ID   T10B_PONAB              Reviewed;         102 AA.
AC   Q5RDJ0;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit Tim10 B;
DE   AltName: Full=Mitochondrial import inner membrane translocase subunit Tim9 B;
DE   AltName: Full=TIMM10B;
DE            Short=Tim10b;
GN   Name=TIMM10B; Synonyms=FXC1, TIM9B, TIMM9B;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the TIM22 complex, a complex that mediates the
CC       import and insertion of multi-pass transmembrane proteins into the
CC       mitochondrial inner membrane. The TIM22 complex forms a twin-pore
CC       translocase that uses the membrane potential as the external driving
CC       force. In the TIM22 complex, it may act as a docking point for the
CC       soluble 70 kDa complex that guides the target proteins in transit
CC       through the aqueous mitochondrial intermembrane space.
CC       {ECO:0000250|UniProtKB:Q9Y5J6}.
CC   -!- SUBUNIT: Component of the TIM22 complex, which core is composed of
CC       TIMM22, associated with TIMM10 (TIMM10A and/or TIMM10B), TIMM9, AGK and
CC       TIMM29. {ECO:0000250|UniProtKB:Q9Y5J6}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:Q9Y5J6}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q9Y5J6}.
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 TIMM10B from cytoplasm into mitochondrion, the
CC       Cys residues probably coordinate zinc, thereby preventing folding and
CC       allowing its transfer across mitochondrial outer membrane.
CC       {ECO:0000250|UniProtKB:P87108}.
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DR   EMBL; CR857919; CAH90167.1; -; mRNA.
DR   RefSeq; NP_001125053.1; NM_001131581.1.
DR   AlphaFoldDB; Q5RDJ0; -.
DR   SMR; Q5RDJ0; -.
DR   STRING; 9601.ENSPPYP00000004060; -.
DR   Ensembl; ENSPPYT00000055128; ENSPPYP00000045083; ENSPPYG00000003541.
DR   GeneID; 100171934; -.
DR   KEGG; pon:100171934; -.
DR   CTD; 26515; -.
DR   eggNOG; KOG3479; Eukaryota.
DR   GeneTree; ENSGT00450000040326; -.
DR   HOGENOM; CLU_141397_2_2_1; -.
DR   InParanoid; Q5RDJ0; -.
DR   OMA; CFNRCVD; -.
DR   OrthoDB; 1627953at2759; -.
DR   TreeFam; TF106188; -.
DR   Proteomes; UP000001595; Chromosome 11.
DR   GO; GO:0042719; C:mitochondrial intermembrane space protein transporter complex; IEA:UniProt.
DR   GO; GO:0042721; C:TIM22 mitochondrial import inner membrane insertion complex; ISS:UniProtKB.
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   Pfam; PF02953; zf-Tim10_DDP; 1.
DR   SUPFAM; SSF144122; SSF144122; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Protein transport; Reference proteome;
KW   Translocation; Transport; Zinc.
FT   CHAIN           1..102
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit Tim10 B"
FT                   /id="PRO_0000228050"
FT   MOTIF           27..51
FT                   /note="Twin CX3C motif"
FT   DISULFID        27..51
FT                   /evidence="ECO:0000250|UniProtKB:P87108"
FT   DISULFID        31..47
FT                   /evidence="ECO:0000250|UniProtKB:P87108"
SQ   SEQUENCE   102 AA;  11430 MW;  84A3E3C945D124A5 CRC64;
     MEQQQQQQQL RNLRDFLLVY NRMTELCFQR CVPSLHHRAL DAEEEACLHS CAGKLIHSNH
     RLMAAYVQLM PALVQRRIAD YEAASAVPGV AAEQPGVSPS GS