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Q9WVA2 (TIM8A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitochondrial import inner membrane translocase subunit Tim8 A
Alternative name(s):
Deafness dystonia protein 1 homolog
Gene names
Name:Timm8a1
Synonyms:Ddp1, Tim8a, Timm8a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length97 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 TIMM8-TIMM13 complex mediates the import of proteins such as TIMM23, SLC25A12/ARALAR1 and SLC25A13/ARALAR2, while the predominant TIMM9-TIMM10 70 kDa complex mediates the import of much more proteins By similarity.

Subunit structure

Heterohexamer; composed of 3 copies of TIMM8A and 3 copies of TIMM13, named soluble 70 kDa complex. Associates with the TIM22 complex, whose core is composed of TIMM22 By similarity.

Subcellular location

Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side By similarity.

Tissue specificity

Present at high level in liver and brain, and at lower level in muscle and heart. In CNS sections, it is predominantly present in the soma and the dendritic portion of the Purkinje cells of the cerebellum, but not in the glial cells. Scattered expression also is also detected in the brain stem, olfactory bulb, substantia nigra, hippocampus and striatum (at protein level). Ubiquitously expressed. Ref.2 Ref.5

Domain

The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space. However, during the transit of TIMM8A from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane By similarity.

Sequence similarities

Belongs to the small Tim family.

Ontologies

Keywords
   Biological processProtein transport
Translocation
Transport
   Cellular componentMembrane
Mitochondrion
Mitochondrion inner membrane
   LigandMetal-binding
Zinc
   Molecular functionChaperone
   PTMDisulfide bond
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmitochondrial inner membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 9797Mitochondrial import inner membrane translocase subunit Tim8 A
PRO_0000193585

Regions

Motif43 – 6624Twin CX3C motif

Amino acid modifications

Modified residue871Phosphoserine Ref.6
Modified residue941Phosphoserine By similarity
Modified residue961Phosphoserine Ref.6
Disulfide bond43 ↔ 66 By similarity
Disulfide bond47 ↔ 62 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9WVA2 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 16C23D7C351BDF00

FASTA9711,042
        10         20         30         40         50         60 
MESSTSSSGS ALGAVDPQLQ HFIEVETQKQ RFQQLVHQMT ELCWEKCMDK PGPKLDSRAE 

        70         80         90 
ACFVNCVERF IDTSQFILNR LEQTQKSKPV FSESLSD 

« Hide

References

« Hide 'large scale' references
[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]"Cloning and expression of mouse deafness dystonia peptide 1 cDNA."
Nakane T., Inada Y., Ito F., Itoh N., Tazawa S., Chiba S.
Biochem. Biophys. Res. Commun. 273:759-764(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Adipocyte.
[3]"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. expand/collapse author list , 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].
Tissue: Submandibular gland.
[4]"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].
Strain: C57BL/6J and Czech II.
Tissue: Mammary gland and Thymus.
[5]"The calcium-binding aspartate/glutamate carriers, citrin and aralar1, are new substrates for the DDP1/TIMM8a-TIMM13 complex."
Roesch K., Hynds P.J., Varga R., Tranebjaerg L., Koehler C.M.
Hum. Mol. Genet. 13:2101-2111(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87 AND SER-96, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF150081 mRNA. Translation: AAD39988.1.
AB031055 mRNA. Translation: BAA90770.1.
AK011402 mRNA. Translation: BAB27594.1.
AK088903 mRNA. Translation: BAC40644.1.
AK090079 mRNA. Translation: BAC41082.1.
AK165573 mRNA. Translation: BAE38265.1.
BC004796 mRNA. Translation: AAH04796.1.
BC094631 mRNA. Translation: AAH94631.1.
CCDSCCDS41122.1.
PIRJC7322.
RefSeqNP_038926.1. NM_013898.2.
UniGeneMm.214504.

3D structure databases

ProteinModelPortalQ9WVA2.
SMRQ9WVA2. Positions 29-84.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9WVA2. 2 interactions.
MINTMINT-4137932.

PTM databases

PhosphoSiteQ9WVA2.

Proteomic databases

MaxQBQ9WVA2.
PaxDbQ9WVA2.
PRIDEQ9WVA2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000052902; ENSMUSP00000049749; ENSMUSG00000045455.
ENSMUST00000054213; ENSMUSP00000050156; ENSMUSG00000048007.
GeneID30058.
KEGGmmu:30058.
UCSCuc009ugd.1. mouse.

Organism-specific databases

CTD30058.
MGIMGI:1353433. Timm8a1.

Phylogenomic databases

eggNOGNOG238740.
GeneTreeENSGT00390000016102.
HOGENOMHOG000115758.
HOVERGENHBG060492.
InParanoidQ9WVA2.
KOK17780.
OMADRSEEPC.
OrthoDBEOG79W97P.
PhylomeDBQ9WVA2.
TreeFamTF106191.

Gene expression databases

BgeeQ9WVA2.
GenevestigatorQ9WVA2.

Family and domain databases

Gene3D1.10.287.810. 1 hit.
InterProIPR004217. Tim10/DDP_fam_Znf.
[Graphical view]
PfamPF02953. zf-Tim10_DDP. 1 hit.
[Graphical view]
SUPFAMSSF144122. SSF144122. 1 hit.
ProtoNetSearch...

Other

NextBio307190.
PROQ9WVA2.
SOURCESearch...

Entry information

Entry nameTIM8A_MOUSE
AccessionPrimary (citable) accession number: Q9WVA2
Secondary accession number(s): Q542E5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot