TIM13_DANRE
ID TIM13_DANRE Reviewed; 95 AA.
AC Q6DGJ3;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit Tim13;
GN Name=timm13; Synonyms=tim13a, timm13a; ORFNames=zgc:92895;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
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 TIMM8-
CC TIMM13 complex mediates the import of some proteins while the
CC predominant TIMM9-TIMM10 70 kDa complex mediates the import of much
CC more proteins (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterohexamer; composed of 3 copies of TIMM8 (TIMM8A or
CC TIMM8B) and 3 copies of TIMM13, named soluble 70 kDa complex.
CC Associates with the TIM22 complex, whose core is composed of TIMM22 (By
CC 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 TIMM13 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}.
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DR EMBL; BC076351; AAH76351.1; -; mRNA.
DR RefSeq; NP_001002465.1; NM_001002465.2.
DR AlphaFoldDB; Q6DGJ3; -.
DR SMR; Q6DGJ3; -.
DR STRING; 7955.ENSDARP00000075599; -.
DR PaxDb; Q6DGJ3; -.
DR PRIDE; Q6DGJ3; -.
DR Ensembl; ENSDART00000081156; ENSDARP00000075599; ENSDARG00000058297.
DR GeneID; 436738; -.
DR KEGG; dre:436738; -.
DR CTD; 26517; -.
DR ZFIN; ZDB-GENE-040718-167; timm13.
DR eggNOG; KOG1733; Eukaryota.
DR GeneTree; ENSGT00390000014000; -.
DR HOGENOM; CLU_141397_0_2_1; -.
DR InParanoid; Q6DGJ3; -.
DR OMA; MAAWNQV; -.
DR OrthoDB; 1566384at2759; -.
DR PhylomeDB; Q6DGJ3; -.
DR TreeFam; TF106194; -.
DR PRO; PR:Q6DGJ3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 22.
DR Bgee; ENSDARG00000058297; Expressed in somite and 35 other tissues.
DR ExpressionAtlas; Q6DGJ3; baseline and differential.
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..95
FT /note="Mitochondrial import inner membrane translocase
FT subunit Tim13"
FT /id="PRO_0000228066"
FT MOTIF 46..69
FT /note="Twin CX3C motif"
FT DISULFID 46..69
FT /evidence="ECO:0000250"
FT DISULFID 50..65
FT /evidence="ECO:0000250"
SQ SEQUENCE 95 AA; 10621 MW; 4AE085C71A1B4703 CRC64;
MEGFGSDFSS GSSSGKMDTG TIMEQVKVQI AVANAQELLQ RMTDKCFKKC IGKPGSTLDN
SEQKCIAMCM DRYMDAWNTV SRAYNSRLQR ERAHI