TI13A_XENLA
ID TI13A_XENLA Reviewed; 96 AA.
AC Q6GPY0;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit Tim13-A;
GN Name=timm13-a; Synonyms=tim13a-a, timm13a-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-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-A from cytoplasm into mitochondrion, the
CC Cys 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH72975.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC072975; AAH72975.1; ALT_INIT; mRNA.
DR RefSeq; NP_001093227.1; NM_001099757.1.
DR AlphaFoldDB; Q6GPY0; -.
DR SMR; Q6GPY0; -.
DR GeneID; 443601; -.
DR KEGG; xla:443601; -.
DR CTD; 443601; -.
DR Xenbase; XB-GENE-993983; timm13.L.
DR OMA; MAAWNQV; -.
DR OrthoDB; 1566384at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 443601; Expressed in muscle tissue and 19 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: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..96
FT /note="Mitochondrial import inner membrane translocase
FT subunit Tim13-A"
FT /id="PRO_0000228067"
FT MOTIF 47..70
FT /note="Twin CX3C motif"
FT DISULFID 47..70
FT /evidence="ECO:0000250"
FT DISULFID 51..66
FT /evidence="ECO:0000250"
SQ SEQUENCE 96 AA; 10605 MW; 51A7D2C04704C31A CRC64;
MEGFGSDFSV GGSSAGKVDT GAIMEQVKVQ IAVANAQELL QRMTDKCFRK CIGKPGGSLD
NSEQKCIAMC MDRYMDAWNT VSRAYNSRLQ RERAKM