TOM34_MOUSE
ID TOM34_MOUSE Reviewed; 309 AA.
AC Q9CYG7; A2A5N5; A2A5N6; Q3THD0; Q812F1; Q812F2; Q9D059;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Mitochondrial import receptor subunit TOM34;
DE AltName: Full=Translocase of outer membrane 34 kDa subunit;
GN Name=Tomm34;
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 [GENOMIC DNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=C57BL/6J;
RX PubMed=12801914; DOI=10.1093/jb/mvg080;
RA Terada K., Ueno S., Yomogida K., Imai T., Kiyonari H., Takeda N., Yano M.,
RA Abe S., Aizawa S., Mori M.;
RT "Expression of Tom34 splicing isoforms in mouse testis and knockout of
RT Tom34 in mice.";
RL J. Biochem. 133:625-631(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Embryo, and Tongue;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-186,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, 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: Plays a role in the import of cytosolically synthesized
CC preproteins into mitochondria. Binds the mature portion of precursor
CC proteins. Interacts with cellular components, and possesses weak ATPase
CC activity. May be a chaperone-like protein that helps to keep newly
CC synthesized precursors in an unfolded import compatible state (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with HSP90A, VCP, ATP6V1D, KIAA0665, AMPK, and DMAP1
CC through its TPR repeat. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion outer
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Isoforms 1 and 2 are produced by 2 alternative initial coding
CC exons with very similar sequences which differ at only 4 positions.;
CC Name=1; Synonyms=Tomm34a;
CC IsoId=Q9CYG7-1; Sequence=Displayed;
CC Name=2; Synonyms=Tomm34b;
CC IsoId=Q9CYG7-2; Sequence=VSP_035044;
CC -!- TISSUE SPECIFICITY: Isoform 1 is ubiquitously expressed while isoform 2
CC is expressed only in mature testicular germ cells. Isoform 1 is
CC expressed in all testicular cells. Isoform 2 is highly expressed in
CC early to late pachytene cells but expression is significantly decreased
CC in round spermatid cells. {ECO:0000269|PubMed:12801914}.
CC -!- DEVELOPMENTAL STAGE: Isoform 2 is hardly detectable in testis at 1 week
CC post partum but expression gradually increases for 2 to 4 weeks post
CC partum. Isoform 1 is detected during this period but its expression
CC does not change. {ECO:0000269|PubMed:12801914}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable, grow normally and both males and
CC females are fertile. There is no effect on spermatogenesis or protein
CC import into mitochondria. {ECO:0000269|PubMed:12801914}.
CC -!- SIMILARITY: Belongs to the Tom34 family. {ECO:0000305}.
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DR EMBL; AB087254; BAC57494.1; -; Genomic_DNA.
DR EMBL; AB087254; BAC57495.1; -; Genomic_DNA.
DR EMBL; AK011786; BAB27840.1; -; mRNA.
DR EMBL; AK017699; BAB30882.1; -; mRNA.
DR EMBL; AK075873; BAC36020.1; -; mRNA.
DR EMBL; AK168329; BAE40267.1; -; mRNA.
DR EMBL; AL591542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018278; AAH18278.1; -; mRNA.
DR CCDS; CCDS17020.1; -. [Q9CYG7-2]
DR CCDS; CCDS71187.1; -. [Q9CYG7-1]
DR RefSeq; NP_001278084.1; NM_001291155.1. [Q9CYG7-1]
DR RefSeq; NP_080272.1; NM_025996.5. [Q9CYG7-2]
DR RefSeq; XP_006500130.1; XM_006500067.1. [Q9CYG7-2]
DR AlphaFoldDB; Q9CYG7; -.
DR SMR; Q9CYG7; -.
DR BioGRID; 211975; 9.
DR IntAct; Q9CYG7; 1.
DR STRING; 10090.ENSMUSP00000018466; -.
DR iPTMnet; Q9CYG7; -.
DR PhosphoSitePlus; Q9CYG7; -.
DR EPD; Q9CYG7; -.
DR jPOST; Q9CYG7; -.
DR MaxQB; Q9CYG7; -.
DR PaxDb; Q9CYG7; -.
DR PeptideAtlas; Q9CYG7; -.
DR PRIDE; Q9CYG7; -.
DR ProteomicsDB; 260649; -. [Q9CYG7-1]
DR ProteomicsDB; 260650; -. [Q9CYG7-2]
DR Antibodypedia; 12625; 327 antibodies from 26 providers.
DR DNASU; 67145; -.
DR Ensembl; ENSMUST00000018466; ENSMUSP00000018466; ENSMUSG00000018322. [Q9CYG7-2]
DR Ensembl; ENSMUST00000109384; ENSMUSP00000105010; ENSMUSG00000018322. [Q9CYG7-1]
DR GeneID; 67145; -.
DR KEGG; mmu:67145; -.
DR UCSC; uc008ntr.2; mouse. [Q9CYG7-2]
DR UCSC; uc008nts.2; mouse. [Q9CYG7-1]
DR CTD; 10953; -.
DR MGI; MGI:1914395; Tomm34.
DR VEuPathDB; HostDB:ENSMUSG00000018322; -.
DR eggNOG; KOG1124; Eukaryota.
DR GeneTree; ENSGT00940000161058; -.
DR HOGENOM; CLU_061396_0_0_1; -.
DR InParanoid; Q9CYG7; -.
DR OMA; KRWECLP; -.
DR OrthoDB; 1428825at2759; -.
DR PhylomeDB; Q9CYG7; -.
DR TreeFam; TF106202; -.
DR BioGRID-ORCS; 67145; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Tomm34; mouse.
DR PRO; PR:Q9CYG7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9CYG7; protein.
DR Bgee; ENSMUSG00000018322; Expressed in floor plate of midbrain and 258 other tissues.
DR Genevisible; Q9CYG7; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0006626; P:protein targeting to mitochondrion; ISO:MGI.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Chaperone; Cytoplasm; Isopeptide bond; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat; Ubl conjugation.
FT CHAIN 1..309
FT /note="Mitochondrial import receptor subunit TOM34"
FT /id="PRO_0000106335"
FT REPEAT 9..42
FT /note="TPR 1"
FT REPEAT 51..84
FT /note="TPR 2"
FT REPEAT 85..118
FT /note="TPR 3"
FT REPEAT 193..226
FT /note="TPR 4"
FT REPEAT 227..260
FT /note="TPR 5"
FT REPEAT 261..294
FT /note="TPR 6"
FT REGION 158..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15785"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 197
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15785"
FT VAR_SEQ 1..26
FT /note="MAPKVSDSVEQLRAAGNQNFRNGQYG -> MAPKLSDSVEELRAAGNQSFRN
FT GQYA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035044"
FT CONFLICT 59
FT /note="A -> S (in Ref. 1; BAC57494/BAC57495)"
FT /evidence="ECO:0000305"
FT MOD_RES Q9CYG7-2:8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 309 AA; 34278 MW; 4367551F4063278A CRC64;
MAPKVSDSVE QLRAAGNQNF RNGQYGEASA LYERALRLLQ ARGSADPEEE SVLYSNRAAC
YLKDGNCTDC IKDCTSALAL VPFSIKPLLR RASAYEALEK YALAYVDYKT VLQIDNSVAS
ALEGINRITR ALMDSLGPEW RLKLPPIPVV PVSAQKRWNS LPSDNHKETA KTKSKEATAT
KSRVPSAGDV ERAKALKEEG NDLVKKGNHK KAIEKYSESL LCSSLESATY SNRALCHLVL
KQYKEAVKDC TEALKLDGKN VKAFYRRAQA YKALKDYKSS LSDISSLLQI EPRNGPAQKL
RQEVNQNMN
