ID   TIM13_RAT               Reviewed;          95 AA.
AC   P62076; Q9UHL8; Q9WTL1;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit Tim13;
GN   Name=Timm13; Synonyms=Tim13a, Timm13a;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
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 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 proteins such as TIMM23,
CC       SLC25A12/ARALAR1 and SLC25A13/ARALAR2, while the predominant TIMM9-
CC       TIMM10 70 kDa complex mediates the import of much more proteins (By
CC       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; AF144701; AAD39952.1; -; mRNA.
DR   RefSeq; NP_665724.1; NM_145781.2.
DR   AlphaFoldDB; P62076; -.
DR   SMR; P62076; -.
DR   STRING; 10116.ENSRNOP00000026648; -.
DR   jPOST; P62076; -.
DR   PaxDb; P62076; -.
DR   PRIDE; P62076; -.
DR   GeneID; 252928; -.
DR   KEGG; rno:252928; -.
DR   UCSC; RGD:628845; rat.
DR   CTD; 26517; -.
DR   RGD; 628845; Timm13.
DR   eggNOG; KOG1733; Eukaryota.
DR   HOGENOM; CLU_141397_0_2_1; -.
DR   InParanoid; P62076; -.
DR   OMA; MAAWNQV; -.
DR   OrthoDB; 1566384at2759; -.
DR   PhylomeDB; P62076; -.
DR   TreeFam; TF106194; -.
DR   PRO; PR:P62076; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000019682; Expressed in pancreas and 19 other tissues.
DR   Genevisible; P62076; RN.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISO:RGD.
DR   GO; GO:0042719; C:mitochondrial intermembrane space protein transporter complex; ISO:RGD.
DR   GO; GO:0005739; C:mitochondrion; IDA:RGD.
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   Acetylation; Chaperone; Disulfide bond; Membrane; Metal-binding;
KW   Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW   Protein transport; Reference proteome; Translocation; Transport; Zinc.
FT   CHAIN           1..95
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit Tim13"
FT                   /id="PRO_0000193625"
FT   MOTIF           46..69
FT                   /note="Twin CX3C motif"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y5L4"
FT   MOD_RES         7
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y5L4"
FT   MOD_RES         53
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P62075"
FT   DISULFID        46..69
FT                   /evidence="ECO:0000250"
FT   DISULFID        50..65
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   95 AA;  10458 MW;  F9A50A2E7F6E64C8 CRC64;
     MDSGFGSDFG GTGGGKLDPG AIMEQVKVQI AVANAQELLQ RMTDKCFRKC IGKPGGSLDN
     SEQKCIAMCM DRYMDAWNTV SRAYNSRLQR ERANM