TIM9_DANRE
ID TIM9_DANRE Reviewed; 84 AA.
AC Q9W762;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit Tim9;
GN Name=timm9; Synonyms=tim9;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10611480; DOI=10.1016/s0014-5793(99)01665-8;
RA Bauer M.F., Rothbauer U., Muehlenbein N., Smith R.J.H., Gerbitz K.-D.,
RA Neupert W., Brunner M., Hofmann S.;
RT "The mitochondrial TIM22 preprotein translocase is highly conserved
RT throughout the eukaryotic kingdom.";
RL FEBS Lett. 464:41-47(1999).
CC -!- FUNCTION: Mitochondrial intermembrane chaperone that participates in
CC the import and insertion of multi-pass transmembrane proteins into the
CC mitochondrial inner membrane. May also be required for the transfer of
CC beta-barrel precursors from the TOM complex to the sorting and assembly
CC machinery (SAM complex) of the outer membrane. Acts as a chaperone-like
CC protein that protects the hydrophobic precursors from aggregation and
CC guide them through the mitochondrial intermembrane space (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterohexamer; composed of 3 copies of TIMM9 and 3 copies of
CC TIMM10/TIM10A, named soluble 70 kDa complex. The complex forms a 6-
CC bladed alpha-propeller structure and associates with the TIMM22
CC component of the TIM22 complex. Interacts with multi-pass transmembrane
CC proteins in transit (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Intermembrane side
CC {ECO:0000250}.
CC -!- DOMAIN: The twin CX3C motif contains 4 conserved Cys residues that form
CC 2 disulfide bonds in the mitochondrial intermembrane space. However,
CC during the transit of TIMM9 from cytoplasm into mitochondrion, the Cys
CC residues probably coordinate zinc, thereby preventing folding and
CC allowing its transfer across mitochondrial outer membrane (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small Tim family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD40013.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF150107; AAD40013.1; ALT_INIT; mRNA.
DR PIR; T51193; T51193.
DR AlphaFoldDB; Q9W762; -.
DR SMR; Q9W762; -.
DR STRING; 7955.ENSDARP00000106401; -.
DR ZFIN; ZDB-GENE-021206-14; timm9.
DR eggNOG; KOG3479; Eukaryota.
DR InParanoid; Q9W762; -.
DR PhylomeDB; Q9W762; -.
DR Reactome; R-DRE-1268020; Mitochondrial protein import.
DR PRO; PR:Q9W762; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.810; -; 1.
DR InterPro; IPR004217; Tim10-like.
DR InterPro; IPR035427; Tim10-like_dom_sf.
DR Pfam; PF02953; zf-Tim10_DDP; 1.
DR SUPFAM; SSF144122; SSF144122; 1.
PE 3: Inferred from homology;
KW Chaperone; Disulfide bond; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Protein transport; Reference proteome;
KW Translocation; Transport; Zinc.
FT CHAIN 1..84
FT /note="Mitochondrial import inner membrane translocase
FT subunit Tim9"
FT /id="PRO_0000228036"
FT MOTIF 28..52
FT /note="Twin CX3C motif"
FT DISULFID 28..52
FT /evidence="ECO:0000250"
FT DISULFID 32..48
FT /evidence="ECO:0000250"
SQ SEQUENCE 84 AA; 10173 MW; 4EB82164CAC155A5 CRC64;
MAAQVTESDQ IKQFKEFLGT YNKLTENCFM DCVKDFTTRE VKPEETTCSE SCLQKYLKMT
QRISMRFQEY HIQQNERWPQ KPDY