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TIM8A_XENLA
ID   TIM8A_XENLA             Reviewed;          94 AA.
AC   Q66L32;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit Tim8 A;
GN   Name=timm8a; Synonyms=tim8a;
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].
RG   NIH - Xenopus Gene Collection (XGC) 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 TIMM8A and 3 copies of
CC       TIMM13, named soluble 70 kDa complex. Associates with the TIM22
CC       complex, whose core is composed of TIMM22 (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 TIMM8A 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; BC078465; AAH78465.1; -; mRNA.
DR   RefSeq; NP_001087186.1; NM_001093717.1.
DR   AlphaFoldDB; Q66L32; -.
DR   SMR; Q66L32; -.
DR   DNASU; 447075; -.
DR   GeneID; 447075; -.
DR   KEGG; xla:447075; -.
DR   CTD; 447075; -.
DR   Xenbase; XB-GENE-6254561; timm8b.L.
DR   OMA; SKQKVQM; -.
DR   OrthoDB; 1593287at2759; -.
DR   Proteomes; UP000186698; Chromosome 7L.
DR   Bgee; 447075; 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..94
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit Tim8 A"
FT                   /id="PRO_0000228024"
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   94 AA;  10409 MW;  404CA99E9B0E72F6 CRC64;
     MSDFDSNLDL AGTGASPAEA AELQRMLAVE QQKAQFTAQV HNFMDVCWDK CIDRPGNKLD
     SRTESCLVSC VDRFIDTTLS ITNRFAQIVQ KGAH
 
 
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