ID   TOM34_PONAB             Reviewed;         309 AA.
AC   A4K2V0; Q5RAI1;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Mitochondrial import receptor subunit TOM34;
DE   AltName: Full=Translocase of outer membrane 34 kDa subunit;
GN   Name=TOMM34;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=17267810; DOI=10.1101/gr.6004607;
RG   NISC comparative sequencing program;
RA   Hurle B., Swanson W., Green E.D.;
RT   "Comparative sequence analyses reveal rapid and divergent evolutionary
RT   changes of the WFDC locus in the primate lineage.";
RL   Genome Res. 17:276-286(2007).
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; CR859034; CAH91229.1; -; mRNA.
DR   EMBL; DP000045; ABO52985.1; -; Genomic_DNA.
DR   RefSeq; NP_001125725.1; NM_001132253.1.
DR   AlphaFoldDB; A4K2V0; -.
DR   SMR; A4K2V0; -.
DR   STRING; 9601.ENSPPYP00000012334; -.
DR   Ensembl; ENSPPYT00000012816; ENSPPYP00000012334; ENSPPYG00000011044.
DR   GeneID; 100172650; -.
DR   CTD; 10953; -.
DR   eggNOG; KOG1124; Eukaryota.
DR   GeneTree; ENSGT00940000161058; -.
DR   HOGENOM; CLU_061396_0_0_1; -.
DR   InParanoid; A4K2V0; -.
DR   OMA; KRWECLP; -.
DR   OrthoDB; 1428825at2759; -.
DR   TreeFam; TF106202; -.
DR   Proteomes; UP000001595; Chromosome 20.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:Ensembl.
DR   GO; GO:0006626; P:protein targeting to mitochondrion; IEA:Ensembl.
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   SMART; SM00028; TPR; 6.
DR   SUPFAM; SSF48452; SSF48452; 2.
DR   PROSITE; PS50005; TPR; 5.
DR   PROSITE; PS50293; TPR_REGION; 2.
PE   2: Evidence at transcript 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_0000329293"
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          161..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         160
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15785"
FT   MOD_RES         186
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15785"
FT   CROSSLNK        197
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q15785"
FT   CONFLICT        8
FT                   /note="C -> S (in Ref. 1; CAH91229)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        117
FT                   /note="S -> N (in Ref. 1; CAH91229)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        122
FT                   /note="L -> V (in Ref. 1; CAH91229)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        126
FT                   /note="N -> S (in Ref. 1; CAH91229)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        194
FT                   /note="K -> R (in Ref. 1; CAH91229)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        242
FT                   /note="Q -> P (in Ref. 1; CAH91229)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   309 AA;  34534 MW;  6ABBEA174DB33BFF CRC64;
     MAPKFPDCVE ELRAAGNESF RNGQYAEASA LYGRALRVLQ AQGSSDPEEE SVLYSNRAAC
     HLKDGNCRDC IKDCTSALAL VPFSIKPLLR RASAYEALEK YPMAYVDYKT VLQIDDSVTS
     ALEGINRMTR ALMDSLGPEW RLKLPSIPLV PVSAQKRWNS LPSENHKEMA KSKSKETTAT
     KNRVPSAGDV EKAKVLKEEG NELVKKGNHK KAIEKYSESL LCSNLESATY SNRALCYLVL
     KQYTEAVKDC TEALKLDGKN VKAFYRRAQA HKALKDYKSS FADISNLLQI EPRNGPAQKL
     RQEVKQNLH