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Protein

Mitochondrial import inner membrane translocase subunit TIM13

Gene

TIM13

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 some 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. The TIM8-TIM13 complex is non essential and only mediates the import of few proteins under precise conditions while the predominant TIM9-TIM10 70 kDa complex is crucial and mediates the import of much more proteins. Strictly required for import of TIM23 in some conditions, when a low membrane potential exists in the mitochondria.5 Publications

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • protein transporter activity 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-30873-MONOMER.
ReactomeiREACT_334110. 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 TIM13
Gene namesi
Name:TIM13
Ordered Locus Names:YGR181W
ORF Names:G7157
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VII

Organism-specific databases

CYGDiYGR181w.
EuPathDBiFungiDB:YGR181W.
SGDiS000003413. TIM13.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: UniProtKB-SubCell
  • mitochondrial intermembrane space Source: SGD
  • mitochondrial intermembrane space protein transporter complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi57 – 571C → S: Abolishes import into mitochondrion; when associated with S-61. 1 Publication
Mutagenesisi61 – 611C → S: Abolishes import into mitochondrion; when associated with S-57. 1 Publication
Mutagenesisi73 – 731C → S: Abolishes import into mitochondrion; when associated with S-77. 1 Publication
Mutagenesisi77 – 771C → S: Abolishes import into mitochondrion; when associated with S-73. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 105105Mitochondrial import inner membrane translocase subunit TIM13PRO_0000193632Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi57 ↔ 77Curated
Disulfide bondi61 ↔ 73Curated

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP53299.
PaxDbiP53299.
PeptideAtlasiP53299.

Interactioni

Subunit structurei

Heterohexamer; composed of 3 copies of TIM8 and 3 copies of TIM13, named soluble 70 kDa complex. Associates with the TIM22 complex, whose core is composed of TIM18, TIM22 and TIM54. Interacts with the transmembrane regions of multi-pass transmembrane proteins in transit.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TIM8P577444EBI-9121,EBI-9013892

Protein-protein interaction databases

BioGridi33434. 92 interactions.
DIPiDIP-5547N.
IntActiP53299. 6 interactions.
MINTiMINT-563654.

Structurei

Secondary structure

1
105
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi47 – 6115Combined sources
Helixi71 – 9323Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CJHX-ray2.60A/C/E/G/I/K42-105[»]
ProteinModelPortaliP53299.
SMRiP53299. Positions 46-99.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53299.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi57 – 7721Twin 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 TIM13 from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane.1 Publication

Sequence similaritiesi

Belongs to the small Tim family.Curated

Phylogenomic databases

eggNOGiNOG246901.
GeneTreeiENSGT00390000014000.
HOGENOMiHOG000115759.
InParanoidiP53299.
KOiK17781.
OMAiRTYIARI.
OrthoDBiEOG751NV3.

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.

P53299-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLSSIFGGG APSQQKEAAT TAKTTPNPIA KELKNQIAQE LAVANATELV
60 70 80 90 100
NKISENCFEK CLTSPYATRN DACIDQCLAK YMRSWNVISK AYISRIQNAS

ASGEI
Length:105
Mass (Da):11,286
Last modified:October 1, 1996 - v1
Checksum:iB1DDFE87AFDC52A3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99074 Genomic DNA. Translation: CAA67526.1.
Z72966 Genomic DNA. Translation: CAA97207.1.
AY558508 Genomic DNA. Translation: AAS56834.1.
BK006941 Genomic DNA. Translation: DAA08276.1.
PIRiS64495.
RefSeqiNP_011697.3. NM_001181310.3.

Genome annotation databases

EnsemblFungiiYGR181W; YGR181W; YGR181W.
GeneIDi853093.
KEGGisce:YGR181W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99074 Genomic DNA. Translation: CAA67526.1.
Z72966 Genomic DNA. Translation: CAA97207.1.
AY558508 Genomic DNA. Translation: AAS56834.1.
BK006941 Genomic DNA. Translation: DAA08276.1.
PIRiS64495.
RefSeqiNP_011697.3. NM_001181310.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CJHX-ray2.60A/C/E/G/I/K42-105[»]
ProteinModelPortaliP53299.
SMRiP53299. Positions 46-99.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33434. 92 interactions.
DIPiDIP-5547N.
IntActiP53299. 6 interactions.
MINTiMINT-563654.

Protein family/group databases

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

Proteomic databases

MaxQBiP53299.
PaxDbiP53299.
PeptideAtlasiP53299.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR181W; YGR181W; YGR181W.
GeneIDi853093.
KEGGisce:YGR181W.

Organism-specific databases

CYGDiYGR181w.
EuPathDBiFungiDB:YGR181W.
SGDiS000003413. TIM13.

Phylogenomic databases

eggNOGiNOG246901.
GeneTreeiENSGT00390000014000.
HOGENOMiHOG000115759.
InParanoidiP53299.
KOiK17781.
OMAiRTYIARI.
OrthoDBiEOG751NV3.

Enzyme and pathway databases

BioCyciYEAST:G3O-30873-MONOMER.
ReactomeiREACT_334110. Mitochondrial protein import.

Miscellaneous databases

EvolutionaryTraceiP53299.
NextBioi973081.
PROiP53299.

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. "DNA sequence analysis of a 23,002 bp DNA fragment of the right arm of Saccharomyces cerevisiae chromosome VII."
    Arroyo J., Garcia-Gonzalez M., Garcia-Saez M.I., Sanchez-Perez M., Nombela C.
    Yeast 13:357-363(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    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. "Different import pathways through the mitochondrial intermembrane space for inner membrane proteins."
    Leuenberger D., Bally N.A., Schatz G., Koehler C.M.
    EMBO J. 18:4816-4822(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH THE TIM22 COMPLEX.
  6. "The role of the TIM8-13 complex in the import of Tim23 into mitochondria."
    Paschen S.A., Rothbauer U., Kaldi K., Bauer M.F., Neupert W., Brunner M.
    EMBO J. 19:6392-6400(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "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.
  8. "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.
  9. "The role of the Tim8p-Tim13p complex in a conserved import pathway for mitochondrial polytopic inner membrane proteins."
    Curran S.P., Leuenberger D., Schmidt E., Koehler C.M.
    J. Cell Biol. 158:1017-1027(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, PROBABLE DISULFIDE BONDS, LACK OF ZINC-BINDING WHEN PRESENT IN THE MITOCHONDRIAL INTERMEMBRANE SPACE.
  10. "Import of small Tim proteins into the mitochondrial intermembrane space."
    Lutz T., Neupert W., Herrmann J.M.
    EMBO J. 22:4400-4408(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ZINC-BINDING WHEN PRESENT IN THE CYTOSOL, DOMAIN, MUTAGENESIS OF CYS-57; CYS-61; CYS-73 AND CYS-77.

Entry informationi

Entry nameiTIM13_YEAST
AccessioniPrimary (citable) accession number: P53299
Secondary accession number(s): D6VUW5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 22, 2015
This is version 126 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, 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 VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3

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 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.