TIM13_CAEEL
ID TIM13_CAEEL Reviewed; 108 AA.
AC O45319;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit tim-13;
GN Name=tin-13; Synonyms=tim-13; ORFNames=DY3.1;
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).
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. Also 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. The tim-8-
CC tim-13 complex mediates the import of some proteins while the
CC predominant tim-9/tin-9.1-tim-10/tin-10 70 kDa complex mediates the
CC import of much more proteins (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterohexamer; composed of 3 copies of tim-8/ddp-1 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 (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 tin-13/tim-13 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 -!- SIMILARITY: Belongs to the small Tim family. {ECO:0000305}.
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DR EMBL; AF144704; AAD39955.1; -; mRNA.
DR EMBL; Z96047; CAB09410.1; -; Genomic_DNA.
DR PIR; T20389; T20389.
DR RefSeq; NP_492370.1; NM_059969.4.
DR AlphaFoldDB; O45319; -.
DR SMR; O45319; -.
DR BioGRID; 38119; 6.
DR STRING; 6239.DY3.1; -.
DR EPD; O45319; -.
DR PaxDb; O45319; -.
DR PeptideAtlas; O45319; -.
DR EnsemblMetazoa; DY3.1.1; DY3.1.1; WBGene00006574.
DR GeneID; 172686; -.
DR KEGG; cel:CELE_DY3.1; -.
DR UCSC; DY3.1; c. elegans.
DR CTD; 172686; -.
DR WormBase; DY3.1; CE15745; WBGene00006574; tin-13.
DR eggNOG; KOG1733; Eukaryota.
DR GeneTree; ENSGT00390000014000; -.
DR HOGENOM; CLU_141397_0_0_1; -.
DR InParanoid; O45319; -.
DR OMA; MAAWNQV; -.
DR OrthoDB; 1566384at2759; -.
DR PhylomeDB; O45319; -.
DR PRO; PR:O45319; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006574; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042719; C:mitochondrial intermembrane space protein transporter complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IBA:GO_Central.
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..108
FT /note="Mitochondrial import inner membrane translocase
FT subunit tim-13"
FT /id="PRO_0000193627"
FT REGION 89..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 45..68
FT /note="Twin CX3C motif"
FT DISULFID 45..68
FT /evidence="ECO:0000250"
FT DISULFID 49..64
FT /evidence="ECO:0000250"
SQ SEQUENCE 108 AA; 11685 MW; 7CF2DA7EC6B229AB CRC64;
MDQLLDVETL KKLSPEQQEQ VISGVKQQAA LANAQNLVTD ISEKCTNKCI TAPGSSLASG
EKQCLQRCMD RFMESWNLVS QTLQKRLQEE MASSGGMGGG FGQGPSFS
