TIM8B_MOUSE
ID TIM8B_MOUSE Reviewed; 83 AA.
AC P62077; Q3TF77; Q9QUT4;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit Tim8 B;
DE AltName: Full=Deafness dystonia protein 2 homolog;
GN Name=Timm8b; Synonyms=Ddp2, Tim8b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, Heart, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- 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}.
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; AF196314; AAF13228.1; -; mRNA.
DR EMBL; AK003382; BAB22753.1; -; mRNA.
DR EMBL; AK004190; BAB23213.1; -; mRNA.
DR EMBL; AK012925; BAB28552.1; -; mRNA.
DR EMBL; AK169258; BAE41021.1; -; mRNA.
DR EMBL; AK018718; BAB31364.1; -; mRNA.
DR EMBL; AK019422; BAB31713.1; -; mRNA.
DR EMBL; BC029239; AAH29239.1; -; mRNA.
DR CCDS; CCDS40624.1; -.
DR RefSeq; NP_038925.1; NM_013897.2.
DR AlphaFoldDB; P62077; -.
DR SMR; P62077; -.
DR BioGRID; 205959; 7.
DR IntAct; P62077; 1.
DR STRING; 10090.ENSMUSP00000039335; -.
DR iPTMnet; P62077; -.
DR PhosphoSitePlus; P62077; -.
DR EPD; P62077; -.
DR jPOST; P62077; -.
DR MaxQB; P62077; -.
DR PaxDb; P62077; -.
DR PeptideAtlas; P62077; -.
DR PRIDE; P62077; -.
DR ProteomicsDB; 262822; -.
DR Antibodypedia; 32120; 88 antibodies from 14 providers.
DR DNASU; 30057; -.
DR Ensembl; ENSMUST00000044051; ENSMUSP00000039335; ENSMUSG00000039016.
DR GeneID; 30057; -.
DR KEGG; mmu:30057; -.
DR UCSC; uc009pjw.2; mouse.
DR CTD; 26521; -.
DR MGI; MGI:1353424; Timm8b.
DR VEuPathDB; HostDB:ENSMUSG00000039016; -.
DR eggNOG; KOG3489; Eukaryota.
DR GeneTree; ENSGT00940000155479; -.
DR HOGENOM; CLU_141397_1_2_1; -.
DR InParanoid; P62077; -.
DR OMA; SKQKVQM; -.
DR OrthoDB; 1593287at2759; -.
DR PhylomeDB; P62077; -.
DR TreeFam; TF106191; -.
DR BioGRID-ORCS; 30057; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Timm8b; mouse.
DR PRO; PR:P62077; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P62077; protein.
DR Bgee; ENSMUSG00000039016; Expressed in right kidney and 288 other tissues.
DR Genevisible; P62077; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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:0000250|UniProtKB:Q9Y5J9"
FT CHAIN 2..83
FT /note="Mitochondrial import inner membrane translocase
FT subunit Tim8 B"
FT /id="PRO_0000193588"
FT MOTIF 36..59
FT /note="Twin CX3C motif"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5J9"
FT DISULFID 36..59
FT /evidence="ECO:0000250"
FT DISULFID 40..55
FT /evidence="ECO:0000250"
SQ SEQUENCE 83 AA; 9286 MW; 04C47BA531CB689C CRC64;
MAELGEADEA ELQRLVAAEQ QKAQFTAQVH HFMELCWDKC VEKPGSRLDS RTENCLSSCV
DRFIDTTLAI TGRFAQIVQK GGQ
