T10B_CAEEL
ID T10B_CAEEL Reviewed; 111 AA.
AC Q9Y0V2; Q5FC56;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit Tim10B;
DE AltName: Full=Mitochondrial import inner membrane translocase subunit Tim9B;
DE AltName: Full=Tim-10b;
DE AltName: Full=Tim10b;
GN Name=tin-9.2; Synonyms=tim-9b; ORFNames=B0564.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10611480; DOI=10.1016/s0014-5793(99)01665-8;
RA Bauer M.F., Rothbauer U., Muehlenbein N., Smith R.J.H., Gerbitz K.-D.,
RA Neupert W., Brunner M., Hofmann S.;
RT "The mitochondrial TIM22 preprotein translocase is highly conserved
RT throughout the eukaryotic kingdom.";
RL FEBS Lett. 464:41-47(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP SUBCELLULAR LOCATION, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15485840; DOI=10.1074/jbc.m409618200;
RA Curran S.P., Leverich E.P., Koehler C.M., Larsen P.L.;
RT "Defective mitochondrial protein translocation precludes normal
RT Caenorhabditis elegans development.";
RL J. Biol. Chem. 279:54655-54662(2004).
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 (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:15485840}.
CC -!- SUBUNIT: Component of the TIM22 complex, whose core is composed of tim-
CC 22, associated with peripheral protein tin-9.2/tim-10b and the 70 kDa
CC heterohexamer. In most cases, the 70 kDa complex is composed of TIMM9
CC and TIMM10 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:15485840}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15485840}.
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 tin-9.2/tim-10b from the cytoplasm into the
CC mitochondrion, the Cys residues probably coordinate zinc, thereby
CC preventing folding and allowing its transfer across the mitochondrial
CC outer membrane (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Worms display a small body size, a reduced number
CC of progeny, partial embryonic lethality and defective formation of the
CC somatic gonad due to defects in import of proteins into mitochondria.
CC {ECO:0000269|PubMed:15485840}.
CC -!- SIMILARITY: Belongs to the small Tim family. {ECO:0000305}.
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DR EMBL; AF150109; AAD40015.1; -; mRNA.
DR EMBL; Z73422; CAI46556.1; -; Genomic_DNA.
DR RefSeq; NP_001021275.1; NM_001026104.4.
DR AlphaFoldDB; Q9Y0V2; -.
DR SMR; Q9Y0V2; -.
DR IntAct; Q9Y0V2; 1.
DR STRING; 6239.B0564.1b.2; -.
DR EPD; Q9Y0V2; -.
DR PeptideAtlas; Q9Y0V2; -.
DR EnsemblMetazoa; B0564.1b.1; B0564.1b.1; WBGene00044083.
DR EnsemblMetazoa; B0564.1b.2; B0564.1b.2; WBGene00044083.
DR UCSC; B0564.1b.1; c. elegans.
DR WormBase; B0564.1b; CE37950; WBGene00044083; tin-9.2.
DR eggNOG; ENOG502SGVK; Eukaryota.
DR HOGENOM; CLU_2199383_0_0_1; -.
DR OMA; CFKKCAN; -.
DR OrthoDB; 1627953at2759; -.
DR PhylomeDB; Q9Y0V2; -.
DR PRO; PR:Q9Y0V2; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00044083; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q9Y0V2; baseline and differential.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0040039; P:inductive cell migration; IMP:WormBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:WormBase.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
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..111
FT /note="Mitochondrial import inner membrane translocase
FT subunit Tim10B"
FT /id="PRO_0000193602"
FT REGION 73..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 24..48
FT /note="Twin CX3C motif"
FT DISULFID 24..48
FT /evidence="ECO:0000250"
FT DISULFID 28..44
FT /evidence="ECO:0000250"
SQ SEQUENCE 111 AA; 12456 MW; C4B9154B15C7439F CRC64;
MNTIQNIQQL REFLTVYNTL SERCFNACAR DYTTSTLTKD EGSCVSQCID KQMLVNRRFM
LVFAEQAPKA LFKQGEQSPT EAIKSAKPEP AVPAPEATPV ETTPVIEENK Q
