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P62075 (TIM13_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. 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 Tim13
Gene names
Name:Timm13
Synonyms:Tim13a, Timm13a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length95 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 TIMM8 (TIMM8A or TIMM8B) 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). 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 TIMM13 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 9595Mitochondrial import inner membrane translocase subunit Tim13
PRO_0000193624

Regions

Motif46 – 6924Twin CX3C motif

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue531N6-succinyllysine Ref.6
Disulfide bond46 ↔ 69 By similarity
Disulfide bond50 ↔ 65 By similarity

Experimental info

Sequence conflict31S → G in BAB22536. Ref.2
Sequence conflict181D → S in AAH11436. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P62075 [UniParc].

Last modified June 21, 2004. Version 1.
Checksum: F9A50A2E7F6E64C8

FASTA9510,458
        10         20         30         40         50         60 
MDSGFGSDFG GTGGGKLDPG AIMEQVKVQI AVANAQELLQ RMTDKCFRKC IGKPGGSLDN 

        70         80         90 
SEQKCIAMCM DRYMDAWNTV SRAYNSRLQR ERANM 

« 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]"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].
Strain: C57BL/6J and NOD.
Tissue: Brain, Thymus and Tongue.
[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 28-41 AND 50-64, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[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]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF144702 mRNA. Translation: AAD39953.1.
AK003054 mRNA. Translation: BAB22536.1.
AK009041 mRNA. Translation: BAB26042.1.
AK009152 mRNA. Translation: BAB26109.1.
AK013230 mRNA. Translation: BAB28728.1.
AK088984 mRNA. Translation: BAC40687.1.
BC011436 mRNA. Translation: AAH11436.1.
CCDSCCDS35989.1.
RefSeqNP_038923.1. NM_013895.4.
UniGeneMm.142132.

3D structure databases

ProteinModelPortalP62075.
SMRP62075. Positions 35-89.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP62075. 2 interactions.
MINTMINT-4996911.

PTM databases

PhosphoSiteP62075.

Proteomic databases

MaxQBP62075.
PaxDbP62075.
PRIDEP62075.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020440; ENSMUSP00000020440; ENSMUSG00000020219.
GeneID30055.
KEGGmmu:30055.
UCSCuc007gfi.2. mouse.

Organism-specific databases

CTD26517.
MGIMGI:1353432. Timm13.

Phylogenomic databases

eggNOGNOG246901.
GeneTreeENSGT00390000014000.
HOGENOMHOG000115759.
HOVERGENHBG079645.
InParanoidP62075.
KOK17781.
OMAGSEETCL.
OrthoDBEOG7Q8CQP.
PhylomeDBP62075.
TreeFamTF106194.

Gene expression databases

BgeeP62075.
GenevestigatorP62075.

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

NextBio307174.
PROP62075.
SOURCESearch...

Entry information

Entry nameTIM13_MOUSE
AccessionPrimary (citable) accession number: P62075
Secondary accession number(s): Q91VM6 expand/collapse secondary AC list , Q9DC89, Q9UHL8, Q9WTL1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: June 21, 2004
Last modified: July 9, 2014
This is version 93 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