TIM54_YEAST
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 03-AUG-2022, entry version 151.
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 PDBsum; 6LO8; -.
DR AlphaFoldDB; P47045; -.
DR SMR; P47045; -.
DR BioGRID; 33700; 272.
DR ComplexPortal; CPX-1629; TIM22 mitochondrial inner membrane twin-pore carrier translocase complex.
DR DIP; DIP-5898N; -.
DR IntAct; P47045; 4.
DR STRING; 4932.YJL054W; -.
DR TCDB; 3.A.8.1.1; the mitochondrial protein translocase (mpt) family.
DR iPTMnet; P47045; -.
DR MaxQB; P47045; -.
DR PaxDb; P47045; -.
DR PRIDE; P47045; -.
DR EnsemblFungi; YJL054W_mRNA; YJL054W; YJL054W.
DR GeneID; 853392; -.
DR KEGG; sce:YJL054W; -.
DR SGD; S000003590; TIM54.
DR VEuPathDB; FungiDB:YJL054W; -.
DR eggNOG; ENOG502QPMQ; Eukaryota.
DR HOGENOM; CLU_039097_0_0_1; -.
DR InParanoid; P47045; -.
DR OMA; EEKEWHK; -.
DR BioCyc; YEAST:G3O-31517-MON; -.
DR Reactome; R-SCE-1483206; Glycerophospholipid biosynthesis.
DR Reactome; R-SCE-1660661; Sphingolipid de novo biosynthesis.
DR PRO; PR:P47045; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47045; protein.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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: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; IPR021056; Mt_import_IM_translocase_Tim54.
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"
FT COMPBIAS 154..171
FT /note="Polar residues"
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
