TIM18_YEAST
ID TIM18_YEAST Reviewed; 192 AA.
AC Q08749; D6W2Z6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM18;
DE Flags: Precursor;
GN Name=TIM18; OrderedLocusNames=YOR297C;
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], FUNCTION, SUBCELLULAR LOCATION,
RP TOPOLOGY, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP TIM22 COMPLEX WITH TIM12; TIM22 AND TIM54.
RC STRAIN=ATCC 24657 / D273-10B;
RX PubMed=10648604; DOI=10.1128/mcb.20.4.1187-1193.2000;
RA Koehler C.M., Murphy M.P., Bally N.A., Leuenberger D., Oppliger W.,
RA Dolfini L., Junne T., Schatz G., Or E.;
RT "Tim18p, a new subunit of the TIM22 complex that mediates insertion of
RT imported proteins into the yeast mitochondrial inner membrane.";
RL Mol. Cell. Biol. 20:1187-1193(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9153758;
RX DOI=10.1002/(sici)1097-0061(199704)13:5<479::aid-yea104>3.0.co;2-g;
RA Poirey R., Cziepluch C., Tobiasch E., Pujol A., Kordes E., Jauniaux J.-C.;
RT "Sequence and analysis of a 36.2 kb fragment from the right arm of yeast
RT chromosome XV reveals 19 open reading frames including SNF2 (5' end), CPA1,
RT SLY41, a putative transport ATPase, a putative ribosomal protein and an
RT SNF2 homologue.";
RL Yeast 13:479-482(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 137.
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 FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND IDENTIFICATION IN THE TIM22
RP COMPLEX WITH TIM22 AND TIM54.
RX PubMed=10637294; DOI=10.1091/mbc.11.1.103;
RA Kerscher O., Sepuri N.B., Jensen R.E.;
RT "Tim18p is a new component of the Tim54p-Tim22p translocon in the
RT mitochondrial inner membrane.";
RL Mol. Biol. Cell 11:103-116(2000).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14504216; DOI=10.1093/genetics/165.1.35;
RA Dunn C.D., Jensen R.E.;
RT "Suppression of a defect in mitochondrial protein import identifies
RT cytosolic proteins required for viability of yeast cells lacking
RT mitochondrial DNA.";
RL Genetics 165:35-45(2003).
RN [7]
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 [8]
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 [9]
RP IDENTIFICATION IN THE TIM22 COMPLEX WITH TIM10; TIM12; TIM22 AND TIM54.
RX PubMed=12637749; DOI=10.1126/science.1080945;
RA Rehling P., Model K., Brandner K., Kovermann P., Sickmann A., Meyer H.E.,
RA Kuehlbrandt W., Wagner R., Truscott K.N., Pfanner N.;
RT "Protein insertion into the mitochondrial inner membrane by a twin-pore
RT translocase.";
RL Science 299:1747-1751(2003).
RN [10]
RP ERRATUM OF PUBMED:12637749.
RA Rehling P., Model K., Brandner K., Kovermann P., Sickmann A., Meyer H.E.,
RA Kuehlbrandt W., Wagner R., Truscott K.N., Pfanner N.;
RL Science 300:251-251(2003).
CC -!- FUNCTION: Component of the TIM22 complex, a complex that mediates the
CC import and insertion of multi-pass transmembrane proteins into the
CC mitochondrial inner membrane. The TIM22 complex forms a twin-pore
CC translocase that uses the membrane potential as external driving force.
CC Its role in the complex is unclear but it may be involved in the
CC assembly and stabilization of the TIM22 complex.
CC {ECO:0000269|PubMed:10637294, ECO:0000269|PubMed:10648604,
CC ECO:0000269|PubMed:14504216}.
CC -!- SUBUNIT: Component of the TIM22 complex, whose core is composed of
CC TIM18, TIM22 and TIM54, associated with the peripheral proteins
CC MRS5/TIM12 and the 70 kDa heterohexamer composed of TIM9 and TIM10 (or
CC TIM8 and TIM13). {ECO:0000269|PubMed:10637294,
CC ECO:0000269|PubMed:10648604, ECO:0000269|PubMed:12637749}.
CC -!- INTERACTION:
CC Q08749; P87108: TIM10; NbExp=2; IntAct=EBI-30499, EBI-9115;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:10637294, ECO:0000269|PubMed:10648604,
CC ECO:0000269|PubMed:14562095}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10637294, ECO:0000269|PubMed:10648604,
CC ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Although cells lacking TIM18 live well and do not
CC display any strong phenotype, they do not survive in the absence of
CC mitochondrial DNA. {ECO:0000269|PubMed:14504216}.
CC -!- MISCELLANEOUS: Present with 4440 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CybS family. {ECO:0000305}.
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DR EMBL; AF200324; AAF13717.1; -; Genomic_DNA.
DR EMBL; Z75205; CAA99525.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11062.2; -; Genomic_DNA.
DR PIR; S67201; S67201.
DR RefSeq; NP_014940.4; NM_001183716.4.
DR PDB; 6LO8; EM; 3.83 A; D=1-192.
DR PDBsum; 6LO8; -.
DR AlphaFoldDB; Q08749; -.
DR SMR; Q08749; -.
DR BioGRID; 34685; 305.
DR ComplexPortal; CPX-1629; TIM22 mitochondrial inner membrane twin-pore carrier translocase complex.
DR DIP; DIP-5205N; -.
DR IntAct; Q08749; 5.
DR MINT; Q08749; -.
DR STRING; 4932.YOR297C; -.
DR TCDB; 3.A.8.1.1; the mitochondrial protein translocase (mpt) family.
DR iPTMnet; Q08749; -.
DR MaxQB; Q08749; -.
DR PaxDb; Q08749; -.
DR PRIDE; Q08749; -.
DR EnsemblFungi; YOR297C_mRNA; YOR297C; YOR297C.
DR GeneID; 854472; -.
DR KEGG; sce:YOR297C; -.
DR SGD; S000005823; TIM18.
DR VEuPathDB; FungiDB:YOR297C; -.
DR eggNOG; KOG4097; Eukaryota.
DR GeneTree; ENSGT00390000010003; -.
DR HOGENOM; CLU_096618_0_1_1; -.
DR InParanoid; Q08749; -.
DR OMA; DYIPKRK; -.
DR BioCyc; YEAST:G3O-33782-MON; -.
DR Reactome; R-SCE-71403; Citric acid cycle (TCA cycle).
DR PRO; PR:Q08749; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08749; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0042721; C:TIM22 mitochondrial import inner membrane insertion complex; IDA:SGD.
DR GO; GO:0006915; P:apoptotic process; IMP:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0071806; P:protein transmembrane transport; IEA:GOC.
DR GO; GO:0046685; P:response to arsenic-containing substance; IMP:SGD.
DR GO; GO:0006970; P:response to osmotic stress; IMP:SGD.
DR CDD; cd03496; SQR_TypeC_CybS; 1.
DR Gene3D; 1.20.1300.10; -; 1.
DR InterPro; IPR007992; CybS.
DR InterPro; IPR034804; SQR/QFR_C/D.
DR PANTHER; PTHR13337; PTHR13337; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Protein transport; Reference proteome; Transit peptide; Translocation;
KW Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..42
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 43..192
FT /note="Mitochondrial import inner membrane translocase
FT subunit TIM18"
FT /id="PRO_0000228080"
FT TOPO_DOM 43..88
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..113
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..144
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..192
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT CONFLICT 137
FT /note="E -> G (in Ref. 1; AAF13717, 2 and 3; CAA99525)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 192 AA; 21972 MW; FE5DBEF3E3446CF7 CRC64;
MLLFPGLKPV LNASTVIVNP VRAVFPGLVL STKRSFYSIN RLNAENKIND IANTSKEASS
SVQMFKPPEF SQFKDSYQKD YERIAKYTLI PLTMVPFYAS FTGGVINPLL DASLSSIFLI
YLQYGFTSCI IDYIPKEKYP RWHKLALYCL YGGSMLSLYG IYELETKNNG FVDLVKKLWN
ENDDHLYIFG RN
