T10B_XENLA
ID T10B_XENLA Reviewed; 125 AA.
AC Q6GR66;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit Tim10 B;
DE AltName: Full=Mitochondrial import inner membrane translocase subunit Tim9 B;
GN Name=timm10b; Synonyms=fxc1, tim9b, timm9b;
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].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-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. {ECO:0000250|UniProtKB:Q9Y5J6}.
CC -!- SUBUNIT: Component of the TIM22 complex.
CC {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}.
CC -!- SIMILARITY: Belongs to the small Tim family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC071063; AAH71063.1; -; mRNA.
DR RefSeq; NP_001085318.1; NM_001091849.1.
DR AlphaFoldDB; Q6GR66; -.
DR SMR; Q6GR66; -.
DR GeneID; 443743; -.
DR KEGG; xla:443743; -.
DR CTD; 443743; -.
DR Xenbase; XB-GENE-6251887; timm10b.S.
DR OrthoDB; 1627953at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 443743; Expressed in oocyte and 19 other tissues.
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 2: Evidence at transcript level;
KW Disulfide bond; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Protein transport; Reference proteome;
KW Translocation; Transport; Zinc.
FT CHAIN 1..125
FT /note="Mitochondrial import inner membrane translocase
FT subunit Tim10 B"
FT /id="PRO_0000228052"
FT REGION 87..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 25..49
FT /note="Twin CX3C motif"
FT COMPBIAS 101..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 25..49
FT /evidence="ECO:0000250|UniProtKB:P87108"
FT DISULFID 29..45
FT /evidence="ECO:0000250|UniProtKB:P87108"
SQ SEQUENCE 125 AA; 14038 MW; 11E3155204FC457D CRC64;
MEGEQQQLRN LRDFLLVYNK MTELCFSRCA KNLNYRSVTM EEEQCLDSCA SKFIRANHRL
MSAYVSLMPS VVQRRMAEYE GAAANVPPIE TEPSADHMPP VISSHSGNSP TNKQLDSVSD
LPVGK