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Protein

Mitochondrial import inner membrane translocase subunit TIM10

Gene

TIM10

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 TIM9, it may function as a substrate sensor.13 Publications

GO - Molecular functioni

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

GO - Biological processi

  • protein import into mitochondrial inner membrane Source: SGD
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-31244-MONOMER.

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 TIM10
Alternative name(s):
Mitochondrial intermembrane protein MRS11
Gene namesi
Name:TIM10
Synonyms:MRS11
Ordered Locus Names:YHR005C-A
ORF Names:YHR005BC
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VIII

Organism-specific databases

EuPathDBiFungiDB:YHR005C-A.
SGDiS000003530. TIM10.

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 – 401C → S: Induces impairment in folding and loss of zinc-binding. 2 Publications
Mutagenesisi44 – 441C → S: Loss of function due to severely affected folding and the presence of non-native disulfide bonds; loss of zinc-binding. 2 Publications
Mutagenesisi61 – 611C → S: Loss of function due to severely affected folding and the presence of non-native disulfide bonds; loss of zinc-binding. 2 Publications
Mutagenesisi65 – 651C → S: Induces impairment in folding and loss of zinc-binding. 2 Publications

Chemistry

ChEMBLiCHEMBL1741194.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9393Mitochondrial import inner membrane translocase subunit TIM10PRO_0000193622Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi40 ↔ 65
Disulfide bondi44 ↔ 61

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP87108.
PeptideAtlasiP87108.

PTM databases

iPTMnetiP87108.

Interactioni

Subunit structurei

Heterohexamer; composed of 3 copies of TIM9 and 3 copies of TIM10, named soluble 70 kDa complex. Associates directly 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.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TIM12P328302EBI-9115,EBI-11303
TIM18Q087492EBI-9115,EBI-30499
TIM9O747007EBI-9115,EBI-9108

GO - Molecular functioni

  • unfolded protein binding Source: SGD

Protein-protein interaction databases

BioGridi36431. 24 interactions.
DIPiDIP-1141N.
IntActiP87108. 4 interactions.
MINTiMINT-4987878.

Chemistry

BindingDBiP87108.

Structurei

Secondary structure

1
93
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni16 – 194Combined sources
Helixi20 – 4425Combined sources
Helixi56 – 8227Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DXRX-ray2.50B1-93[»]
ProteinModelPortaliP87108.
SMRiP87108. Positions 15-83.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP87108.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 3131Interaction with transmembrane regions of transmembrane proteins in transitAdd
BLAST
Regioni73 – 9321Required for heterohexamerizationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi40 – 6526Twin 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 TIM10 from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane.

Sequence similaritiesi

Belongs to the small Tim family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000003068.
HOGENOMiHOG000211421.
InParanoidiP87108.
KOiK17778.
OMAiMDPMKAQ.
OrthoDBiEOG7VHT9C.

Family and domain databases

Gene3Di1.10.287.810. 1 hit.
InterProiIPR027100. Tim10.
IPR004217. Tim10/DDP_fam_Znf.
IPR027247. Tim10/Tim12.
[Graphical view]
PANTHERiPTHR11038. PTHR11038. 1 hit.
PTHR11038:SF16. PTHR11038:SF16. 1 hit.
PfamiPF02953. zf-Tim10_DDP. 1 hit.
[Graphical view]
SUPFAMiSSF144122. SSF144122. 1 hit.

Sequencei

Sequence statusi: Complete.

P87108-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFLGFGGGQ PQLSSQQKIQ AAEAELDLVT DMFNKLVNNC YKKCINTSYS
60 70 80 90
EGELNKNESS CLDRCVAKYF ETNVQVGENM QKMGQSFNAA GKF
Length:93
Mass (Da):10,305
Last modified:July 1, 1997 - v1
Checksum:i70DD4764B944FF17
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z80875 Genomic DNA. Translation: CAB02581.1.
U10555 Genomic DNA. Translation: AAB68435.1.
BK006934 Genomic DNA. Translation: DAA06693.1.
PIRiS72314.
RefSeqiNP_011869.1. NM_001181427.1.

Genome annotation databases

EnsemblFungiiYHR005C-A; YHR005C-A; YHR005C-A.
GeneIDi856395.
KEGGisce:YHR005C-A.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z80875 Genomic DNA. Translation: CAB02581.1.
U10555 Genomic DNA. Translation: AAB68435.1.
BK006934 Genomic DNA. Translation: DAA06693.1.
PIRiS72314.
RefSeqiNP_011869.1. NM_001181427.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DXRX-ray2.50B1-93[»]
ProteinModelPortaliP87108.
SMRiP87108. Positions 15-83.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36431. 24 interactions.
DIPiDIP-1141N.
IntActiP87108. 4 interactions.
MINTiMINT-4987878.

Chemistry

BindingDBiP87108.
ChEMBLiCHEMBL1741194.

Protein family/group databases

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

PTM databases

iPTMnetiP87108.

Proteomic databases

MaxQBiP87108.
PeptideAtlasiP87108.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYHR005C-A; YHR005C-A; YHR005C-A.
GeneIDi856395.
KEGGisce:YHR005C-A.

Organism-specific databases

EuPathDBiFungiDB:YHR005C-A.
SGDiS000003530. TIM10.

Phylogenomic databases

GeneTreeiENSGT00390000003068.
HOGENOMiHOG000211421.
InParanoidiP87108.
KOiK17778.
OMAiMDPMKAQ.
OrthoDBiEOG7VHT9C.

Enzyme and pathway databases

BioCyciYEAST:G3O-31244-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP87108.
NextBioi981917.
PROiP87108.

Family and domain databases

Gene3Di1.10.287.810. 1 hit.
InterProiIPR027100. Tim10.
IPR004217. Tim10/DDP_fam_Znf.
IPR027247. Tim10/Tim12.
[Graphical view]
PANTHERiPTHR11038. PTHR11038. 1 hit.
PTHR11038:SF16. PTHR11038:SF16. 1 hit.
PfamiPF02953. zf-Tim10_DDP. 1 hit.
[Graphical view]
SUPFAMiSSF144122. SSF144122. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A soluble 12-kDa protein of the mitochondrial intermembrane space, Mrs11p, is essential for mitochondrial biogenesis and viability of yeast cells."
    Jarosch E., Rodel G., Schweyen R.J.
    Mol. Gen. Genet. 255:157-165(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
    Strain: ATCC 44774 / DBY747.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "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: PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT.
  5. Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, ZINC-BINDING WHEN PRESENT IN THE CYTOSOL, MUTAGENESIS OF CYS-40; CYS-44; CYS-61 AND CYS-65.
  6. "Import of carrier proteins into the mitochondrial inner membrane mediated by Tim22."
    Sirrenberg C., Bauer M.D., Guiard B., Neupert W., Brunner M.
    Nature 384:582-585(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ZINC-BINDING, SUBCELLULAR LOCATION, INTERACTION WITH TIM12 AND TIM22.
  7. "Import of mitochondrial carriers mediated by essential proteins of the intermembrane space."
    Koehler C.M., Jarosch E., Tokatlidis K., Schmid K., Schweyen R.J., Schatz G.
    Science 279:369-373(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TIM12 AND TIM22.
  8. "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: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH TIM9 AND TIM12.
  9. "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.
  10. "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.
  11. "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.
  12. "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.
  13. "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.
  14. Cited for: FUNCTION, SUBUNIT.
  15. "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.
  16. "Protein insertion into the mitochondrial inner membrane by a twin-pore translocase."
    Rehling P., Model K., Brandner K., Kovermann P., Sickmann A., Meyer H.E., Kuehlbrandt W., Wagner R., Truscott K.N., Pfanner N.
    Science 299:1747-1751(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE TIM22 COMPLEX WITH TIM12; TIM18; TIM22 AND TIM54.
  17. "Juxtaposition of the two distal CX3C motifs via intrachain disulfide bonding is essential for the folding of Tim10."
    Allen S., Lu H., Thornton D., Tokatlidis K.
    J. Biol. Chem. 278:38505-38513(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS, MUTAGENESIS OF CYS-40; CYS-44; CYS-61 AND CYS-65.
  18. "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.
  19. "Functional TIM10 chaperone assembly is redox-regulated in vivo."
    Lu H., Allen S., Wardleworth L., Savory P., Tokatlidis K.
    J. Biol. Chem. 279:18952-18958(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  20. "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.
  21. "Zinc binding stabilizes mitochondrial Tim10 in a reduced and import-competent state kinetically."
    Lu H., Woodburn J.
    J. Mol. Biol. 353:897-910(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ZINC-BINDING.

Entry informationi

Entry nameiTIM10_YEAST
AccessioniPrimary (citable) accession number: P87108
Secondary accession number(s): D3DKU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: July 1, 1997
Last modified: May 11, 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 VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: 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.