TIM8A_MOUSE
ID TIM8A_MOUSE Reviewed; 97 AA.
AC Q9WVA2; Q542E5;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit Tim8 A;
DE AltName: Full=Deafness dystonia protein 1 homolog;
GN Name=Timm8a1; Synonyms=Ddp1, Tim8a, Timm8a;
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 [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Adipocyte;
RX PubMed=10873677; DOI=10.1006/bbrc.2000.3004;
RA Nakane T., Inada Y., Ito F., Itoh N., Tazawa S., Chiba S.;
RT "Cloning and expression of mouse deafness dystonia peptide 1 cDNA.";
RL Biochem. Biophys. Res. Commun. 273:759-764(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Submandibular gland;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Mammary gland, and Thymus;
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 TISSUE SPECIFICITY.
RX PubMed=15254020; DOI=10.1093/hmg/ddh217;
RA Roesch K., Hynds P.J., Varga R., Tranebjaerg L., Koehler C.M.;
RT "The calcium-binding aspartate/glutamate carriers, citrin and aralar1, are
RT new substrates for the DDP1/TIMM8a-TIMM13 complex.";
RL Hum. Mol. Genet. 13:2101-2111(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87 AND SER-96, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; SER-94 AND SER-96, AND
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: Mitochondrial intermembrane chaperone that participates in
CC the import and insertion of some multi-pass transmembrane proteins into
CC the mitochondrial inner membrane. Also 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. The TIMM8-
CC TIMM13 complex mediates the import of proteins such as TIMM23,
CC SLC25A12/ARALAR1 and SLC25A13/ARALAR2, while the predominant TIMM9-
CC TIMM10 70 kDa complex mediates the import of much more proteins (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterohexamer; composed of 3 copies of TIMM8A and 3 copies of
CC TIMM13, named soluble 70 kDa complex. Associates with the TIM22
CC 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: Present at high level in liver and brain, and at
CC lower level in muscle and heart. In CNS sections, it is predominantly
CC present in the soma and the dendritic portion of the Purkinje cells of
CC the cerebellum, but not in the glial cells. Scattered expression also
CC is also detected in the brain stem, olfactory bulb, substantia nigra,
CC hippocampus and striatum (at protein level). Ubiquitously expressed.
CC {ECO:0000269|PubMed:10873677, ECO:0000269|PubMed:15254020}.
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 TIMM8A 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; AF150081; AAD39988.1; -; mRNA.
DR EMBL; AB031055; BAA90770.1; -; mRNA.
DR EMBL; AK011402; BAB27594.1; -; mRNA.
DR EMBL; AK088903; BAC40644.1; -; mRNA.
DR EMBL; AK090079; BAC41082.1; -; mRNA.
DR EMBL; AK165573; BAE38265.1; -; mRNA.
DR EMBL; BC004796; AAH04796.1; -; mRNA.
DR EMBL; BC094631; AAH94631.1; -; mRNA.
DR CCDS; CCDS41122.1; -.
DR PIR; JC7322; JC7322.
DR RefSeq; NP_038926.1; NM_013898.3.
DR AlphaFoldDB; Q9WVA2; -.
DR SMR; Q9WVA2; -.
DR BioGRID; 205960; 4.
DR IntAct; Q9WVA2; 1.
DR STRING; 10090.ENSMUSP00000049749; -.
DR iPTMnet; Q9WVA2; -.
DR PhosphoSitePlus; Q9WVA2; -.
DR EPD; Q9WVA2; -.
DR jPOST; Q9WVA2; -.
DR MaxQB; Q9WVA2; -.
DR PaxDb; Q9WVA2; -.
DR PeptideAtlas; Q9WVA2; -.
DR PRIDE; Q9WVA2; -.
DR ProteomicsDB; 262787; -.
DR Ensembl; ENSMUST00000054213; ENSMUSP00000050156; ENSMUSG00000048007.
DR GeneID; 30058; -.
DR KEGG; mmu:30058; -.
DR UCSC; uc009ugd.1; mouse.
DR CTD; 30058; -.
DR MGI; MGI:1353433; Timm8a1.
DR VEuPathDB; HostDB:ENSMUSG00000048007; -.
DR eggNOG; KOG3489; Eukaryota.
DR GeneTree; ENSGT00940000154661; -.
DR HOGENOM; CLU_141397_1_2_1; -.
DR InParanoid; Q9WVA2; -.
DR OMA; QATQVCL; -.
DR OrthoDB; 1593287at2759; -.
DR PhylomeDB; Q9WVA2; -.
DR TreeFam; TF106191; -.
DR BioGRID-ORCS; 30058; 10 hits in 50 CRISPR screens.
DR PRO; PR:Q9WVA2; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9WVA2; protein.
DR Bgee; ENSMUSG00000048007; Expressed in morula and 102 other tissues.
DR Genevisible; Q9WVA2; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:MGI.
DR GO; GO:0042719; C:mitochondrial intermembrane space protein transporter complex; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0006626; P:protein targeting to mitochondrion; ISO:MGI.
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 Chaperone; Disulfide bond; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Translocation; Transport; Zinc.
FT CHAIN 1..97
FT /note="Mitochondrial import inner membrane translocase
FT subunit Tim8 A"
FT /id="PRO_0000193585"
FT MOTIF 43..66
FT /note="Twin CX3C motif"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT DISULFID 43..66
FT /evidence="ECO:0000250"
FT DISULFID 47..62
FT /evidence="ECO:0000250"
SQ SEQUENCE 97 AA; 11042 MW; 16C23D7C351BDF00 CRC64;
MESSTSSSGS ALGAVDPQLQ HFIEVETQKQ RFQQLVHQMT ELCWEKCMDK PGPKLDSRAE
ACFVNCVERF IDTSQFILNR LEQTQKSKPV FSESLSD
