ID   TIM8B_BOVIN             Reviewed;          83 AA.
AC   Q3SZ93;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit Tim8 B;
GN   Name=TIMM8B;
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=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable mitochondrial intermembrane chaperone that
CC       participates in the import and insertion of some multi-pass
CC       transmembrane proteins into the mitochondrial inner membrane. Also
CC       required for the transfer of beta-barrel precursors from the TOM
CC       complex to the sorting and assembly machinery (SAM complex) of the
CC       outer membrane. Acts as a chaperone-like protein that protects the
CC       hydrophobic precursors from aggregation and guide them through the
CC       mitochondrial intermembrane space (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heterohexamer; possibly composed of 3 copies of TIMM8B and 3
CC       copies of TIMM13, named soluble 70 kDa complex. Associates with the
CC       TIM22 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 TIMM8B 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; BC103032; AAI03033.1; -; mRNA.
DR   RefSeq; NP_001032718.1; NM_001037629.1.
DR   AlphaFoldDB; Q3SZ93; -.
DR   SMR; Q3SZ93; -.
DR   STRING; 9913.ENSBTAP00000002594; -.
DR   PaxDb; Q3SZ93; -.
DR   Ensembl; ENSBTAT00000002594; ENSBTAP00000002594; ENSBTAG00000002000.
DR   GeneID; 618131; -.
DR   KEGG; bta:618131; -.
DR   CTD; 26521; -.
DR   VEuPathDB; HostDB:ENSBTAG00000002000; -.
DR   VGNC; VGNC:54899; TIMM8B.
DR   eggNOG; KOG3489; Eukaryota.
DR   GeneTree; ENSGT00940000155479; -.
DR   HOGENOM; CLU_141397_1_2_1; -.
DR   InParanoid; Q3SZ93; -.
DR   OMA; SKQKVQM; -.
DR   OrthoDB; 1593287at2759; -.
DR   TreeFam; TF106191; -.
DR   Proteomes; UP000009136; Chromosome 15.
DR   Bgee; ENSBTAG00000002000; Expressed in semen and 106 other tissues.
DR   ExpressionAtlas; Q3SZ93; baseline and differential.
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   Acetylation; Chaperone; Disulfide bond; Membrane; Metal-binding;
KW   Mitochondrion; Mitochondrion inner membrane; Protein transport;
KW   Reference proteome; Translocation; Transport; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y5J9"
FT   CHAIN           2..83
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit Tim8 B"
FT                   /id="PRO_0000228025"
FT   MOTIF           36..59
FT                   /note="Twin CX3C motif"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y5J9"
FT   DISULFID        36..59
FT                   /evidence="ECO:0000250"
FT   DISULFID        40..55
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   83 AA;  9372 MW;  9DC47BA345DB8692 CRC64;
     MAELGEADEA ELQRLVAAEQ QKAQFTAQVH HFMELCWDKC VEKPGNRLDS RTENCLSSCV
     DRFIDTTLAI TSRFAQIVQR GGQ