O74700 (TIM9_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mitochondrial import inner membrane translocase subunit TIM9

Gene names

Name:	TIM9
Ordered Locus Names:	YEL020W-A
ORF Names:	YEL020BW

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	87 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 TIM10, it may have a strong structural role. Ref.1 Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.15 Ref.16
Subunit structure	Heterohexamer; composed of 3 copies of TIM9 and 3 copies of TIM10, named soluble 70 kDa complex. Associates 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.1 Ref.5 Ref.11 Ref.12
Subcellular location	Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side Ref.1 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 TIM9 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 Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	protein import into mitochondrial inner membrane Inferred from direct assay Ref.1. 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.1Ref.5. Source: SGD
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein transporter activity Inferred from direct assay Ref.1. Source: SGD unfolded protein binding Inferred from direct assay Ref.12. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TIM10	P87108	7	EBI-9108,EBI-9115

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 87

87

Mitochondrial import inner membrane translocase subunit TIM9

PRO_0000193610

Regions

Motif

35 – 59

25

Twin CX3C motif

Amino acid modifications

Disulfide bond

35 ↔ 59

Probable

Disulfide bond

39 ↔ 55

Probable

Experimental info

Mutagenesis

40

1

V → A in tim9-3; impairs the import of mitochondrial carrier proteins into mitochondria; when associated with P-60. Ref.14

Mutagenesis

52

1

E → G in tim9-19; impairs the import of mitochondrial carrier proteins into mitochondria. Ref.14

Mutagenesis

60

1

S → P in tim9-3; impairs the import of mitochondrial carrier proteins into mitochondria; when associated with A-40. Ref.14

Mutagenesis

67

1

S → C: Impairs the import of mitochondrial carrier proteins into mitochondria. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

87

Helix Strand Turn

Details...

Helix

14 – 39

26

Beta strand

44 – 47

4

Helix

50 – 69

20

Helix

73 – 76

4

Sequences

	Sequence		Length	Mass (Da)
	O74700 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 5160E5DBA52065C7	FASTA	87	10,202
	10 20 30 40 50 60 MDALNSKEQQ EFQKVVEQKQ MKDFMRLYSN LVERCFTDCV NDFTTSKLTN KEQTCIMKCS 70 80 EKFLKHSERV GQRFQEQNAA LGQGLGR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH TIM10, MUTAGENESIS OF SER-67.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W. Nature 387:78-81(1997) [PubMed: 9169868] [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]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"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: PROTEIN SEQUENCE OF 27-33 AND 74-87, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH TIM10 AND TIM12.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"The role of Tim9p in the assembly of the TIM22 import complexes." Leuenberger D., Curran S.P., Wong D., Koehler C.M. Traffic 4:144-152(2003) [PubMed: 12656987] [Abstract] Cited for: MUTAGENESIS OF VAL-40; GLU-52 AND SER-60.
[15]	"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.
[16]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U18530 Genomic DNA. No translation available.
AF093244 Genomic DNA. Translation: AAC83169.1.
AY557798 Genomic DNA. Translation: AAS56124.1.
BK006939 Genomic DNA. Translation: DAA07632.1.

PIR

S78717.

RefSeq

NP_010894.1. NM_001184349.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3DXR	X-ray	2.50	A	1-87	[»]

ProteinModelPortal

O74700.

SMR

O74700. Positions 12-80.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5806N.

IntAct

O74700. 2 interactions.

STRING

O74700.

Protein family/group databases

TCDB

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

Proteomic databases

PeptideAtlas

O74700.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YEL020W-A; YEL020W-A; YEL020W-A.

GeneID

856693.

KEGG

sce:YEL020W-A.

NMPDR

fig|4932.3.peg.1949.

Organism-specific databases

CYGD

YEL020w-a.

SGD

S000007256. TIM9.

Phylogenomic databases

eggNOG

fuNOG10876.

GeneTree

EFGT00050000003668.

HOGENOM

HBG628226.

OMA

MKDFMRL.

OrthoDB

EOG4DBXQH.

Gene expression databases

ArrayExpress

O74700.

Genevestigator

O74700.

GermOnline

YEL020W-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

982742.

Entry information

Entry name

TIM9_YEAST

Accession

Primary (citable) accession number: O74700
Secondary accession number(s): D3DLM8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	November 1, 1998
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