TIM9_YEAST
ID TIM9_YEAST Reviewed; 87 AA.
AC O74700; D3DLM8;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit TIM9;
GN Name=TIM9; OrderedLocusNames=YEL020W-A; ORFNames=YEL020BW;
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], PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH TIM10, AND MUTAGENESIS OF
RP SER-67.
RX PubMed=9822593; DOI=10.1093/emboj/17.22.6477;
RA Koehler C.M., Merchant S., Oppliger W., Schmid K., Jarosch E., Dolfini L.,
RA Junne T., Schatz G., Tokatlidis K.;
RT "Tim9p, an essential partner subunit of Tim10p for the import of
RT mitochondrial carrier proteins.";
RL EMBO J. 17:6477-6486(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
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 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 [5]
RP PROTEIN SEQUENCE OF 27-33 AND 74-87, FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH TIM10 AND TIM12.
RX PubMed=9889188; DOI=10.1093/emboj/18.2.313;
RA Adam A., Endres M., Sirrenberg C., Lottspeich F., Neupert W., Brunner M.;
RT "Tim9, a new component of the TIM22.54 translocase in mitochondria.";
RL EMBO J. 18:313-319(1999).
RN [6]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=14973126; DOI=10.1074/jbc.m313046200;
RA Lu H., Golovanov A.P., Alcock F., Grossmann J.G., Allen S., Lian L.-Y.,
RA Tokatlidis K.;
RT "The structural basis of the TIM10 chaperone assembly.";
RL J. Biol. Chem. 279:18959-18966(2004).
RN [7]
RP FUNCTION.
RX PubMed=10369662; DOI=10.1093/emboj/18.12.3214;
RA Endres M., Neupert W., Brunner M.;
RT "Transport of the ADP/ATP carrier of mitochondria from the TOM complex to
RT the TIM22.54 complex.";
RL EMBO J. 18:3214-3221(1999).
RN [8]
RP FUNCTION.
RX PubMed=10995434; DOI=10.1083/jcb.150.6.1271;
RA Davis A.J., Sepuri N.B., Holder J., Johnson A.E., Jensen R.E.;
RT "Two intermembrane space TIM complexes interact with different domains of
RT Tim23p during its import into mitochondria.";
RL J. Cell Biol. 150:1271-1282(2000).
RN [9]
RP FUNCTION.
RX PubMed=11483513; DOI=10.1093/emboj/20.15.4099;
RA Luciano P., Vial S., Vergnolle M.A.S., Dyall S.D., Robinson D.R.,
RA Tokatlidis K.;
RT "Functional reconstitution of the import of the yeast ADP/ATP carrier
RT mediated by the TIM10 complex.";
RL EMBO J. 20:4099-4106(2001).
RN [10]
RP FUNCTION.
RX PubMed=11509656; DOI=10.1128/mcb.21.18.6132-6138.2001;
RA Murphy M.P., Leuenberger D., Curran S.P., Oppliger W., Koehler C.M.;
RT "The essential function of the small Tim proteins in the TIM22 import
RT pathway does not depend on formation of the soluble 70-kilodalton
RT complex.";
RL Mol. Cell. Biol. 21:6132-6138(2001).
RN [11]
RP SUBUNIT, DISULFIDE BONDS, AND LACK OF ZINC-BINDING WHEN PRESENT IN THE
RP MITOCHONDRIAL INTERMEMBRANE SPACE.
RX PubMed=11867522; DOI=10.1093/emboj/21.5.942;
RA Curran S.P., Leuenberger D., Oppliger W., Koehler C.M.;
RT "The Tim9p-Tim10p complex binds to the transmembrane domains of the ADP/ATP
RT carrier.";
RL EMBO J. 21:942-953(2002).
RN [12]
RP FUNCTION, AND SUBUNIT.
RX PubMed=12138093; DOI=10.1074/jbc.m202310200;
RA Vial S., Lu H., Allen S., Savory P., Thornton D., Sheehan J.,
RA Tokatlidis K.;
RT "Assembly of Tim9 and Tim10 into a functional chaperone.";
RL J. Biol. Chem. 277:36100-36108(2002).
RN [13]
RP FUNCTION.
RX PubMed=12391147; DOI=10.1128/mcb.22.22.7780-7789.2002;
RA Truscott K.N., Wiedemann N., Rehling P., Mueller H., Meisinger C.,
RA Pfanner N., Guiard B.;
RT "Mitochondrial import of the ADP/ATP carrier: the essential TIM complex of
RT the intermembrane space is required for precursor release from the TOM
RT complex.";
RL Mol. Cell. Biol. 22:7780-7789(2002).
RN [14]
RP MUTAGENESIS OF VAL-40; GLU-52 AND SER-60.
RX PubMed=12656987; DOI=10.1034/j.1600-0854.2003.00095.x;
RA Leuenberger D., Curran S.P., Wong D., Koehler C.M.;
RT "The role of Tim9p in the assembly of the TIM22 import complexes.";
RL Traffic 4:144-152(2003).
RN [15]
RP FUNCTION IN TRANSFER OF BETA-BARREL PROTEINS.
RX PubMed=14978039; DOI=10.1074/jbc.m400050200;
RA Wiedemann N., Truscott K.N., Pfannschmidt S., Guiard B., Meisinger C.,
RA Pfanner N.;
RT "Biogenesis of the protein import channel Tom40 of the mitochondrial outer
RT membrane: intermembrane space components are involved in an early stage of
RT the assembly pathway.";
RL J. Biol. Chem. 279:18188-18194(2004).
RN [16]
RP FUNCTION.
RX PubMed=16039669; DOI=10.1016/j.jmb.2005.06.010;
RA Vergnolle M.A.S., Baud C., Golovanov A.P., Alcock F., Luciano P.,
RA Lian L.-Y., Tokatlidis K.;
RT "Distinct domains of small Tims involved in subunit interaction and
RT substrate recognition.";
RL J. Mol. Biol. 351:839-849(2005).
RN [17]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16823961; DOI=10.1021/pr050477f;
RA Reinders J., Zahedi R.P., Pfanner N., Meisinger C., Sickmann A.;
RT "Toward the complete yeast mitochondrial proteome: multidimensional
RT separation techniques for mitochondrial proteomics.";
RL J. Proteome Res. 5:1543-1554(2006).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
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 [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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: Mitochondrial intermembrane chaperone that participates in
CC the import and insertion of multi-pass transmembrane proteins into the
CC mitochondrial inner membrane. Also required for the transfer of beta-
CC barrel precursors from the TOM complex to the sorting and assembly
CC machinery (SAM complex) of the outer membrane. Acts as a chaperone-like
CC protein that protects the hydrophobic precursors from aggregation and
CC guide them through the mitochondrial intermembrane space. Compared to
CC TIM10, it may have a strong structural role.
CC {ECO:0000269|PubMed:10369662, ECO:0000269|PubMed:10995434,
CC ECO:0000269|PubMed:11483513, ECO:0000269|PubMed:11509656,
CC ECO:0000269|PubMed:12138093, ECO:0000269|PubMed:12391147,
CC ECO:0000269|PubMed:14978039, ECO:0000269|PubMed:16039669,
CC ECO:0000269|PubMed:9822593, ECO:0000269|PubMed:9889188}.
CC -!- SUBUNIT: Heterohexamer; composed of 3 copies of TIM9 and 3 copies of
CC TIM10, named soluble 70 kDa complex. Associates with the TIM12
CC component of the TIM22 complex, whose core is composed of TIM18, TIM22
CC and TIM54. Interacts with the transmembrane regions of multi-pass
CC transmembrane proteins in transit. {ECO:0000269|PubMed:11867522,
CC ECO:0000269|PubMed:12138093, ECO:0000269|PubMed:9822593,
CC ECO:0000269|PubMed:9889188}.
CC -!- INTERACTION:
CC O74700; P87108: TIM10; NbExp=7; IntAct=EBI-9108, EBI-9115;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:9822593,
CC ECO:0000269|PubMed:9889188}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:9822593,
CC ECO:0000269|PubMed:9889188}; Intermembrane side
CC {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:9822593,
CC ECO:0000269|PubMed:9889188}. Mitochondrion intermembrane space
CC {ECO:0000269|PubMed:22984289}.
CC -!- DOMAIN: The twin CX3C motif contains 4 conserved Cys residues that form
CC 2 disulfide bonds in the mitochondrial intermembrane space. However,
CC during the transit of TIM9 from cytoplasm into mitochondrion, the Cys
CC residues probably coordinate zinc, thereby preventing folding and
CC allowing its transfer across mitochondrial outer membrane (Probable).
CC {ECO:0000305|PubMed:11867522}.
CC -!- SIMILARITY: Belongs to the small Tim family. {ECO:0000305}.
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DR EMBL; U18530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF093244; AAC83169.1; -; Genomic_DNA.
DR EMBL; AY557798; AAS56124.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07632.1; -; Genomic_DNA.
DR PIR; S78717; S78717.
DR RefSeq; NP_010894.1; NM_001184349.1.
DR PDB; 3DXR; X-ray; 2.50 A; A=1-87.
DR PDB; 6LO8; EM; 3.83 A; E/G/I=1-87.
DR PDBsum; 3DXR; -.
DR PDBsum; 6LO8; -.
DR AlphaFoldDB; O74700; -.
DR SASBDB; O74700; -.
DR SMR; O74700; -.
DR BioGRID; 36709; 21.
DR ComplexPortal; CPX-1629; TIM22 mitochondrial inner membrane twin-pore carrier translocase complex.
DR ComplexPortal; CPX-2268; TIM9-TIM10 mitochondrial intermembrane space protein transporter complex.
DR ComplexPortal; CPX-2950; TIM9-TIM10-TIM12 mitochondrial intermembrane space protein transporter complex.
DR DIP; DIP-5806N; -.
DR IntAct; O74700; 3.
DR MINT; O74700; -.
DR STRING; 4932.YEL020W-A; -.
DR TCDB; 3.A.8.1.1; the mitochondrial protein translocase (mpt) family.
DR iPTMnet; O74700; -.
DR MaxQB; O74700; -.
DR PaxDb; O74700; -.
DR PRIDE; O74700; -.
DR EnsemblFungi; YEL020W-A_mRNA; YEL020W-A; YEL020W-A.
DR GeneID; 856693; -.
DR KEGG; sce:YEL020W-A; -.
DR SGD; S000007256; TIM9.
DR VEuPathDB; FungiDB:YEL020W-A; -.
DR eggNOG; KOG3479; Eukaryota.
DR HOGENOM; CLU_141397_3_0_1; -.
DR InParanoid; O74700; -.
DR OMA; QDFLRMY; -.
DR BioCyc; YEAST:G3O-30387-MON; -.
DR Reactome; R-SCE-1268020; Mitochondrial protein import.
DR EvolutionaryTrace; O74700; -.
DR PRO; PR:O74700; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; O74700; protein.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:ComplexPortal.
DR GO; GO:0042719; C:mitochondrial intermembrane space protein transporter complex; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:ComplexPortal.
DR GO; GO:0042721; C:TIM22 mitochondrial import inner membrane insertion complex; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140318; F:protein transporter activity; IDA:SGD.
DR GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IDA:SGD.
DR Gene3D; 1.10.287.810; -; 1.
DR InterPro; IPR004217; Tim10-like.
DR InterPro; IPR035427; Tim10-like_dom_sf.
DR Pfam; PF02953; zf-Tim10_DDP; 1.
DR SUPFAM; SSF144122; SSF144122; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chaperone; Direct protein sequencing;
KW Disulfide bond; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Protein transport; Reference proteome;
KW Translocation; Transport; Zinc.
FT CHAIN 1..87
FT /note="Mitochondrial import inner membrane translocase
FT subunit TIM9"
FT /id="PRO_0000193610"
FT MOTIF 35..59
FT /note="Twin CX3C motif"
FT /evidence="ECO:0000305|PubMed:11867522"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT DISULFID 35..59
FT /evidence="ECO:0000305|PubMed:11867522"
FT DISULFID 39..55
FT /evidence="ECO:0000305|PubMed:11867522"
FT MUTAGEN 40
FT /note="V->A: In tim9-3; impairs the import of mitochondrial
FT carrier proteins into mitochondria; when associated with P-
FT 60."
FT /evidence="ECO:0000269|PubMed:12656987"
FT MUTAGEN 52
FT /note="E->G: In tim9-19; impairs the import of
FT mitochondrial carrier proteins into mitochondria."
FT /evidence="ECO:0000269|PubMed:12656987"
FT MUTAGEN 60
FT /note="S->P: In tim9-3; impairs the import of mitochondrial
FT carrier proteins into mitochondria; when associated with A-
FT 40."
FT /evidence="ECO:0000269|PubMed:12656987"
FT MUTAGEN 67
FT /note="S->C: Impairs the import of mitochondrial carrier
FT proteins into mitochondria."
FT /evidence="ECO:0000269|PubMed:9822593"
FT HELIX 14..39
FT /evidence="ECO:0007829|PDB:3DXR"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:3DXR"
FT HELIX 50..76
FT /evidence="ECO:0007829|PDB:3DXR"
SQ SEQUENCE 87 AA; 10202 MW; 5160E5DBA52065C7 CRC64;
MDALNSKEQQ EFQKVVEQKQ MKDFMRLYSN LVERCFTDCV NDFTTSKLTN KEQTCIMKCS
EKFLKHSERV GQRFQEQNAA LGQGLGR
