TIM8_CAEEL
ID TIM8_CAEEL Reviewed; 83 AA.
AC Q9N408; Q9Y0V8;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit Tim8 {ECO:0000250|UniProtKB:Q9Y1A3};
GN Name=ddp-1 {ECO:0000312|WormBase:Y39A3CR.4};
GN Synonyms=tim-8 {ECO:0000312|WormBase:Y39A3CR.4};
GN ORFNames=Y39A3CR.4 {ECO:0000312|WormBase:Y39A3CR.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15485840; DOI=10.1074/jbc.m409618200;
RA Curran S.P., Leverich E.P., Koehler C.M., Larsen P.L.;
RT "Defective mitochondrial protein translocation precludes normal
RT Caenorhabditis elegans development.";
RL J. Biol. Chem. 279:54655-54662(2004).
CC -!- FUNCTION: Mitochondrial intermembrane chaperone that participates in
CC the import and insertion of some multi-pass transmembrane proteins into
CC the mitochondrial inner membrane (By similarity). Also required for the
CC transfer of beta-barrel precursors from the TOM complex to the sorting
CC and assembly machinery (SAM complex) of the outer membrane (By
CC similarity). Acts as a chaperone-like protein that protects the
CC hydrophobic precursors from aggregation and guide them through the
CC mitochondrial intermembrane space (By similarity). The ddp-1/tim-8-tim-
CC 13 complex mediates the import of some proteins while the predominant
CC tim-9/tin-9.1-tim-10/tin-10 70 kDa complex mediates the import of much
CC more proteins (PubMed:15485840). {ECO:0000250|UniProtKB:Q17754,
CC ECO:0000269|PubMed:15485840}.
CC -!- SUBUNIT: Heterohexamer; composed of 3 copies of ddp-1/tim-8 and 3
CC copies of tin-13/tim-13, named soluble 70 kDa complex. Associates with
CC the TIM22 complex, whose core is composed of tim-22.
CC {ECO:0000250|UniProtKB:O74700}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:O74700}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O74700}; Intermembrane side
CC {ECO:0000250|UniProtKB:O74700}.
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 ddp-1/tim-8 from cytoplasm into mitochondrion,
CC the Cys residues probably coordinate zinc, thereby preventing folding
CC and allowing its transfer across mitochondrial outer membrane.
CC {ECO:0000250|UniProtKB:O74700}.
CC -!- DISRUPTION PHENOTYPE: Worms display mitochondria with an interconnected
CC morphology, presumably due to defects in the assembly of outer membrane
CC fission/fusion components. {ECO:0000269|PubMed:15485840}.
CC -!- SIMILARITY: Belongs to the small Tim family. {ECO:0000305}.
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DR EMBL; AF150086; AAD39993.1; -; mRNA.
DR EMBL; FO080225; CCD62165.1; -; Genomic_DNA.
DR RefSeq; NP_497467.1; NM_065066.5.
DR AlphaFoldDB; Q9N408; -.
DR SMR; Q9N408; -.
DR BioGRID; 40586; 1.
DR STRING; 6239.Y39A3CR.4; -.
DR EPD; Q9N408; -.
DR PaxDb; Q9N408; -.
DR PeptideAtlas; Q9N408; -.
DR EnsemblMetazoa; Y39A3CR.4.1; Y39A3CR.4.1; WBGene00000941.
DR GeneID; 175331; -.
DR KEGG; cel:CELE_Y39A3CR.4; -.
DR UCSC; Y39A3CR.4; c. elegans.
DR CTD; 175331; -.
DR WormBase; Y39A3CR.4; CE21655; WBGene00000941; ddp-1.
DR eggNOG; KOG3489; Eukaryota.
DR HOGENOM; CLU_141397_1_2_1; -.
DR InParanoid; Q9N408; -.
DR OMA; DVCFADY; -.
DR OrthoDB; 1593287at2759; -.
DR PhylomeDB; Q9N408; -.
DR PRO; PR:Q9N408; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000941; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007005; P:mitochondrion organization; IMP:WormBase.
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 InterPro; IPR039238; Tim8/13.
DR PANTHER; PTHR19338; PTHR19338; 1.
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..83
FT /note="Mitochondrial import inner membrane translocase
FT subunit Tim8"
FT /id="PRO_0000228027"
FT MOTIF 35..60
FT /note="Twin CX3C motif"
FT /evidence="ECO:0000250|UniProtKB:O74700"
FT DISULFID 35..60
FT /evidence="ECO:0000250|UniProtKB:O74700"
FT DISULFID 39..56
FT /evidence="ECO:0000250|UniProtKB:O74700"
FT CONFLICT 57
FT /note="I -> F (in Ref. 1; AAD39993)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 83 AA; 9578 MW; 9EDE7AE144A7ECB7 CRC64;
MDSADPQLNR FLQQLQAETQ RQKFTEQVHT LTGRCWDVCF ADYRPPSKMD GKTQTCIQNC
VNRMIDASNF MVEHLSKMNG GHV
