRSF022603; UCP022603; 1.
PE 1: Evidence at protein level;
KW Mitochondrion; Protein transport; Reference proteome; Transport.
FT CHAIN 1..196
FT /note="Mitochondrial intermembrane space cysteine motif-
FT containing protein MIX23"
FT /id="PRO_0000202439"
FT MOTIF 99..114
FT /note="Cx14C motif"
FT /evidence="ECO:0000303|PubMed:22984289"
FT MOTIF 178..192
FT /note="Cx13C motif"
FT /evidence="ECO:0000303|PubMed:22984289"
FT MUTAGEN 38
FT /note="C->S: Loss of MIA40-dependent import into the
FT mitochondrial intermembrane space; when associated with S-
FT 77, S-99, S-114, S-178 and S-192."
FT /evidence="ECO:0000269|PubMed:32826315"
FT MUTAGEN 77
FT /note="C->S: Loss of MIA40-dependent import into the
FT mitochondrial intermembrane space; when associated with S-
FT 38, S-99, S-114, S-178 and S-192."
FT /evidence="ECO:0000269|PubMed:32826315"
FT MUTAGEN 99
FT /note="C->S: Loss of MIA40-dependent import into the
FT mitochondrial intermembrane space; when associated with S-
FT 38, S-77, S-114, S-178 and S-192."
FT /evidence="ECO:0000269|PubMed:32826315"
FT MUTAGEN 114
FT /note="C->S: Loss of MIA40-dependent import into the
FT mitochondrial intermembrane space; when associated with S-
FT 38, S-77, S-99, S-178 and S-192."
FT /evidence="ECO:0000269|PubMed:32826315"
FT MUTAGEN 178
FT /note="C->S: Loss of MIA40-dependent import into the
FT mitochondrial intermembrane space; when associated with S-
FT 38, S-77, S-99, S-114 and S-192."
FT /evidence="ECO:0000269|PubMed:32826315"
FT MUTAGEN 192
FT /note="C->S: Loss of MIA40-dependent import into the
FT mitochondrial intermembrane space; when associated with S-
FT 38, S-77, S-99, S-114 and S-178."
FT /evidence="ECO:0000269|PubMed:32826315"
SQ SEQUENCE 196 AA; 22966 MW; E54356AE336896B5 CRC64;
MVDNRRTFTA PQSLLETNLT FPNDEPSLTT ITVTRERCVD PSLIDSFLRF LRHGSDDIIR
QKLNNYRKGS INGKNKCKEF LKQELYPNWQ IRNNIISFCE KEAAEMKNET DQQCGNNKKT
TAEPLIDARI DPYAARERAE KQEAQYKDWT KVTEWVANNR KIEQILTSTT EGILRQNCEQ
NNDYLKEFTQ FCKDNS
