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Protein

Mitochondrial import inner membrane translocase subunit TIM9

Gene

TIM9

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. Compared to TIM10, it may have a strong structural role.10 Publications

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • protein transporter activity Source: SGD
  • unfolded protein binding Source: SGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Protein transport, Translocation, Transport

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-30387-MONOMER.
ReactomeiR-SCE-1268020. Mitochondrial protein import.

Protein family/group databases

TCDBi3.A.8.1.1. the mitochondrial protein translocase (mpt) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial import inner membrane translocase subunit TIM9
Gene namesi
Name:TIM9
Ordered Locus Names:YEL020W-A
ORF Names:YEL020BW
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YEL020W-A.
SGDiS000007256. TIM9.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi40 – 401V → A in tim9-3; impairs the import of mitochondrial carrier proteins into mitochondria; when associated with P-60. 1 Publication
Mutagenesisi52 – 521E → G in tim9-19; impairs the import of mitochondrial carrier proteins into mitochondria. 1 Publication
Mutagenesisi60 – 601S → P in tim9-3; impairs the import of mitochondrial carrier proteins into mitochondria; when associated with A-40. 1 Publication
Mutagenesisi67 – 671S → C: Impairs the import of mitochondrial carrier proteins into mitochondria. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8787Mitochondrial import inner membrane translocase subunit TIM9PRO_0000193610Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Disulfide bondi35 ↔ 591 Publication
Disulfide bondi39 ↔ 551 Publication

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

MaxQBiO74700.
PeptideAtlasiO74700.

Interactioni

Subunit structurei

Heterohexamer; composed of 3 copies of TIM9 and 3 copies of TIM10, named soluble 70 kDa complex. Associates with the TIM12 component of the TIM22 complex, whose core is composed of TIM18, TIM22 and TIM54. Interacts with the transmembrane regions of multi-pass transmembrane proteins in transit.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TIM10P871087EBI-9108,EBI-9115

GO - Molecular functioni

  • unfolded protein binding Source: SGD

Protein-protein interaction databases

BioGridi36709. 15 interactions.
DIPiDIP-5806N.
IntActiO74700. 3 interactions.
MINTiMINT-4987906.

Structurei

Secondary structure

1
87
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 3926Combined sources
Beta strandi44 – 474Combined sources
Helixi50 – 7627Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DXRX-ray2.50A1-87[»]
ProteinModelPortaliO74700.
SMRiO74700. Positions 12-80.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO74700.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi35 – 5925Twin CX3C motifAdd
BLAST

Domaini

The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space. However, during the transit of TIM9 from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane (Probable).Curated

Sequence similaritiesi

Belongs to the small Tim family.Curated

Phylogenomic databases

GeneTreeiENSGT00450000040278.
HOGENOMiHOG000185786.
InParanoidiO74700.
KOiK17777.
OMAiSNLVERC.
OrthoDBiEOG77DJK9.

Family and domain databases

Gene3Di1.10.287.810. 1 hit.
InterProiIPR004217. Tim10/DDP_fam_Znf.
[Graphical view]
PfamiPF02953. zf-Tim10_DDP. 1 hit.
[Graphical view]
SUPFAMiSSF144122. SSF144122. 1 hit.

Sequencei

Sequence statusi: Complete.

O74700-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDALNSKEQQ EFQKVVEQKQ MKDFMRLYSN LVERCFTDCV NDFTTSKLTN
60 70 80
KEQTCIMKCS EKFLKHSERV GQRFQEQNAA LGQGLGR
Length:87
Mass (Da):10,202
Last modified:November 1, 1998 - v1
Checksum:i5160E5DBA52065C7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18530 Genomic DNA. No translation available.
AF093244 Genomic DNA. Translation: AAC83169.1.
AY557798 Genomic DNA. Translation: AAS56124.1.
BK006939 Genomic DNA. Translation: DAA07632.1.
PIRiS78717.
RefSeqiNP_010894.1. NM_001184349.1.

Genome annotation databases

EnsemblFungiiYEL020W-A; YEL020W-A; YEL020W-A.
GeneIDi856693.
KEGGisce:YEL020W-A.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18530 Genomic DNA. No translation available.
AF093244 Genomic DNA. Translation: AAC83169.1.
AY557798 Genomic DNA. Translation: AAS56124.1.
BK006939 Genomic DNA. Translation: DAA07632.1.
PIRiS78717.
RefSeqiNP_010894.1. NM_001184349.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DXRX-ray2.50A1-87[»]
ProteinModelPortaliO74700.
SMRiO74700. Positions 12-80.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36709. 15 interactions.
DIPiDIP-5806N.
IntActiO74700. 3 interactions.
MINTiMINT-4987906.

Protein family/group databases

TCDBi3.A.8.1.1. the mitochondrial protein translocase (mpt) family.

Proteomic databases

MaxQBiO74700.
PeptideAtlasiO74700.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYEL020W-A; YEL020W-A; YEL020W-A.
GeneIDi856693.
KEGGisce:YEL020W-A.

Organism-specific databases

EuPathDBiFungiDB:YEL020W-A.
SGDiS000007256. TIM9.

Phylogenomic databases

GeneTreeiENSGT00450000040278.
HOGENOMiHOG000185786.
InParanoidiO74700.
KOiK17777.
OMAiSNLVERC.
OrthoDBiEOG77DJK9.

Enzyme and pathway databases

BioCyciYEAST:G3O-30387-MONOMER.
ReactomeiR-SCE-1268020. Mitochondrial protein import.

Miscellaneous databases

EvolutionaryTraceiO74700.
PROiO74700.

Family and domain databases

Gene3Di1.10.287.810. 1 hit.
InterProiIPR004217. Tim10/DDP_fam_Znf.
[Graphical view]
PfamiPF02953. zf-Tim10_DDP. 1 hit.
[Graphical view]
SUPFAMiSSF144122. SSF144122. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Tim9p, an essential partner subunit of Tim10p for the import of mitochondrial carrier proteins."
    Koehler C.M., Merchant S., Oppliger W., Schmid K., Jarosch E., Dolfini L., Junne T., Schatz G., Tokatlidis K.
    EMBO J. 17:6477-6486(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH TIM10, MUTAGENESIS OF SER-67.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Tim9, a new component of the TIM22.54 translocase in mitochondria."
    Adam A., Endres M., Sirrenberg C., Lottspeich F., Neupert W., Brunner M.
    EMBO J. 18:313-319(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-33 AND 74-87, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH TIM10 AND TIM12.
  6. Cited for: PARTIAL PROTEIN SEQUENCE.
  7. "Transport of the ADP/ATP carrier of mitochondria from the TOM complex to the TIM22.54 complex."
    Endres M., Neupert W., Brunner M.
    EMBO J. 18:3214-3221(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Two intermembrane space TIM complexes interact with different domains of Tim23p during its import into mitochondria."
    Davis A.J., Sepuri N.B., Holder J., Johnson A.E., Jensen R.E.
    J. Cell Biol. 150:1271-1282(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Functional reconstitution of the import of the yeast ADP/ATP carrier mediated by the TIM10 complex."
    Luciano P., Vial S., Vergnolle M.A.S., Dyall S.D., Robinson D.R., Tokatlidis K.
    EMBO J. 20:4099-4106(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "The essential function of the small Tim proteins in the TIM22 import pathway does not depend on formation of the soluble 70-kilodalton complex."
    Murphy M.P., Leuenberger D., Curran S.P., Oppliger W., Koehler C.M.
    Mol. Cell. Biol. 21:6132-6138(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "The Tim9p-Tim10p complex binds to the transmembrane domains of the ADP/ATP carrier."
    Curran S.P., Leuenberger D., Oppliger W., Koehler C.M.
    EMBO J. 21:942-953(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, DISULFIDE BONDS, LACK OF ZINC-BINDING WHEN PRESENT IN THE MITOCHONDRIAL INTERMEMBRANE SPACE.
  12. Cited for: FUNCTION, SUBUNIT.
  13. "Mitochondrial import of the ADP/ATP carrier: the essential TIM complex of the intermembrane space is required for precursor release from the TOM complex."
    Truscott K.N., Wiedemann N., Rehling P., Mueller H., Meisinger C., Pfanner N., Guiard B.
    Mol. Cell. Biol. 22:7780-7789(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "The role of Tim9p in the assembly of the TIM22 import complexes."
    Leuenberger D., Curran S.P., Wong D., Koehler C.M.
    Traffic 4:144-152(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF VAL-40; GLU-52 AND SER-60.
  15. "Biogenesis of the protein import channel Tom40 of the mitochondrial outer membrane: intermembrane space components are involved in an early stage of the assembly pathway."
    Wiedemann N., Truscott K.N., Pfannschmidt S., Guiard B., Meisinger C., Pfanner N.
    J. Biol. Chem. 279:18188-18194(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRANSFER OF BETA-BARREL PROTEINS.
  16. "Distinct domains of small Tims involved in subunit interaction and substrate recognition."
    Vergnolle M.A.S., Baud C., Golovanov A.P., Alcock F., Luciano P., Lian L.-Y., Tokatlidis K.
    J. Mol. Biol. 351:839-849(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTIM9_YEAST
AccessioniPrimary (citable) accession number: O74700
Secondary accession number(s): D3DLM8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 1998
Last modified: June 8, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.