TIM10_CAEEL
ID TIM10_CAEEL Reviewed; 86 AA.
AC Q9Y0V6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit Tim10;
GN Name=tin-10; Synonyms=tim-10; ORFNames=Y66D12A.22;
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 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 (Probable).
CC {ECO:0000305|PubMed:15485840}.
CC -!- SUBUNIT: Heterohexamer; composed of 3 copies of tim-9/tin-9.1 and 3
CC copies of tim-10/tin-10, named soluble 70 kDa complex. The complex
CC associates with the tim-22 component of the TIM22 complex. Interacts
CC with multi-pass transmembrane proteins in transit (By similarity).
CC {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 tim-10/tin-10 from cytoplasm into mitochondrion,
CC the Cys residues probably coordinate zinc, thereby preventing folding
CC and allowing its transfer across mitochondrial outer membrane (By
CC similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Worms a small body size, reduced number of
CC progeny produced and partial embryonic lethality due to defects in
CC import of proteins into mitochondria. {ECO:0000269|PubMed:15485840}.
CC -!- SIMILARITY: Belongs to the small Tim family. {ECO:0000305}.
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DR EMBL; AF150094; AAD40000.1; -; mRNA.
DR EMBL; AL161712; CAC70139.1; -; Genomic_DNA.
DR RefSeq; NP_499480.1; NM_067079.5.
DR AlphaFoldDB; Q9Y0V6; -.
DR SMR; Q9Y0V6; -.
DR BioGRID; 41761; 2.
DR STRING; 6239.Y66D12A.22.1; -.
DR EPD; Q9Y0V6; -.
DR PaxDb; Q9Y0V6; -.
DR PeptideAtlas; Q9Y0V6; -.
DR EnsemblMetazoa; Y66D12A.22.1; Y66D12A.22.1; WBGene00006573.
DR EnsemblMetazoa; Y66D12A.22.2; Y66D12A.22.2; WBGene00006573.
DR EnsemblMetazoa; Y66D12A.22.3; Y66D12A.22.3; WBGene00006573.
DR GeneID; 176580; -.
DR UCSC; Y66D12A.22.2; c. elegans.
DR CTD; 176580; -.
DR WormBase; Y66D12A.22; CE28800; WBGene00006573; tin-10.
DR eggNOG; KOG3480; Eukaryota.
DR GeneTree; ENSGT00390000003068; -.
DR HOGENOM; CLU_162151_2_0_1; -.
DR InParanoid; Q9Y0V6; -.
DR OMA; ELEIEMM; -.
DR OrthoDB; 1477334at2759; -.
DR PhylomeDB; Q9Y0V6; -.
DR PRO; PR:Q9Y0V6; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006573; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0042719; C:mitochondrial intermembrane space protein transporter complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IMP:WormBase.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:WormBase.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR Gene3D; 1.10.287.810; -; 1.
DR InterPro; IPR027100; Tim10.
DR InterPro; IPR004217; Tim10-like.
DR InterPro; IPR035427; Tim10-like_dom_sf.
DR PANTHER; PTHR11038:SF16; PTHR11038:SF16; 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..86
FT /note="Mitochondrial import inner membrane translocase
FT subunit Tim10"
FT /id="PRO_0000228059"
FT MOTIF 29..54
FT /note="Twin CX3C motif"
FT DISULFID 29..54
FT /evidence="ECO:0000250"
FT DISULFID 33..50
FT /evidence="ECO:0000250"
SQ SEQUENCE 86 AA; 9608 MW; 1D0A9B49C6AFFBBA CRC64;
MATDAQMAQV AELEVEMMSD MYRRMTNSCQ AKCIATAFRE SELTKGEAVC LDRCVAKYLD
VHEKLGKRLT SMSQGDEAAL QKIAQQ