TIM8A_BOVIN
ID TIM8A_BOVIN Reviewed; 97 AA.
AC Q3ZBS8;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit Tim8 A;
GN Name=TIMM8A; Synonyms=TIM8A;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Reticulocyte;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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 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 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; BC103131; AAI03132.1; -; mRNA.
DR RefSeq; NP_001029652.1; NM_001034480.2.
DR AlphaFoldDB; Q3ZBS8; -.
DR SMR; Q3ZBS8; -.
DR STRING; 9913.ENSBTAP00000030114; -.
DR PaxDb; Q3ZBS8; -.
DR PRIDE; Q3ZBS8; -.
DR Ensembl; ENSBTAT00000030129; ENSBTAP00000030114; ENSBTAG00000022292.
DR GeneID; 515109; -.
DR KEGG; bta:515109; -.
DR CTD; 1678; -.
DR VEuPathDB; HostDB:ENSBTAG00000022292; -.
DR VGNC; VGNC:49578; TIMM8A.
DR eggNOG; KOG3489; Eukaryota.
DR GeneTree; ENSGT00940000154661; -.
DR HOGENOM; CLU_141397_1_2_1; -.
DR InParanoid; Q3ZBS8; -.
DR OMA; QATQVCL; -.
DR OrthoDB; 1593287at2759; -.
DR TreeFam; TF106191; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000022292; Expressed in oocyte and 106 other tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042719; C:mitochondrial intermembrane space protein transporter complex; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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; Phosphoprotein; Protein transport;
KW Reference proteome; Translocation; Transport; Zinc.
FT CHAIN 1..97
FT /note="Mitochondrial import inner membrane translocase
FT subunit Tim8 A"
FT /id="PRO_0000228020"
FT MOTIF 43..66
FT /note="Twin CX3C motif"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVA2"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVA2"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60220"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60220"
FT DISULFID 43..66
FT /evidence="ECO:0000250"
FT DISULFID 47..62
FT /evidence="ECO:0000250"
SQ SEQUENCE 97 AA; 11014 MW; 4840823C8F13F4AF CRC64;
MDSSSSSSAA GLGSVDPQLQ HFIEVETQKQ RFQQLVHQMT ELCWEKCMDK PGPKLDSRAE
ACFVNCVERF IDTSQFILNR LEQTQKSKPV FSESLSD