T10B_HUMAN
ID T10B_HUMAN Reviewed; 103 AA.
AC Q9Y5J6; Q96FF3;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit Tim10 B;
DE AltName: Full=Fracture callus protein 1;
DE AltName: Full=FxC1;
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10552927; DOI=10.1006/geno.1999.5966;
RA Jin H., Kendall E., Freeman T.C., Roberts R.G., Vetrie D.L.P.;
RT "The human family of deafness/dystonia peptide (DDP) related mitochondrial
RT import proteins.";
RL Genomics 61:259-267(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pheochromocytoma;
RA Peng Y., Li Y., Jia J., Xu S., Han Z., Fu G., Chen Z.;
RT "A novel gene expressed in human pheochromocytoma.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-90.
RC TISSUE=Bone marrow;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=11489896; DOI=10.1074/jbc.m105313200;
RA Rothbauer U., Hofmann S., Muehlenbein N., Paschen S.A., Gerbitz K.-D.,
RA Neupert W., Brunner M., Bauer M.F.;
RT "Role of the deafness dystonia peptide 1 (DDP1) in import of human Tim23
RT into the inner membrane of mitochondria.";
RL J. Biol. Chem. 276:37327-37334(2001).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP TIMM9; TIMM10A AND TIMM22.
RX PubMed=14726512; DOI=10.1074/jbc.m312485200;
RA Muehlenbein N., Hofmann S., Rothbauer U., Bauer M.F.;
RT "Organization and function of the small Tim complexes acting along the
RT import pathway of metabolite carriers into mammalian mitochondria.";
RL J. Biol. Chem. 279:13540-13546(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [9]
RP IDENTIFICATION IN THE TIM22 COMPLEX.
RX PubMed=28712724; DOI=10.1016/j.molcel.2017.06.013;
RA Vukotic M., Nolte H., Koenig T., Saita S., Ananjew M., Krueger M.,
RA Tatsuta T., Langer T.;
RT "Acylglycerol kinase mutated in Sengers Syndrome is a subunit of the TIM22
RT protein translocase in mitochondria.";
RL Mol. Cell 0:0-0(2017).
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:0000269|PubMed:14726512}.
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 (PubMed:28712724). {ECO:0000269|PubMed:14726512,
CC ECO:0000269|PubMed:28712724}.
CC -!- INTERACTION:
CC Q9Y5J6; O00303: EIF3F; NbExp=3; IntAct=EBI-1200382, EBI-711990;
CC Q9Y5J6; O14964: HGS; NbExp=3; IntAct=EBI-1200382, EBI-740220;
CC Q9Y5J6; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-1200382, EBI-6426443;
CC Q9Y5J6; O95983-2: MBD3; NbExp=3; IntAct=EBI-1200382, EBI-11978579;
CC Q9Y5J6; O14770-4: MEIS2; NbExp=3; IntAct=EBI-1200382, EBI-8025850;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:11489896, ECO:0000269|PubMed:14726512}; Peripheral
CC membrane protein {ECO:0000269|PubMed:11489896,
CC ECO:0000269|PubMed:14726512}.
CC -!- TISSUE SPECIFICITY: Ubiquitous, with highest expression in heart,
CC kidney, liver and skeletal muscle. {ECO:0000269|PubMed:10611480,
CC ECO:0000269|PubMed:14726512}.
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}.
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DR EMBL; AF152355; AAF15105.1; -; mRNA.
DR EMBL; AF150105; AAD40011.1; -; mRNA.
DR EMBL; AF183415; AAG09684.1; -; mRNA.
DR EMBL; BC011014; AAH11014.1; -; mRNA.
DR CCDS; CCDS7766.1; -.
DR RefSeq; NP_036324.1; NM_012192.3.
DR PDB; 7CGP; EM; 3.70 A; J=1-103.
DR PDBsum; 7CGP; -.
DR AlphaFoldDB; Q9Y5J6; -.
DR SMR; Q9Y5J6; -.
DR BioGRID; 117720; 25.
DR ComplexPortal; CPX-6126; TIM9-TIM10-TIM10B mitochondrial intermembrane space protein transporter complex.
DR IntAct; Q9Y5J6; 13.
DR STRING; 9606.ENSP00000254616; -.
DR GlyGen; Q9Y5J6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y5J6; -.
DR PhosphoSitePlus; Q9Y5J6; -.
DR BioMuta; TIMM10B; -.
DR EPD; Q9Y5J6; -.
DR jPOST; Q9Y5J6; -.
DR MassIVE; Q9Y5J6; -.
DR MaxQB; Q9Y5J6; -.
DR PaxDb; Q9Y5J6; -.
DR PeptideAtlas; Q9Y5J6; -.
DR PRIDE; Q9Y5J6; -.
DR ProteomicsDB; 86421; -.
DR TopDownProteomics; Q9Y5J6; -.
DR Antibodypedia; 23876; 110 antibodies from 20 providers.
DR DNASU; 26515; -.
DR Ensembl; ENST00000254616.11; ENSP00000254616.6; ENSG00000132286.12.
DR Ensembl; ENST00000533379.1; ENSP00000436948.1; ENSG00000132286.12.
DR GeneID; 26515; -.
DR KEGG; hsa:26515; -.
DR MANE-Select; ENST00000254616.11; ENSP00000254616.6; NM_012192.4; NP_036324.1.
DR UCSC; uc001mdn.5; human.
DR CTD; 26515; -.
DR GeneCards; TIMM10B; -.
DR HGNC; HGNC:4022; TIMM10B.
DR HPA; ENSG00000132286; Low tissue specificity.
DR MIM; 607388; gene.
DR neXtProt; NX_Q9Y5J6; -.
DR OpenTargets; ENSG00000132286; -.
DR PharmGKB; PA28438; -.
DR VEuPathDB; HostDB:ENSG00000132286; -.
DR eggNOG; KOG3479; Eukaryota.
DR GeneTree; ENSGT00450000040326; -.
DR HOGENOM; CLU_141397_2_2_1; -.
DR InParanoid; Q9Y5J6; -.
DR OMA; CFNRCVD; -.
DR OrthoDB; 1627953at2759; -.
DR PhylomeDB; Q9Y5J6; -.
DR TreeFam; TF106188; -.
DR PathwayCommons; Q9Y5J6; -.
DR Reactome; R-HSA-1268020; Mitochondrial protein import.
DR SignaLink; Q9Y5J6; -.
DR BioGRID-ORCS; 26515; 17 hits in 1081 CRISPR screens.
DR ChiTaRS; TIMM10B; human.
DR GeneWiki; FXC1; -.
DR GenomeRNAi; 26515; -.
DR Pharos; Q9Y5J6; Tdark.
DR PRO; PR:Q9Y5J6; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9Y5J6; protein.
DR Bgee; ENSG00000132286; Expressed in secondary oocyte and 186 other tissues.
DR ExpressionAtlas; Q9Y5J6; baseline and differential.
DR Genevisible; Q9Y5J6; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:BHF-UCL.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:ComplexPortal.
DR GO; GO:0042719; C:mitochondrial intermembrane space protein transporter complex; IDA:BHF-UCL.
DR GO; GO:0042721; C:TIM22 mitochondrial import inner membrane insertion complex; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140318; F:protein transporter activity; ISS:FlyBase.
DR GO; GO:0051082; F:unfolded protein binding; ISS:FlyBase.
DR GO; GO:0007160; P:cell-matrix adhesion; TAS:ProtInc.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; ISS:FlyBase.
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 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Protein transport; Reference proteome;
KW Translocation; Transport; Zinc.
FT CHAIN 1..103
FT /note="Mitochondrial import inner membrane translocase
FT subunit Tim10 B"
FT /id="PRO_0000193598"
FT MOTIF 28..52
FT /note="Twin CX3C motif"
FT DISULFID 28..52
FT /evidence="ECO:0000250|UniProtKB:P87108"
FT DISULFID 32..48
FT /evidence="ECO:0000250|UniProtKB:P87108"
FT VARIANT 66
FT /note="A -> S (in dbSNP:rs60702727)"
FT /id="VAR_061843"
FT VARIANT 90
FT /note="G -> S (in dbSNP:rs17850713)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_025665"
SQ SEQUENCE 103 AA; 11586 MW; B76CCC81668B1F31 CRC64;
MERQQQQQQQ LRNLRDFLLV YNRMTELCFQ RCVPSLHHRA LDAEEEACLH SCAGKLIHSN
HRLMAAYVQL MPALVQRRIA DYEAASAVPG VAAEQPGVSP SGS
