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Protein

Mitochondrial import inner membrane translocase subunit Tim9

Gene

Timm9

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Protein transport, Translocation, Transport

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial import inner membrane translocase subunit Tim9
Gene namesi
Name:Timm9
Synonyms:Tim9, Tim9a, Timm9a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi621656. Timm9.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 8988Mitochondrial import inner membrane translocase subunit Tim9PRO_0000193597Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Disulfide bondi28 ↔ 52By similarity
Disulfide bondi32 ↔ 48By similarity

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

PaxDbiQ9WV97.
PRIDEiQ9WV97.

PTM databases

iPTMnetiQ9WV97.
PhosphoSiteiQ9WV97.

Expressioni

Gene expression databases

BgeeiENSRNOG00000008222.
GenevisibleiQ9WV97. RN.

Interactioni

Subunit structurei

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 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000010871.

Structurei

3D structure databases

ProteinModelPortaliQ9WV97.
SMRiQ9WV97. Positions 9-87.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi28 – 5225Twin CX3C motifAdd
BLAST

Domaini

The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space. However, during the transit of TIMM9 from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane (By similarity).By similarity

Sequence similaritiesi

Belongs to the small Tim family.Curated

Phylogenomic databases

eggNOGiKOG3479. Eukaryota.
ENOG4111TUA. LUCA.
GeneTreeiENSGT00450000040278.
HOGENOMiHOG000185786.
HOVERGENiHBG083156.
InParanoidiQ9WV97.
KOiK17777.
OMAiSNLVERC.
PhylomeDBiQ9WV97.
TreeFamiTF106192.

Family and domain databases

Gene3Di1.10.287.810. 1 hit.
InterProiIPR004217. Tim10/DDP_fam_Znf.
[Graphical view]
PfamiPF02953. zf-Tim10_DDP. 1 hit.
[Graphical view]
SUPFAMiSSF144122. SSF144122. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9WV97-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAQIPESDQ IKQFKEFLGT YNKLTETCFL DCVKDFTTRE VKPEEVTCSE
60 70 80
HCLQKYLKMT QRISMRFQEY HIQQNEALAA KAGLLGQPR
Length:89
Mass (Da):10,376
Last modified:March 21, 2006 - v3
Checksum:i00F17CF491A09548
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti67 – 682FQ → E in AAD40008 (Ref. 2) Curated
Sequence conflicti79 – 791A → V in AAD40008 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03049301 Genomic DNA. No translation available.
AF150102 mRNA. Translation: AAD40008.1. Different termination.
RefSeqiNP_001263358.1. NM_001276429.1.
NP_001263359.1. NM_001276430.1.
NP_598288.1. NM_133604.1.
UniGeneiRn.8459.

Genome annotation databases

EnsembliENSRNOT00000010871; ENSRNOP00000010871; ENSRNOG00000008222.
ENSRNOT00000088790; ENSRNOP00000071324; ENSRNOG00000008222.
GeneIDi171139.
KEGGirno:171139.
UCSCiRGD:621656. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03049301 Genomic DNA. No translation available.
AF150102 mRNA. Translation: AAD40008.1. Different termination.
RefSeqiNP_001263358.1. NM_001276429.1.
NP_001263359.1. NM_001276430.1.
NP_598288.1. NM_133604.1.
UniGeneiRn.8459.

3D structure databases

ProteinModelPortaliQ9WV97.
SMRiQ9WV97. Positions 9-87.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000010871.

PTM databases

iPTMnetiQ9WV97.
PhosphoSiteiQ9WV97.

Proteomic databases

PaxDbiQ9WV97.
PRIDEiQ9WV97.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000010871; ENSRNOP00000010871; ENSRNOG00000008222.
ENSRNOT00000088790; ENSRNOP00000071324; ENSRNOG00000008222.
GeneIDi171139.
KEGGirno:171139.
UCSCiRGD:621656. rat.

Organism-specific databases

CTDi26520.
RGDi621656. Timm9.

Phylogenomic databases

eggNOGiKOG3479. Eukaryota.
ENOG4111TUA. LUCA.
GeneTreeiENSGT00450000040278.
HOGENOMiHOG000185786.
HOVERGENiHBG083156.
InParanoidiQ9WV97.
KOiK17777.
OMAiSNLVERC.
PhylomeDBiQ9WV97.
TreeFamiTF106192.

Miscellaneous databases

PROiQ9WV97.

Gene expression databases

BgeeiENSRNOG00000008222.
GenevisibleiQ9WV97. RN.

Family and domain databases

Gene3Di1.10.287.810. 1 hit.
InterProiIPR004217. Tim10/DDP_fam_Znf.
[Graphical view]
PfamiPF02953. zf-Tim10_DDP. 1 hit.
[Graphical view]
SUPFAMiSSF144122. SSF144122. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiTIM9_RAT
AccessioniPrimary (citable) accession number: Q9WV97
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: March 21, 2006
Last modified: September 7, 2016
This is version 114 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.