TIM8B_HUMAN
ID TIM8B_HUMAN Reviewed; 83 AA.
AC Q9Y5J9; B0YJA5; Q3KQS9; Q9UN04;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit Tim8 B;
DE AltName: Full=DDP-like protein;
DE AltName: Full=Deafness dystonia protein 2;
GN Name=TIMM8B; Synonyms=DDP2, DDPL, TIM8B;
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=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 [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, Mammary gland, and Testis;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 33-83.
RC TISSUE=Heart;
RA Xia J.-H., He Y.-G., Yu K.-P., Zheng Z.-H., Tan S.;
RT "Molecular cloning of DDP-like gene.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
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).
CC -!- FUNCTION: Probable mitochondrial intermembrane chaperone that
CC participates in the import and insertion of some multi-pass
CC transmembrane proteins into the mitochondrial inner membrane. Also
CC required for the transfer of beta-barrel precursors from the TOM
CC complex to the sorting and assembly machinery (SAM complex) of the
CC outer membrane. Acts as a chaperone-like protein that protects the
CC hydrophobic precursors from aggregation and guide them through the
CC mitochondrial intermembrane space (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterohexamer; possibly composed of 3 copies of TIMM8B and 3
CC copies of TIMM13, named soluble 70 kDa complex. Associates with the
CC TIM22 complex, whose core is composed of TIMM22 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Intermembrane side
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous, with highest expression in heart,
CC kidney, liver and skeletal muscle. {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 TIMM8B from cytoplasm into mitochondrion, the Cys
CC residues probably coordinate zinc, thereby preventing folding and
CC allowing its transfer across mitochondrial outer membrane (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small Tim family. {ECO:0000305}.
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DR EMBL; AF152350; AAF15100.1; -; mRNA.
DR EMBL; AF150087; AAD39994.1; -; mRNA.
DR EMBL; AK312169; BAG35103.1; -; mRNA.
DR EMBL; EF445036; ACA06083.1; -; Genomic_DNA.
DR EMBL; BC000711; AAH00711.1; -; mRNA.
DR EMBL; BC105986; AAI05987.1; -; mRNA.
DR EMBL; BC106067; AAI06068.1; -; mRNA.
DR EMBL; AF165967; AAD51801.1; -; mRNA.
DR CCDS; CCDS8357.2; -.
DR RefSeq; NP_036591.2; NM_012459.2.
DR AlphaFoldDB; Q9Y5J9; -.
DR SMR; Q9Y5J9; -.
DR BioGRID; 117725; 48.
DR ComplexPortal; CPX-6132; TIM8B-TIM13 mitochondrial intermembrane space protein transporter complex.
DR IntAct; Q9Y5J9; 35.
DR MINT; Q9Y5J9; -.
DR STRING; 9606.ENSP00000438455; -.
DR iPTMnet; Q9Y5J9; -.
DR PhosphoSitePlus; Q9Y5J9; -.
DR BioMuta; TIMM8B; -.
DR EPD; Q9Y5J9; -.
DR jPOST; Q9Y5J9; -.
DR MassIVE; Q9Y5J9; -.
DR MaxQB; Q9Y5J9; -.
DR PaxDb; Q9Y5J9; -.
DR PeptideAtlas; Q9Y5J9; -.
DR PRIDE; Q9Y5J9; -.
DR ProteomicsDB; 86423; -.
DR TopDownProteomics; Q9Y5J9; -.
DR Antibodypedia; 32120; 88 antibodies from 14 providers.
DR DNASU; 26521; -.
DR Ensembl; ENST00000504148.3; ENSP00000422122.2; ENSG00000150779.12.
DR GeneID; 26521; -.
DR KEGG; hsa:26521; -.
DR MANE-Select; ENST00000504148.3; ENSP00000422122.2; NM_012459.4; NP_036591.3.
DR UCSC; uc058hho.1; human.
DR CTD; 26521; -.
DR DisGeNET; 26521; -.
DR GeneCards; TIMM8B; -.
DR HGNC; HGNC:11818; TIMM8B.
DR HPA; ENSG00000150779; Low tissue specificity.
DR MIM; 606659; gene.
DR neXtProt; NX_Q9Y5J9; -.
DR OpenTargets; ENSG00000150779; -.
DR PharmGKB; PA36524; -.
DR VEuPathDB; HostDB:ENSG00000150779; -.
DR eggNOG; KOG3489; Eukaryota.
DR GeneTree; ENSGT00940000155479; -.
DR HOGENOM; CLU_141397_1_2_1; -.
DR InParanoid; Q9Y5J9; -.
DR OMA; SKQKVQM; -.
DR OrthoDB; 1593287at2759; -.
DR PhylomeDB; Q9Y5J9; -.
DR PathwayCommons; Q9Y5J9; -.
DR Reactome; R-HSA-1268020; Mitochondrial protein import.
DR SignaLink; Q9Y5J9; -.
DR BioGRID-ORCS; 26521; 18 hits in 1082 CRISPR screens.
DR ChiTaRS; TIMM8B; human.
DR GenomeRNAi; 26521; -.
DR Pharos; Q9Y5J9; Tbio.
DR PRO; PR:Q9Y5J9; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9Y5J9; protein.
DR Bgee; ENSG00000150779; Expressed in tongue squamous epithelium and 208 other tissues.
DR ExpressionAtlas; Q9Y5J9; baseline and differential.
DR Genevisible; Q9Y5J9; HS.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IC:ComplexPortal.
DR GO; GO:0042719; C:mitochondrial intermembrane space protein transporter complex; TAS:BHF-UCL.
DR GO; GO:0140318; F:protein transporter activity; ISS:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; ISS:FlyBase.
DR GO; GO:0006626; P:protein targeting to mitochondrion; TAS:ProtInc.
DR GO; GO:0007605; P:sensory perception of sound; TAS:ProtInc.
DR Gene3D; 1.10.287.810; -; 1.
DR InterPro; IPR004217; Tim10-like.
DR InterPro; IPR035427; Tim10-like_dom_sf.
DR InterPro; IPR039238; Tim8/13.
DR PANTHER; PTHR19338; PTHR19338; 1.
DR Pfam; PF02953; zf-Tim10_DDP; 1.
DR SUPFAM; SSF144122; SSF144122; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Disulfide bond; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Protein transport;
KW Reference proteome; Translocation; Transport; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..83
FT /note="Mitochondrial import inner membrane translocase
FT subunit Tim8 B"
FT /id="PRO_0000193587"
FT MOTIF 36..59
FT /note="Twin CX3C motif"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT DISULFID 36..59
FT /evidence="ECO:0000250"
FT DISULFID 40..55
FT /evidence="ECO:0000250"
SQ SEQUENCE 83 AA; 9344 MW; 9DC47BB475DB8692 CRC64;
MAELGEADEA ELQRLVAAEQ QKAQFTAQVH HFMELCWDKC VEKPGNRLDS RTENCLSSCV
DRFIDTTLAI TSRFAQIVQK GGQ
