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Protein

Mitochondrial import inner membrane translocase subunit Tim10

Gene

Timm10

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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. May also be 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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Protein transport, Translocation, Transport

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial import inner membrane translocase subunit Tim10
Gene namesi
Name:Timm10
Synonyms:Tim10
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1353429. Timm10.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: MGI
  • mitochondrial intermembrane space protein transporter complex Source: BHF-UCL
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9090Mitochondrial import inner membrane translocase subunit Tim10PRO_0000193613Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi29 ↔ 54By similarity
Disulfide bondi33 ↔ 50By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiP62073.
MaxQBiP62073.
PaxDbiP62073.
PeptideAtlasiP62073.
PRIDEiP62073.

PTM databases

iPTMnetiP62073.
PhosphoSiteiP62073.

Expressioni

Gene expression databases

BgeeiP62073.
GenevisibleiP62073. MM.

Interactioni

Subunit structurei

Heterohexamer; composed of 3 copies of TIMM9 and 3 copies of TIMM10/TIM10A, named soluble 70 kDa complex. The complex forms a 6-bladed alpha-propeller structure and associates with the TIMM22 component of the TIM22 complex. Interacts with multi-pass transmembrane proteins in transit. Also forms a complex composed of TIMM9, TIMM10/TIM10A and FXC1/TIM10B (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiP62073. 1 interaction.
STRINGi10090.ENSMUSP00000028470.

Structurei

3D structure databases

ProteinModelPortaliP62073.
SMRiP62073. Positions 1-90.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi29 – 5426Twin 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 TIMM10 from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane (By similarity).By similarity

Sequence similaritiesi

Belongs to the small Tim family.Curated

Phylogenomic databases

eggNOGiKOG3480. Eukaryota.
ENOG4112539. LUCA.
GeneTreeiENSGT00390000003068.
HOGENOMiHOG000211421.
HOVERGENiHBG055029.
InParanoidiP62073.
KOiK17778.
OMAiMDPMKAQ.
OrthoDBiEOG7N37GD.
PhylomeDBiP62073.
TreeFamiTF106193.

Family and domain databases

Gene3Di1.10.287.810. 1 hit.
InterProiIPR004217. Tim10/DDP_fam_Znf.
IPR027247. Tim10/Tim12.
[Graphical view]
PANTHERiPTHR11038. PTHR11038. 1 hit.
PfamiPF02953. zf-Tim10_DDP. 1 hit.
[Graphical view]
SUPFAMiSSF144122. SSF144122. 1 hit.

Sequencei

Sequence statusi: Complete.

P62073-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPLRAQQLA AELEVEMMAD MYNRMTSACH RKCVPPHYKE AELSKGESVC
60 70 80 90
LDRCVSKYLD IHERMGKKLT ELSMQDEELM KRVQQSSGPA
Length:90
Mass (Da):10,333
Last modified:June 21, 2004 - v1
Checksum:iD20EFAE694D14BAB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 132EL → DV in AAD39996 (PubMed:10611480).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF150090 mRNA. Translation: AAD39996.1.
AK008088 mRNA. Translation: BAB25452.1.
BC031448 mRNA. Translation: AAH31448.1.
CCDSiCCDS38161.1.
RefSeqiNP_038927.2. NM_013899.2.
UniGeneiMm.21826.

Genome annotation databases

EnsembliENSMUST00000028470; ENSMUSP00000028470; ENSMUSG00000027076.
ENSMUST00000111631; ENSMUSP00000107258; ENSMUSG00000027076.
GeneIDi30059.
KEGGimmu:30059.
UCSCiuc008kjh.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF150090 mRNA. Translation: AAD39996.1.
AK008088 mRNA. Translation: BAB25452.1.
BC031448 mRNA. Translation: AAH31448.1.
CCDSiCCDS38161.1.
RefSeqiNP_038927.2. NM_013899.2.
UniGeneiMm.21826.

3D structure databases

ProteinModelPortaliP62073.
SMRiP62073. Positions 1-90.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP62073. 1 interaction.
STRINGi10090.ENSMUSP00000028470.

PTM databases

iPTMnetiP62073.
PhosphoSiteiP62073.

Proteomic databases

EPDiP62073.
MaxQBiP62073.
PaxDbiP62073.
PeptideAtlasiP62073.
PRIDEiP62073.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028470; ENSMUSP00000028470; ENSMUSG00000027076.
ENSMUST00000111631; ENSMUSP00000107258; ENSMUSG00000027076.
GeneIDi30059.
KEGGimmu:30059.
UCSCiuc008kjh.2. mouse.

Organism-specific databases

CTDi26519.
MGIiMGI:1353429. Timm10.

Phylogenomic databases

eggNOGiKOG3480. Eukaryota.
ENOG4112539. LUCA.
GeneTreeiENSGT00390000003068.
HOGENOMiHOG000211421.
HOVERGENiHBG055029.
InParanoidiP62073.
KOiK17778.
OMAiMDPMKAQ.
OrthoDBiEOG7N37GD.
PhylomeDBiP62073.
TreeFamiTF106193.

Miscellaneous databases

PROiP62073.
SOURCEiSearch...

Gene expression databases

BgeeiP62073.
GenevisibleiP62073. MM.

Family and domain databases

Gene3Di1.10.287.810. 1 hit.
InterProiIPR004217. Tim10/DDP_fam_Znf.
IPR027247. Tim10/Tim12.
[Graphical view]
PANTHERiPTHR11038. PTHR11038. 1 hit.
PfamiPF02953. zf-Tim10_DDP. 1 hit.
[Graphical view]
SUPFAMiSSF144122. SSF144122. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The mitochondrial TIM22 preprotein translocase is highly conserved throughout the eukaryotic kingdom."
    Bauer M.F., Rothbauer U., Muehlenbein N., Smith R.J.H., Gerbitz K.-D., Neupert W., Brunner M., Hofmann S.
    FEBS Lett. 464:41-47(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Small intestine.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary tumor.
  4. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 46-53 AND 68-82, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart and Kidney.

Entry informationi

Entry nameiTIM10_MOUSE
AccessioniPrimary (citable) accession number: P62073
Secondary accession number(s): Q9WV99, Q9WVA0, Q9Y5J8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: June 21, 2004
Last modified: July 6, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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.