TOM34_RAT
ID TOM34_RAT Reviewed; 309 AA.
AC Q3KRD5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Mitochondrial import receptor subunit TOM34;
DE AltName: Full=Translocase of outer membrane 34 kDa subunit;
GN Name=Tomm34;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-186, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- SIMILARITY: Belongs to the Tom34 family. {ECO:0000305}.
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DR EMBL; BC105768; AAI05769.1; -; mRNA.
DR RefSeq; NP_001037709.1; NM_001044244.2.
DR AlphaFoldDB; Q3KRD5; -.
DR SMR; Q3KRD5; -.
DR STRING; 10116.ENSRNOP00000049550; -.
DR iPTMnet; Q3KRD5; -.
DR PhosphoSitePlus; Q3KRD5; -.
DR jPOST; Q3KRD5; -.
DR PaxDb; Q3KRD5; -.
DR PRIDE; Q3KRD5; -.
DR GeneID; 311621; -.
DR KEGG; rno:311621; -.
DR CTD; 10953; -.
DR RGD; 1309029; Tomm34.
DR VEuPathDB; HostDB:ENSRNOG00000029799; -.
DR eggNOG; KOG1124; Eukaryota.
DR HOGENOM; CLU_061396_0_0_1; -.
DR InParanoid; Q3KRD5; -.
DR OMA; KRWECLP; -.
DR OrthoDB; 1428825at2759; -.
DR PhylomeDB; Q3KRD5; -.
DR TreeFam; TF106202; -.
DR PRO; PR:Q3KRD5; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000029799; Expressed in frontal cortex and 20 other tissues.
DR Genevisible; Q3KRD5; RN.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0031072; F:heat shock protein binding; ISO:RGD.
DR GO; GO:0006626; P:protein targeting to mitochondrion; ISO:RGD.
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 Chaperone; Cytoplasm; Isopeptide bond; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Phosphoprotein; Reference proteome; Repeat;
KW TPR repeat; Ubl conjugation.
FT CHAIN 1..309
FT /note="Mitochondrial import receptor subunit TOM34"
FT /id="PRO_0000329295"
FT REPEAT 9..42
FT /note="TPR 1"
FT REPEAT 51..84
FT /note="TPR 2"
FT REPEAT 86..118
FT /note="TPR 3"
FT REPEAT 193..226
FT /note="TPR 4"
FT REPEAT 227..260
FT /note="TPR 5"
FT REPEAT 262..294
FT /note="TPR 6"
FT REGION 158..187
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:22673903"
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:16641100,
FT ECO:0007744|PubMed:22673903"
FT CROSSLNK 197
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15785"
SQ SEQUENCE 309 AA; 34461 MW; 66793000104468CE CRC64;
MAPKVSDSVE QLRAAGNQNF RNGQYGEASA LYERALRLLQ ARGSADPEEE SVLYSNRAAC
YLKDGNCTDC IKDCTSALAL VPFSIKPLLR RASAYEALEK YSLAYVDYKT VLQIDNSVAS
ALEGINRITR ALMDSLGPEW RLKLPPIPVV PVSAQKRWSS LPSENHKETA KSKSKETTAT
KNRVPSAGDV ERARVLKEEG NELVKKGNHK KAIEKYSESL LFSSLESATY SNRALCHLVL
KQYKEAEKDC TEALKLDGKN VKAFYRRAQA YKALKDYKSS LADISSLLQI EPRNGPAHKL
RQEVNQNMN
