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 27-MAR-2024, entry version 166. 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 EMDB; EMD-9958; -. DR SMR; P62072; -. DR BioGRID; 117723; 100. 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; 20. 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; 9606-ENSP00000257245; -. DR PeptideAtlas; P62072; -. DR ProteomicsDB; 57362; -. DR Pumba; P62072; -. DR TopDownProteomics; P62072; -. DR Antibodypedia; 43246; 109 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 AGR; HGNC:11814; -. 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; VGENMQK; -. DR OrthoDB; 2872226at2759; -. 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; 695 hits in 1144 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 191 other cell types or tissues. 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:0032977; F:membrane insertase activity; IDA:BHF-UCL. DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL. DR GO; GO:0051087; F:protein-folding chaperone binding; 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; Mitochondrial import inner membrane translocase subunit tim13 like domains; 1. DR InterPro; IPR004217; Tim10-like. DR InterPro; IPR035427; Tim10-like_dom_sf. DR PANTHER; PTHR11038; MITOCHONDRIAL IMPORT INNER MEMBRANE TRANSLOCASE SUBUNIT TIM10; 1. DR PANTHER; PTHR11038:SF16; MITOCHONDRIAL IMPORT INNER MEMBRANE TRANSLOCASE SUBUNIT TIM10; 1. DR Pfam; PF02953; zf-Tim10_DDP; 1. DR SUPFAM; SSF144122; Tim10-like; 1. DR Genevisible; P62072; HS. 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 //