P62072 (TIM10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mitochondrial import inner membrane translocase subunit Tim10

Gene names

Name:	TIMM10
Synonyms:	TIM10

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	90 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.7
Subunit structure	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. Ref.7
Subcellular location	Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side Ref.6 Ref.7.
Tissue specificity	Ubiquitous, with highest expression in heart, kidney, liver and skeletal muscle. Ref.1 Ref.2
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 TIMM10 from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane Probable.
Sequence similarities	Belongs to the small Tim family.

Ontologies

Keywords
Biological process	Protein transport Translocation Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Ligand	Metal-binding Zinc
Molecular function	Chaperone
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular protein metabolic process Traceable author statement. Source: Reactome chaperone-mediated protein transport Inferred from direct assay Ref.9. Source: BHF-UCL protein import into mitochondrial inner membrane Inferred from direct assay Ref.9. Source: BHF-UCL sensory perception of sound Traceable author statement Ref.2. Source: UniProtKB
Cellular_component	mitochondrial inner membrane presequence translocase complex Traceable author statement Ref.2. Source: UniProtKB mitochondrial intermembrane space protein transporter complex Inferred from direct assay Ref.7. Source: BHF-UCL
Molecular_function	transporter activity Inferred from direct assay Ref.9. Source: BHF-UCL zinc ion binding Traceable author statement Ref.2. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TIMM9	Q9Y5J7	5	EBI-1200391,EBI-1200370

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 90

90

Mitochondrial import inner membrane translocase subunit Tim10

PRO_0000193612

Regions

Motif

29 – 54

26

Twin CX3C motif

Amino acid modifications

Disulfide bond

29 ↔ 54

Ref.9

Disulfide bond

33 ↔ 50

Ref.9

Secondary structure

1

.

.

.

.

.

.

.

.

90

Helix Strand Turn

Details...

Turn

14 – 18

5

Helix

19 – 33

15

Beta strand

40 – 42

3

Helix

45 – 74

30

Sequences

	Sequence		Length	Mass (Da)
	P62072 [UniParc]. Last modified June 21, 2004. Version 1. Checksum: D20EFAE694D14BAB	FASTA	90	10,333
	10 20 30 40 50 60 MDPLRAQQLA AELEVEMMAD MYNRMTSACH RKCVPPHYKE AELSKGESVC LDRCVSKYLD 70 80 90 IHERMGKKLT ELSMQDEELM KRVQQSSGPA

References

	« Hide 'large scale' referencesShow '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], TISSUE SPECIFICITY.
[2]	"The human family of deafness/dystonia peptide (DDP) related mitochondrial import proteins." Jin H., Kendall E., Freeman T.C., Roberts R.G., Vetrie D.L.P. Genomics 61:259-267(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: Brain.
[6]	"Role of the deafness dystonia peptide 1 (DDP1) in import of human Tim23 into the inner membrane of mitochondria." Rothbauer U., Hofmann S., Muehlenbein N., Paschen S.A., Gerbitz K.-D., Neupert W., Brunner M., Bauer M.F. J. Biol. Chem. 276:37327-37334(2001) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[7]	"Organization and function of the small Tim complexes acting along the import pathway of metabolite carriers into mammalian mitochondria." Muehlenbein N., Hofmann S., Rothbauer U., Bauer M.F. J. Biol. Chem. 279:13540-13546(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TIMM9; TIMM22 AND FXC1.
[8]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]	"Crystal structure of the mitochondrial chaperone TIM9.10 reveals a six-bladed alpha-propeller." Webb C.T., Gorman M.A., Lazarou M., Ryan M.T., Gulbis J.M. Mol. Cell 21:123-133(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) IN COMPLEX WITH TIMM9, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF150089 mRNA. Translation: AAD39995.1.
AF152354 mRNA. Translation: AAF15104.1.
AK289751 mRNA. Translation: BAF82440.1.
CH471076 Genomic DNA. Translation: EAW73753.1.
BC032133 mRNA. Translation: AAH32133.1.

IPI

IPI00001543.

RefSeq

NP_036588.1. NM_012456.2.

UniGene

Hs.235750.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BSK	X-ray	3.30	B/D/F	1-90	[»]

ProteinModelPortal

P62072.

ModBase

Search...

Protein-protein interaction databases

IntAct

P62072. 4 interactions.

STRING

9606.ENSP00000257245.

PTM databases

PhosphoSite

P62072.

Polymorphism databases

DMDM

49065657.

Proteomic databases

PaxDb

P62072.

PeptideAtlas

P62072.

PRIDE

P62072.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000257245; ENSP00000257245; ENSG00000134809.
ENST00000525158; ENSP00000433627; ENSG00000134809.
ENST00000525587; ENSP00000435678; ENSG00000134809.

GeneID

26519.

KEGG

hsa:26519.

UCSC

uc001nkm.1. human.

Organism-specific databases

CTD

26519.

GeneCards

GC11M057299.

HGNC

HGNC:11814. TIMM10.

HPA

HPA039946.

MIM

602251. gene.

neXtProt

NX_P62072.

PharmGKB

PA36521.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG297225.

HOGENOM

HOG000211421.

HOVERGEN

HBG055029.

InParanoid

P62072.

OMA

EIEMMSD.

OrthoDB

EOG46Q6V5.

PhylomeDB

P62072.

Enzyme and pathway databases

Reactome

REACT_17015. Metabolism of proteins.

Gene expression databases

Bgee

P62072.

CleanEx

HS_TIMM10.

Genevestigator

P62072.

GermOnline

ENSG00000134809. Homo sapiens.

Family and domain databases

Gene3D

1.10.287.810. 1 hit.

InterPro

IPR004217. Tim10/DDP_fam_Znf.
IPR027247. Tim10/Tim12.
[Graphical view]

PANTHER

PTHR11038. PTHR11038. 1 hit.

Pfam

PF02953. zf-Tim10_DDP. 1 hit.
[Graphical view]

SUPFAM

SSF144122. SSF144122. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P62072.

GenomeRNAi

26519.

NextBio

48834.

SOURCE

Search...

Entry information

Entry name

TIM10_HUMAN

Accession

Primary (citable) accession number: P62072
Secondary accession number(s): A8K136 , Q9WV99, Q9WVA0, Q9Y5J8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2004
Last sequence update:	June 21, 2004
Last modified:	May 1, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.