TIM17_YEAST
ID TIM17_YEAST Reviewed; 158 AA.
AC P39515; D6VW42; Q02310;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM17;
DE AltName: Full=Mitochondrial inner membrane protein MIM17;
DE AltName: Full=Mitochondrial protein import protein 2;
GN Name=TIM17; Synonyms=MIM17, MPI2, SMS1; OrderedLocusNames=YJL143W;
GN ORFNames=J0648;
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 77162;
RX PubMed=8050569; DOI=10.1016/0014-5793(94)00669-5;
RA Maarse A.C., Blom J., Keil P., Pfanner N., Meijer M.;
RT "Identification of the essential yeast protein MIM17, an integral
RT mitochondrial inner membrane protein involved in protein import.";
RL FEBS Lett. 349:215-221(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7919535; DOI=10.1091/mbc.5.5.529;
RA Ryan K.R., Menold M.M., Garrett S., Jensen R.E.;
RT "SMS1, a high-copy suppressor of the yeast mas6 mutant, encodes an
RT essential inner membrane protein required for mitochondrial protein
RT import.";
RL Mol. Biol. Cell 5:529-538(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8813765;
RX DOI=10.1002/(sici)1097-0061(19960630)12:8<787::aid-yea954>3.0.co;2-4;
RA Katsoulou C., Tzermia M., Tavernarakis N., Alexandraki D.;
RT "Sequence analysis of a 40.7 kb segment from the left arm of yeast
RT chromosome X reveals 14 known genes and 13 new open reading frames
RT including homologues of genes clustered on the right arm of chromosome
RT XI.";
RL Yeast 12:787-797(1996).
RN [4]
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 [5]
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 [6]
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 [7]
RP CHARACTERIZATION, AND TOPOLOGY.
RX PubMed=8050570; DOI=10.1016/0014-5793(94)00670-9;
RA Kuebrich M., Keil P., Rassow J., Dekker P.J.T., Blom J., Meijer M.,
RA Pfanner N.;
RT "The polytopic mitochondrial inner membrane proteins MIM17 and MIM23
RT operate at the same preprotein import site.";
RL FEBS Lett. 349:222-228(1994).
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 TIM23 COMPLEX.
RX PubMed=15797382; DOI=10.1016/j.cell.2005.01.011;
RA Chacinska A., Lind M., Frazier A.E., Dudek J., Meisinger C., Geissler A.,
RA Sickmann A., Meyer H.E., Truscott K.N., Guiard B., Pfanner N., Rehling P.;
RT "Mitochondrial presequence translocase: switching between TOM tethering and
RT motor recruitment involves Tim21 and Tim17.";
RL Cell 120:817-829(2005).
RN [10]
RP MUTAGENESIS OF ASP-4 AND ASP-8.
RX PubMed=15618217; DOI=10.1074/jbc.m412158200;
RA Meier S., Neupert W., Herrmann J.M.;
RT "Conserved N-terminal negative charges in the Tim17 subunit of the TIM23
RT translocase play a critical role in the import of preproteins into
RT mitochondria.";
RL J. Biol. Chem. 280:7777-7785(2005).
RN [11]
RP DISULFIDE BOND, SUBCELLULAR LOCATION, TOPOLOGY, IDENTIFICATION IN THE TIM23
RP COMPLEX, AND MUTAGENESIS OF CYS-10; CYS-77; CYS-118 AND CYS-120.
RX PubMed=27265872; DOI=10.1038/srep27484;
RA Wrobel L., Sokol A.M., Chojnacka M., Chacinska A.;
RT "The presence of disulfide bonds reveals an evolutionarily conserved
RT mechanism involved in mitochondrial protein translocase assembly.";
RL Sci. Rep. 6:27484-27484(2016).
CC -!- FUNCTION: Essential component of the TIM23 complex, a complex that
CC mediates the translocation of transit peptide-containing proteins
CC across the mitochondrial inner membrane. {ECO:0000269|PubMed:8050570}.
CC -!- SUBUNIT: Component of the TIM23 complex, at least composed of TIM23,
CC TIM17, TIM50 and TIM21 (PubMed:15797382, PubMed:27265872). The complex
CC interacts with the TIM44 component of the PAM complex
CC (PubMed:15797382). {ECO:0000269|PubMed:15797382,
CC ECO:0000269|PubMed:27265872}.
CC -!- INTERACTION:
CC P39515; P42949: PAM16; NbExp=4; IntAct=EBI-9127, EBI-26019;
CC P39515; Q07914: PAM18; NbExp=3; IntAct=EBI-9127, EBI-31963;
CC P39515; P32897: TIM23; NbExp=14; IntAct=EBI-9127, EBI-9136;
CC P39515; Q01852: TIM44; NbExp=2; IntAct=EBI-9127, EBI-9141;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:27265872}; Multi-pass membrane protein.
CC -!- PTM: The disulfide bond is required for stabilization of the TIM23
CC complex. {ECO:0000269|PubMed:27265872}.
CC -!- MISCELLANEOUS: Present with 1210 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the Tim17/Tim22/Tim23 family. {ECO:0000305}.
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DR EMBL; X77796; CAA54823.1; -; Genomic_DNA.
DR EMBL; S74018; AAB32164.1; -; Genomic_DNA.
DR EMBL; X87371; CAA60812.1; -; Genomic_DNA.
DR EMBL; Z49418; CAA89438.1; -; Genomic_DNA.
DR EMBL; AY557852; AAS56178.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08658.1; -; Genomic_DNA.
DR PIR; S46257; S46257.
DR RefSeq; NP_012392.1; NM_001181576.1.
DR AlphaFoldDB; P39515; -.
DR BioGRID; 33615; 38.
DR ComplexPortal; CPX-539; TIM23 mitochondrial inner membrane pre-sequence translocase complex, motor variant.
DR ComplexPortal; CPX-6127; TIM23 mitochondrial inner membrane pre-sequence translocase complex, sort variant.
DR DIP; DIP-2108N; -.
DR IntAct; P39515; 11.
DR MINT; P39515; -.
DR STRING; 4932.YJL143W; -.
DR TCDB; 3.A.8.1.1; the mitochondrial protein translocase (mpt) family.
DR MaxQB; P39515; -.
DR PaxDb; P39515; -.
DR PRIDE; P39515; -.
DR DNASU; 853298; -.
DR EnsemblFungi; YJL143W_mRNA; YJL143W; YJL143W.
DR GeneID; 853298; -.
DR KEGG; sce:YJL143W; -.
DR SGD; S000003679; TIM17.
DR VEuPathDB; FungiDB:YJL143W; -.
DR eggNOG; KOG1652; Eukaryota.
DR GeneTree; ENSGT00390000017780; -.
DR HOGENOM; CLU_087811_3_0_1; -.
DR InParanoid; P39515; -.
DR OMA; CPWVILS; -.
DR BioCyc; YEAST:G3O-31587-MON; -.
DR Reactome; R-SCE-1268020; Mitochondrial protein import.
DR PRO; PR:P39515; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P39515; protein.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; IDA:SGD.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IC:ComplexPortal.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IGI:SGD.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IMP:SGD.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IC:ComplexPortal.
DR InterPro; IPR005678; Tim17.
DR TIGRFAMs; TIGR00980; 3a0801so1tim17; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Protein transport; Reference proteome; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..158
FT /note="Mitochondrial import inner membrane translocase
FT subunit TIM17"
FT /id="PRO_0000210296"
FT TOPO_DOM 1..11
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:27265872"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..58
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..87
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:27265872"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..112
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..158
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT DISULFID 10..77
FT /evidence="ECO:0000305|PubMed:27265872"
FT MUTAGEN 4
FT /note="D->R: Induces abolition of mitochondrial import of
FT transit peptide-containing proteins; when associated with
FT K-8."
FT /evidence="ECO:0000269|PubMed:15618217"
FT MUTAGEN 8
FT /note="D->K: Induces abolition of mitochondrial import of
FT transit peptide-containing proteins; when associated with
FT K-4."
FT /evidence="ECO:0000269|PubMed:15618217"
FT MUTAGEN 10
FT /note="C->S: Abolishes disulfide bond, leading to
FT destabilization of the TIM23 complex."
FT /evidence="ECO:0000269|PubMed:27265872"
FT MUTAGEN 77
FT /note="C->S: Abolishes disulfide bond, leading to
FT destabilization of the TIM23 complex."
FT /evidence="ECO:0000269|PubMed:27265872"
FT MUTAGEN 118
FT /note="C->S: Does not affect oxidation state."
FT /evidence="ECO:0000269|PubMed:27265872"
FT MUTAGEN 120
FT /note="C->S: Does not affect oxidation state."
FT /evidence="ECO:0000269|PubMed:27265872"
FT CONFLICT 33
FT /note="H -> T (in Ref. 2; AAB32164)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 158 AA; 16584 MW; 1760B08F3B60D378 CRC64;
MSADHSRDPC PIVILNDFGG AFAMGAIGGV VWHGIKGFRN SPLGERGSGA MSAIKARAPV
LGGNFGVWGG LFSTFDCAVK AVRKREDPWN AIIAGFFTGG ALAVRGGWRH TRNSSITCAC
LLGVIEGVGL MFQRYAAWQA KPMAPPLPEA PSSQPLQA
