ID   TIM54_YEAST             Reviewed;         478 AA.
AC   P47045; D6VWC8;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   04-NOV-2026, entry version 168.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit TIM54;
GN   Name=TIM54; OrderedLocusNames=YJL054W; ORFNames=J1150;
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=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
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   FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND INTERACTION WITH TIM22.
RX   PubMed=9412462; DOI=10.1083/jcb.139.7.1663;
RA   Kerscher O., Holder J., Srinivasan M., Leung R.S., Jensen R.E.;
RT   "The Tim54p-Tim22p complex mediates insertion of proteins into the
RT   mitochondrial inner membrane.";
RL   J. Cell Biol. 139:1663-1675(1997).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=10397776; DOI=10.1091/mbc.10.7.2461;
RA   Kurz M., Martin H., Rassow J., Pfanner N., Ryan M.T.;
RT   "Biogenesis of Tim proteins of the mitochondrial carrier import pathway:
RT   differential targeting mechanisms and crossing over with the main import
RT   pathway.";
RL   Mol. Biol. Cell 10:2461-2474(1999).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND IDENTIFICATION IN THE TIM22
RP   COMPLEX WITH TIM22 AND TIM18.
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   IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE TIM22
RP   COMPLEX WITH TIM12; TIM22 AND TIM18.
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   [7]
RP   FUNCTION.
RX   PubMed=11864609; DOI=10.1016/s1097-2765(02)00446-x;
RA   Kovermann P., Truscott K.N., Guiard B., Rehling P., Sepuri N.B.,
RA   Mueller H., Jensen R.E., Wagner R., Pfanner N.;
RT   "Tim22, the essential core of the mitochondrial protein insertion complex,
RT   forms a voltage-activated and signal-gated channel.";
RL   Mol. Cell 9:363-373(2002).
RN   [8]
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   [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).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Essential component of the TIM22 complex, a complex that
CC       mediates the import and insertion of multi-pass transmembrane proteins
CC       into the mitochondrial inner membrane. The TIM22 complex forms a twin-
CC       pore translocase that uses the membrane potential as external driving
CC       force. Its precise function within the TIM22 complex is unclear.
CC       {ECO:0000269|PubMed:10637294, ECO:0000269|PubMed:11864609,
CC       ECO:0000269|PubMed:9412462}.
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   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:10397776, ECO:0000269|PubMed:10637294,
CC       ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:9412462}; Single-pass
CC       membrane protein {ECO:0000269|PubMed:10397776,
CC       ECO:0000269|PubMed:10637294, ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:9412462}. Note=Import into inner membrane protein
CC       requires TOM70 function.
CC   -!- SIMILARITY: Belongs to the TIM54 family. {ECO:0000305}.
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DR   EMBL; Z49329; CAA89345.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08744.1; -; Genomic_DNA.
DR   PIR; S56826; S56826.
DR   RefSeq; NP_012481.3; NM_001181487.3.
DR   PDB; 6LO8; EM; 3.83 A; B=1-478.
DR   AlphaFoldDB; P47045; -.
DR   EMDB; EMD-0935; -.
DR   SMR; P47045; -.
DR   BioGRID; 33700; 293.
DR   ComplexPortal; CPX-1629; TIM22 mitochondrial inner membrane twin-pore carrier translocase complex.
DR   DIP; DIP-5898N; -.
DR   FunCoup; P47045; 37.
DR   IntAct; P47045; 16.
DR   STRING; 4932.YJL054W; -.
DR   TCDB; 3.A.8.1.1; the mitochondrial protein translocase (mpt) family.
DR   iPTMnet; P47045; -.
DR   PaxDb; 4932-YJL054W; -.
DR   PeptideAtlas; P47045; -.
DR   EnsemblFungi; YJL054W_mRNA; YJL054W; YJL054W.
DR   GeneID; 853392; -.
DR   KEGG; sce:YJL054W; -.
DR   AGR; SGD:S000003590; -.
DR   SGD; S000003590; TIM54.
DR   VEuPathDB; FungiDB:YJL054W; -.
DR   eggNOG; ENOG502QPMQ; Eukaryota.
DR   HOGENOM; CLU_039097_0_0_1; -.
DR   InParanoid; P47045; -.
DR   OMA; AAFIQPC; -.
DR   OrthoDB; 5598305at2759; -.
DR   BioCyc; YEAST:G3O-31517-MONOMER; -.
DR   Reactome; R-SCE-1660661; Sphingolipid de novo biosynthesis.
DR   Reactome; R-SCE-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR   Reactome; R-SCE-5218921; VEGFR2 mediated cell proliferation.
DR   Reactome; R-SCE-9009391; Extra-nuclear estrogen signaling.
DR   Reactome; R-SCE-9833482; PKR-mediated signaling.
DR   BioGRID-ORCS; 853392; 4 hits in 10 CRISPR screens.
DR   PRO; PR:P47045; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P47045; protein.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
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:0045039; P:protein insertion into mitochondrial inner membrane; IDA:ComplexPortal.
DR   GO; GO:0071806; P:protein transmembrane transport; IEA:GOC.
DR   InterPro; IPR050187; Lipid_Phosphate_FormReg.
DR   InterPro; IPR021056; Mt_import_IM_translocase_Tim54.
DR   PANTHER; PTHR12358:SF101; MITOCHONDRIAL IMPORT INNER MEMBRANE TRANSLOCASE SUBUNIT TIM54; 1.
DR   PANTHER; PTHR12358; SPHINGOSINE KINASE; 1.
DR   Pfam; PF11711; Tim54; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Protein transport; Reference proteome; Translocation; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..478
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit TIM54"
FT                   /id="PRO_0000203062"
FT   TOPO_DOM        1..32
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        33..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        50..478
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REGION          152..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   478 AA;  54183 MW;  0E682BB4035E3A4C CRC64;
     MSSESGKPIA KPIRKPGYTN PALKALGIPA LRLPSRNWMI FWSVLTVSIG GIAYDKYKQR
     QILSHATDLV KPLAEESMEV DKVPRKITVF IAPPPNDYLE SSLKVWRRYV KPVLYYAGLD
     YELVQEDRQG IIRTNVANRI RELRKEILAS TDGQPVKEPN QTVAKPSGSS TSKISSLLPF
     NKIIQDPAEE DDSFDPEIGK KFKENFDWRN VIGIFYTMPK PKHIISEDAL TKDPILSGGV
     ICLGRGAYKE YIAGIHEGLL GPIEKTEKTG STEPKMTGVV EANQIESKVS ESGATELVDA
     EKETALEEAK VQDDLKVDEE NSSEDSQKFL KPFISSDQYP DLQIASELQT PNGEFIRNPN
     TNIPLLINQP LLVIPIPNLI GFTTIPRRIH RFYQKRFYVE DVCSSVVNCV RQTRIRPFDI
     AKDIDLAKDE EKDWPQNWVK QGKEKNSEWT QELVCDPRIT KHMFVYEKPP KEEPESDI
//