TIM10_HUMAN
ID TIM10_HUMAN Reviewed; 90 AA.
AC P62072; A8K136; Q9WV99; Q9WVA0; Q9Y5J8;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit Tim10;
GN Name=TIMM10; Synonyms=TIM10;
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], 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [6]
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TIMM9; TIMM22 AND
RP FXC1.
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 [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
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 [11]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) IN COMPLEX WITH TIMM9, AND DISULFIDE
RP BONDS.
RX PubMed=16387659; DOI=10.1016/j.molcel.2005.11.010;
RA Webb C.T., Gorman M.A., Lazarou M., Ryan M.T., Gulbis J.M.;
RT "Crystal structure of the mitochondrial chaperone TIM9.10 reveals a six-
RT bladed alpha-propeller.";
RL Mol. Cell 21:123-133(2006).
CC -!- FUNCTION: Mitochondrial intermembrane chaperone that participates in
CC the import and insertion of multi-pass transmembrane proteins into the
CC mitochondrial inner membrane. May also be required for the transfer of
CC beta-barrel precursors from the TOM complex to the sorting and assembly
CC machinery (SAM complex) of the outer membrane. Acts as a chaperone-like
CC protein that protects the hydrophobic precursors from aggregation and
CC guide them through the mitochondrial intermembrane space.
CC {ECO:0000269|PubMed:14726512}.
CC -!- SUBUNIT: Heterohexamer; composed of 3 copies of TIMM9 and 3 copies of
CC TIMM10/TIM10A, named soluble 70 kDa complex. The complex forms a 6-
CC bladed alpha-propeller structure and associates with the TIMM22
CC component of the TIM22 complex. Interacts with multi-pass transmembrane
CC proteins in transit. Also forms a complex composed of TIMM9,
CC TIMM10/TIM10A and FXC1/TIM10B. {ECO:0000269|PubMed:14726512,
CC ECO:0000269|PubMed:16387659}.
CC -!- INTERACTION:
CC P62072; A0A0B4J2F2: SIK1B; NbExp=3; IntAct=EBI-1200391, EBI-22345187;
CC P62072; Q8IYX1: TBC1D21; NbExp=3; IntAct=EBI-1200391, EBI-12018146;
CC P62072; Q9Y5J7: TIMM9; NbExp=5; IntAct=EBI-1200391, EBI-1200370;
CC P62072; Q8N720: ZNF655; NbExp=3; IntAct=EBI-1200391, EBI-625509;
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}; Intermembrane side
CC {ECO:0000269|PubMed:11489896, ECO:0000269|PubMed:14726512}.
CC -!- TISSUE SPECIFICITY: Ubiquitous, with highest expression in heart,
CC kidney, liver and skeletal muscle. {ECO:0000269|PubMed:10552927,
CC ECO:0000269|PubMed:10611480}.
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 TIMM10 from cytoplasm into mitochondrion, the Cys
CC residues probably coordinate zinc, thereby preventing folding and
CC allowing its transfer across mitochondrial outer membrane (Probable).
CC {ECO:0000305}.
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; AF150089; AAD39995.1; -; mRNA.
DR EMBL; AF152354; AAF15104.1; -; mRNA.
DR EMBL; AK289751; BAF82440.1; -; mRNA.
DR EMBL; CH471076; EAW73753.1; -; Genomic_DNA.
DR EMBL; BC032133; AAH32133.1; -; mRNA.
DR CCDS; CCDS7959.1; -.
DR RefSeq; NP_036588.1; NM_012456.2.
DR PDB; 2BSK; X-ray; 3.30 A; B/D/F=1-90.
DR PDB; 7CGP; EM; 3.70 A; G/H/I/M/N/O=1-90.
DR PDBsum; 2BSK; -.
DR PDBsum; 7CGP; -.
DR AlphaFoldDB; P62072; -.
DR SMR; P62072; -.
DR BioGRID; 117723; 95.
DR ComplexPortal; CPX-6124; TIM22 mitochondrial inner membrane twin-pore carrier translocase complex.
DR ComplexPortal; CPX-6125; TIM9-TIM10 mitochondrial intermembrane space protein transporter complex.
DR ComplexPortal; CPX-6126; TIM9-TIM10-TIM10B mitochondrial intermembrane space protein transporter complex.
DR CORUM; P62072; -.
DR IntAct; P62072; 19.
DR MINT; P62072; -.
DR STRING; 9606.ENSP00000257245; -.
DR GlyGen; P62072; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62072; -.
DR MetOSite; P62072; -.
DR PhosphoSitePlus; P62072; -.
DR BioMuta; TIMM10; -.
DR DMDM; 49065657; -.
DR EPD; P62072; -.
DR jPOST; P62072; -.
DR MassIVE; P62072; -.
DR MaxQB; P62072; -.
DR PaxDb; P62072; -.
DR PeptideAtlas; P62072; -.
DR PRIDE; P62072; -.
DR ProteomicsDB; 57362; -.
DR TopDownProteomics; P62072; -.
DR Antibodypedia; 43246; 100 antibodies from 22 providers.
DR DNASU; 26519; -.
DR Ensembl; ENST00000257245.9; ENSP00000257245.4; ENSG00000134809.9.
DR Ensembl; ENST00000525158.1; ENSP00000433627.1; ENSG00000134809.9.
DR Ensembl; ENST00000525587.1; ENSP00000435678.1; ENSG00000134809.9.
DR GeneID; 26519; -.
DR KEGG; hsa:26519; -.
DR MANE-Select; ENST00000257245.9; ENSP00000257245.4; NM_012456.3; NP_036588.1.
DR UCSC; uc001nkm.2; human.
DR CTD; 26519; -.
DR DisGeNET; 26519; -.
DR GeneCards; TIMM10; -.
DR HGNC; HGNC:11814; TIMM10.
DR HPA; ENSG00000134809; Low tissue specificity.
DR MIM; 602251; gene.
DR neXtProt; NX_P62072; -.
DR OpenTargets; ENSG00000134809; -.
DR PharmGKB; PA36521; -.
DR VEuPathDB; HostDB:ENSG00000134809; -.
DR eggNOG; KOG3480; Eukaryota.
DR GeneTree; ENSGT00390000003068; -.
DR HOGENOM; CLU_162151_2_0_1; -.
DR InParanoid; P62072; -.
DR OMA; ELEIEMM; -.
DR OrthoDB; 1477334at2759; -.
DR PhylomeDB; P62072; -.
DR TreeFam; TF106193; -.
DR PathwayCommons; P62072; -.
DR Reactome; R-HSA-1268020; Mitochondrial protein import.
DR SignaLink; P62072; -.
DR SIGNOR; P62072; -.
DR BioGRID-ORCS; 26519; 660 hits in 1060 CRISPR screens.
DR ChiTaRS; TIMM10; human.
DR EvolutionaryTrace; P62072; -.
DR GeneWiki; TIMM10; -.
DR GenomeRNAi; 26519; -.
DR Pharos; P62072; Tbio.
DR PRO; PR:P62072; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P62072; protein.
DR Bgee; ENSG00000134809; Expressed in gingival epithelium and 189 other tissues.
DR Genevisible; P62072; 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:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0042721; C:TIM22 mitochondrial import inner membrane insertion complex; IPI:ComplexPortal.
DR GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; TAS:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; IPI:BHF-UCL.
DR GO; GO:0032977; F:membrane insertase activity; IDA:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR GO; GO:0008270; F:zinc ion binding; TAS:UniProtKB.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IDA:BHF-UCL.
DR GO; GO:0006626; P:protein targeting to mitochondrion; TAS:UniProtKB.
DR GO; GO:0007605; P:sensory perception of sound; TAS:UniProtKB.
DR Gene3D; 1.10.287.810; -; 1.
DR InterPro; IPR027100; Tim10.
DR InterPro; IPR004217; Tim10-like.
DR InterPro; IPR035427; Tim10-like_dom_sf.
DR PANTHER; PTHR11038:SF16; PTHR11038:SF16; 1.
DR Pfam; PF02953; zf-Tim10_DDP; 1.
DR SUPFAM; SSF144122; SSF144122; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Disulfide bond; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Protein transport;
KW Reference proteome; Translocation; Transport; Zinc.
FT CHAIN 1..90
FT /note="Mitochondrial import inner membrane translocase
FT subunit Tim10"
FT /id="PRO_0000193612"
FT MOTIF 29..54
FT /note="Twin CX3C motif"
FT DISULFID 29..54
FT /evidence="ECO:0000269|PubMed:16387659"
FT DISULFID 33..50
FT /evidence="ECO:0000269|PubMed:16387659"
FT HELIX 5..10
FT /evidence="ECO:0007829|PDB:2BSK"
FT TURN 14..18
FT /evidence="ECO:0007829|PDB:2BSK"
FT HELIX 19..33
FT /evidence="ECO:0007829|PDB:2BSK"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:2BSK"
FT HELIX 45..74
FT /evidence="ECO:0007829|PDB:2BSK"
FT HELIX 80..86
FT /evidence="ECO:0007829|PDB:2BSK"
SQ SEQUENCE 90 AA; 10333 MW; D20EFAE694D14BAB CRC64;
MDPLRAQQLA AELEVEMMAD MYNRMTSACH RKCVPPHYKE AELSKGESVC LDRCVSKYLD
IHERMGKKLT ELSMQDEELM KRVQQSSGPA
