Mitochondrial import inner membrane translocase subunit TIM10 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P87108 (TIM10_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 91. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Mitochondrial import inner membrane translocase subunit TIM10

Alternative name(s):
Mitochondrial intermembrane protein MRS11

Gene names

Name:	TIM10
Synonyms:	MRS11
Ordered Locus Names:	YHR005C-A
ORF Names:	YHR005BC

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	93 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. 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. Compared to TIM9, it may function as a substrate sensor. Ref.4 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.19 Ref.21
Subunit structure	Heterohexamer; composed of 3 copies of TIM9 and 3 copies of TIM10, named soluble 70 kDa complex. Associates directly with the TIM12 component of the TIM22 complex, whose core is composed of TIM18, TIM22 and TIM54. Interacts with the transmembrane regions of multi-pass transmembrane proteins in transit. Ref.4 Ref.6 Ref.7 Ref.8 Ref.13 Ref.14
Subcellular location	Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side Ref.1 Ref.6 Ref.8.
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 TIM10 from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane.
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 Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	protein import into mitochondrial inner membrane Inferred from direct assay. Source: SGD
Cellular component	mitochondrial inner membrane protein insertion complex Inferred from direct assay. Source: SGD mitochondrial intermembrane space protein transporter complex Inferred from direct assay Ref.4 Ref.8. Source: SGD
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein transporter activity Inferred from direct assay. Source: SGD unfolded protein binding Inferred from direct assay Ref.14. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TIM9	O74700	7	EBI-9115,EBI-9108

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 93

Mitochondrial import inner membrane translocase subunit TIM10

PRO_0000193622

Regions

Region

1 – 31

Interaction with transmembrane regions of transmembrane proteins in transit

Region

73 – 93

Required for heterohexamerization

Motif

40 – 65

Twin CX3C motif

Amino acid modifications

Disulfide bond

40 ↔ 65

Ref.5 Ref.13 Ref.18 Ref.20

Disulfide bond

44 ↔ 61

Ref.5 Ref.13 Ref.18 Ref.20

Experimental info

Mutagenesis

C → S: Induces impairment in folding and loss of zinc-binding. Ref.5 Ref.18

Mutagenesis

C → S: Loss of function due to severely affected folding and the presence of non-native disulfides bonds; loss of zinc-binding. Ref.5 Ref.18

Mutagenesis

C → S: Loss of function due to severely affected folding and the presence of non-native disulfides bonds; loss of zinc-binding. Ref.5 Ref.18

Mutagenesis

C → S: Induces impairment in folding and loss of zinc-binding. Ref.5 Ref.18

Secondary structure

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P87108 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 70DD4764B944FF17
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FASTA

10,305

        10         20         30         40         50         60 
MSFLGFGGGQ PQLSSQQKIQ AAEAELDLVT DMFNKLVNNC YKKCINTSYS EGELNKNESS 

        70         80         90 
CLDRCVAKYF ETNVQVGENM QKMGQSFNAA GKF

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A soluble 12-kDa protein of the mitochondrial intermembrane space, Mrs11p, is essential for mitochondrial biogenesis and viability of yeast cells." Jarosch E., Rodel G., Schweyen R.J. Mol. Gen. Genet. 255:157-165(1997) [PubMed: 9236772] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION. Strain: ATCC 44774 / DBY747.
[2]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII." Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P. Vaudin M. Science 265:2077-2082(1994) [PubMed: 8091229] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Tim9p, an essential partner subunit of Tim10p for the import of mitochondrial carrier proteins." Koehler C.M., Merchant S., Oppliger W., Schmid K., Jarosch E., Dolfini L., Junne T., Schatz G., Tokatlidis K. EMBO J. 17:6477-6486(1998) [PubMed: 9822593] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT.
[5]	"The structural basis of the TIM10 chaperone assembly." Lu H., Golovanov A.P., Alcock F., Grossmann J.G., Allen S., Lian L.-Y., Tokatlidis K. J. Biol. Chem. 279:18959-18966(2004) [PubMed: 14973126] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, ZINC-BINDING WHEN PRESENT IN THE CYTOSOL, MUTAGENESIS OF CYS-40; CYS-44; CYS-61 AND CYS-65.
[6]	"Import of carrier proteins into the mitochondrial inner membrane mediated by Tim22." Sirrenberg C., Bauer M.D., Guiard B., Neupert W., Brunner M. Nature 384:582-585(1996) [PubMed: 8955274] [Abstract] Cited for: FUNCTION, ZINC-BINDING, SUBCELLULAR LOCATION, INTERACTION WITH TIM12 AND TIM22.
[7]	"Import of mitochondrial carriers mediated by essential proteins of the intermembrane space." Koehler C.M., Jarosch E., Tokatlidis K., Schmid K., Schweyen R.J., Schatz G. Science 279:369-373(1998) [PubMed: 9430585] [Abstract] Cited for: FUNCTION, INTERACTION WITH TIM12 AND TIM22.
[8]	"Tim9, a new component of the TIM22.54 translocase in mitochondria." Adam A., Endres M., Sirrenberg C., Lottspeich F., Neupert W., Brunner M. EMBO J. 18:313-319(1999) [PubMed: 9889188] [Abstract] Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH TIM9 AND TIM12.
[9]	"Transport of the ADP/ATP carrier of mitochondria from the TOM complex to the TIM22.54 complex." Endres M., Neupert W., Brunner M. EMBO J. 18:3214-3221(1999) [PubMed: 10369662] [Abstract] Cited for: FUNCTION.
[10]	"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: 10995434] [Abstract] Cited for: FUNCTION.
[11]	"Functional reconstitution of the import of the yeast ADP/ATP carrier mediated by the TIM10 complex." Luciano P., Vial S., Vergnolle M.A.S., Dyall S.D., Robinson D.R., Tokatlidis K. EMBO J. 20:4099-4106(2001) [PubMed: 11483513] [Abstract] Cited for: FUNCTION.
[12]	"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: 11509656] [Abstract] Cited for: FUNCTION.
[13]	"The Tim9p-Tim10p complex binds to the transmembrane domains of the ADP/ATP carrier." Curran S.P., Leuenberger D., Oppliger W., Koehler C.M. EMBO J. 21:942-953(2002) [PubMed: 11867522] [Abstract] Cited for: SUBUNIT, DISULFIDE BONDS, LACK OF ZINC-BINDING WHEN PRESENT IN THE MITOCHONDRIAL INTERMEMBRANE SPACE.
[14]	"Assembly of Tim9 and Tim10 into a functional chaperone." Vial S., Lu H., Allen S., Savory P., Thornton D., Sheehan J., Tokatlidis K. J. Biol. Chem. 277:36100-36108(2002) [PubMed: 12138093] [Abstract] Cited for: FUNCTION, SUBUNIT.
[15]	"Mitochondrial import of the ADP/ATP carrier: the essential TIM complex of the intermembrane space is required for precursor release from the TOM complex." Truscott K.N., Wiedemann N., Rehling P., Mueller H., Meisinger C., Pfanner N., Guiard B. Mol. Cell. Biol. 22:7780-7789(2002) [PubMed: 12391147] [Abstract] Cited for: FUNCTION.
[16]	"Protein insertion into the mitochondrial inner membrane by a twin-pore translocase." Rehling P., Model K., Brandner K., Kovermann P., Sickmann A., Meyer H.E., Kuehlbrandt W., Wagner R., Truscott K.N., Pfanner N. Science 299:1747-1751(2003) [PubMed: 12637749] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE TIM22 COMPLEX WITH TIM12; TIM18; TIM22 AND TIM54.
[17]	Erratum Rehling P., Model K., Brandner K., Kovermann P., Sickmann A., Meyer H.E., Kuehlbrandt W., Wagner R., Truscott K.N., Pfanner N. Science 300:251-251(2003)
[18]	"Juxtaposition of the two distal CX3C motifs via intrachain disulfide bonding is essential for the folding of Tim10." Allen S., Lu H., Thornton D., Tokatlidis K. J. Biol. Chem. 278:38505-38513(2003) [PubMed: 12882976] [Abstract] Cited for: DISULFIDE BONDS, MUTAGENESIS OF CYS-40; CYS-44; CYS-61 AND CYS-65.
[19]	"Biogenesis of the protein import channel Tom40 of the mitochondrial outer membrane: intermembrane space components are involved in an early stage of the assembly pathway." Wiedemann N., Truscott K.N., Pfannschmidt S., Guiard B., Meisinger C., Pfanner N. J. Biol. Chem. 279:18188-18194(2004) [PubMed: 14978039] [Abstract] Cited for: FUNCTION IN TRANSFER OF BETA-BARREL PROTEINS.
[20]	"Functional TIM10 chaperone assembly is redox-regulated in vivo." Lu H., Allen S., Wardleworth L., Savory P., Tokatlidis K. J. Biol. Chem. 279:18952-18958(2004) [PubMed: 14973127] [Abstract] Cited for: DISULFIDE BONDS.
[21]	"Distinct domains of small Tims involved in subunit interaction and substrate recognition." Vergnolle M.A.S., Baud C., Golovanov A.P., Alcock F., Luciano P., Lian L.-Y., Tokatlidis K. J. Mol. Biol. 351:839-849(2005) [PubMed: 16039669] [Abstract] Cited for: FUNCTION.
[22]	"Zinc binding stabilizes mitochondrial Tim10 in a reduced and import-competent state kinetically." Lu H., Woodburn J. J. Mol. Biol. 353:897-910(2005) [PubMed: 16199054] [Abstract] Cited for: ZINC-BINDING.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z80875 Genomic DNA. Translation: CAB02581.1.
U10555 Genomic DNA. Translation: AAB68435.1.
BK006934 Genomic DNA. Translation: DAA06693.1.

PIR

S72314.

RefSeq

NP_011869.1. NM_001181427.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3DXR	X-ray	2.50	B	1-93	[»]

ProteinModelPortal

P87108.

SMR

P87108. Positions 15-83.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1141N.

IntAct

P87108. 3 interactions.

MINT

MINT-4987878.

STRING

P87108.

Protein family/group databases

TCDB

3.A.8.1.1. mitochondrial protein translocase (MPT) family.

Proteomic databases

PeptideAtlas

P87108.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YHR005C-A; YHR005C-A; YHR005C-A.

GeneID

856395.

KEGG

sce:YHR005C-A.

NMPDR

fig|4932.3.peg.3013.

Organism-specific databases

CYGD

YHR005c-a.

SGD

S000003530. TIM10.

Phylogenomic databases

eggNOG

fuNOG12074.

GeneTree

EFGT00050000006018.

HOGENOM

HBG560646.

OMA

EIEMMSD.

OrthoDB

EOG4V46JG.

Gene expression databases

ArrayExpress

P87108.

Genevestigator

P87108.

GermOnline

YHR005C-A. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR004217. Tim8/9/10/13_Znf-like.
[Graphical view]

Gene3D

G3DSA:1.10.287.810. G3DSA:1.10.287.810. 1 hit.

Pfam

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

SUPFAM

SSF144122. SSF144122. 1 hit.

ProtoNet

Search...

Other

NextBio

981917.

Entry information

Entry name

TIM10_YEAST

Accession

Primary (citable) accession number: P87108
Secondary accession number(s): D3DKU9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	July 1, 1997
Last modified:	December 14, 2011
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome VIII

Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents