TIM8A_DANRE
ID TIM8A_DANRE Reviewed; 90 AA.
AC Q6DEM5;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit Tim8 A;
GN Name=timm8a; Synonyms=tim8a; ORFNames=zgc:100916;
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=Embryo;
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 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; BC077084; AAH77084.1; -; mRNA.
DR RefSeq; NP_001003637.1; NM_001003637.3.
DR AlphaFoldDB; Q6DEM5; -.
DR SMR; Q6DEM5; -.
DR STRING; 7955.ENSDARP00000043316; -.
DR PaxDb; Q6DEM5; -.
DR Ensembl; ENSDART00000043317; ENSDARP00000043316; ENSDARG00000023672.
DR GeneID; 445243; -.
DR KEGG; dre:445243; -.
DR CTD; 1678; -.
DR ZFIN; ZDB-GENE-040801-158; timm8a.
DR eggNOG; KOG3489; Eukaryota.
DR GeneTree; ENSGT00940000154661; -.
DR HOGENOM; CLU_141397_1_2_1; -.
DR InParanoid; Q6DEM5; -.
DR OMA; DVCFADY; -.
DR OrthoDB; 1593287at2759; -.
DR PhylomeDB; Q6DEM5; -.
DR TreeFam; TF106191; -.
DR PRO; PR:Q6DEM5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 14.
DR Bgee; ENSDARG00000023672; Expressed in tail and 22 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..90
FT /note="Mitochondrial import inner membrane translocase
FT subunit Tim8 A"
FT /id="PRO_0000228022"
FT MOTIF 36..59
FT /note="Twin CX3C motif"
FT DISULFID 36..59
FT /evidence="ECO:0000250"
FT DISULFID 40..55
FT /evidence="ECO:0000250"
SQ SEQUENCE 90 AA; 10563 MW; 16E0E1A375A28C9A CRC64;
MDTQGVATDP QLQQFIEIES QKQRFQQLVH QMTEVCWEKC MDKPGPKLDS RTEVCFVNCV
ERFIDTSQFI LNRLEQTQRS RGAFSETMTD