ID   TOM20_RAT               Reviewed;         145 AA.
AC   Q62760; O08517; Q63804; Q6AZ66;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   27-MAR-2024, entry version 173.
DE   RecName: Full=Mitochondrial import receptor subunit TOM20 homolog;
DE   AltName: Full=Mitochondrial 20 kDa outer membrane protein;
DE   AltName: Full=Outer mitochondrial membrane receptor Tom20;
GN   Name=Tomm20;
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 [MRNA].
RA   Nuttall S.D., Sinding J., Hanson B., Hoogenraad N.J.;
RL   Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Mihara K., Nomura N., Matsuo H., Sakaguchi M.;
RT   "cDNA cloning and characterization of rat mitochondrial precursor
RT   receptor.";
RL   Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   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   FUNCTION.
RX   PubMed=19401463; DOI=10.1074/jbc.m109.007492;
RA   Anandatheerthavarada H.K., Sepuri N.B., Avadhani N.G.;
RT   "Mitochondrial targeting of cytochrome P450 proteins containing NH2-
RT   terminal chimeric signals involves an unusual TOM20/TOM22 bypass
RT   mechanism.";
RL   J. Biol. Chem. 284:17352-17363(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 AND SER-138, 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).
RN   [6]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=29934347; DOI=10.1523/jneurosci.0699-18.2018;
RA   Lizama B.N., Palubinsky A.M., Raveendran V.A., Moore A.M., Federspiel J.D.,
RA   Codreanu S.G., Liebler D.C., McLaughlin B.;
RT   "Neuronal Preconditioning Requires the Mitophagic Activity of C-terminus of
RT   HSC70-Interacting Protein.";
RL   J. Neurosci. 38:6825-6840(2018).
RN   [7]
RP   STRUCTURE BY NMR OF 51-145.
RX   PubMed=10721992; DOI=10.1016/s0092-8674(00)80691-1;
RA   Abe Y., Shodai T., Muto T., Mihara K., Torii H., Nishikawa S., Endo T.,
RA   Kohda D.;
RT   "Structural basis of presequence recognition by the mitochondrial protein
RT   import receptor Tom20.";
RL   Cell 100:551-560(2000).
CC   -!- FUNCTION: Central component of the receptor complex responsible for the
CC       recognition and translocation of cytosolically synthesized
CC       mitochondrial preproteins. Together with TOM22 functions as the transit
CC       peptide receptor at the surface of the mitochondrion outer membrane and
CC       facilitates the movement of preproteins into the TOM40 translocation
CC       pore (By similarity). Required for the translocation across the
CC       mitochondrial outer membrane of cytochrome P450 monooxygenases.
CC       {ECO:0000250, ECO:0000269|PubMed:19401463}.
CC   -!- SUBUNIT: Forms part of the preprotein translocase complex of the outer
CC       mitochondrial membrane (TOM complex) which consists of at least 7
CC       different proteins (TOMM5, TOMM6, TOMM7, TOMM20, TOMM22, TOMM40 and
CC       TOMM70). Interacts with TOM22. Interacts with APEX1 (By similarity).
CC       Interacts with TBC1D21 (By similarity). {ECO:0000250|UniProtKB:Q15388,
CC       ECO:0000250|UniProtKB:Q9DCC8}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:Q15388}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in neurons at 18.5 dpc (at protein
CC       level). {ECO:0000269|PubMed:29934347}.
CC   -!- PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation
CC       and enhancement of mitophagy. Deubiquitinated by USP30.
CC       {ECO:0000250|UniProtKB:Q15388}.
CC   -!- SIMILARITY: Belongs to the Tom20 family. {ECO:0000305}.
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DR   EMBL; U21871; AAB01506.1; -; mRNA.
DR   EMBL; D63411; BAA09714.1; -; mRNA.
DR   EMBL; BC078715; AAH78715.1; -; mRNA.
DR   RefSeq; NP_690918.1; NM_152935.1.
DR   PDB; 1OM2; NMR; -; A=51-145.
DR   PDB; 2V1S; X-ray; 2.05 A; A/B/C/D/E/F/G=59-126.
DR   PDB; 2V1T; X-ray; 1.92 A; A/B=59-126.
DR   PDB; 3AWR; X-ray; 2.00 A; A/B=59-126.
DR   PDB; 3AX2; X-ray; 1.90 A; A/C/E/G=59-126.
DR   PDB; 3AX3; X-ray; 2.10 A; A/C/E/G=59-126.
DR   PDB; 3AX5; X-ray; 2.20 A; A/C=59-126.
DR   PDB; 5AZ6; X-ray; 2.56 A; A/B=65-126.
DR   PDB; 5AZ7; X-ray; 1.96 A; A=65-126.
DR   PDB; 5AZ8; X-ray; 1.70 A; A=65-126.
DR   PDB; 5AZ9; X-ray; 1.82 A; A=65-126.
DR   PDBsum; 1OM2; -.
DR   PDBsum; 2V1S; -.
DR   PDBsum; 2V1T; -.
DR   PDBsum; 3AWR; -.
DR   PDBsum; 3AX2; -.
DR   PDBsum; 3AX3; -.
DR   PDBsum; 3AX5; -.
DR   PDBsum; 5AZ6; -.
DR   PDBsum; 5AZ7; -.
DR   PDBsum; 5AZ8; -.
DR   PDBsum; 5AZ9; -.
DR   AlphaFoldDB; Q62760; -.
DR   BMRB; Q62760; -.
DR   SMR; Q62760; -.
DR   BioGRID; 251753; 4.
DR   CORUM; Q62760; -.
DR   STRING; 10116.ENSRNOP00000027088; -.
DR   GlyGen; Q62760; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q62760; -.
DR   PhosphoSitePlus; Q62760; -.
DR   PaxDb; 10116-ENSRNOP00000027088; -.
DR   Ensembl; ENSRNOT00000027088.3; ENSRNOP00000027088.2; ENSRNOG00000019980.3.
DR   Ensembl; ENSRNOT00055008742; ENSRNOP00055006641; ENSRNOG00055005434.
DR   Ensembl; ENSRNOT00060008567; ENSRNOP00060006424; ENSRNOG00060005145.
DR   Ensembl; ENSRNOT00065032496; ENSRNOP00065025937; ENSRNOG00065019302.
DR   GeneID; 266601; -.
DR   KEGG; rno:266601; -.
DR   UCSC; RGD:708467; rat.
DR   AGR; RGD:708467; -.
DR   CTD; 9804; -.
DR   RGD; 708467; Tomm20.
DR   eggNOG; KOG4056; Eukaryota.
DR   GeneTree; ENSGT00390000011698; -.
DR   HOGENOM; CLU_100000_0_0_1; -.
DR   InParanoid; Q62760; -.
DR   OMA; PPPIFQI; -.
DR   OrthoDB; 1333327at2759; -.
DR   PhylomeDB; Q62760; -.
DR   TreeFam; TF106200; -.
DR   Reactome; R-RNO-5205685; PINK1-PRKN Mediated Mitophagy.
DR   Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR   EvolutionaryTrace; Q62760; -.
DR   PRO; PR:Q62760; -.
DR   Proteomes; UP000002494; Chromosome 19.
DR   Bgee; ENSRNOG00000019980; Expressed in ovary and 20 other cell types or tissues.
DR   GO; GO:0071944; C:cell periphery; ISO:RGD.
DR   GO; GO:0140494; C:migrasome; ISO:RGD.
DR   GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; ISO:RGD.
DR   GO; GO:0005740; C:mitochondrial envelope; ISO:RGD.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR   GO; GO:0005742; C:mitochondrial outer membrane translocase complex; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR   GO; GO:0097225; C:sperm midpiece; ISS:UniProtKB.
DR   GO; GO:0030943; F:mitochondrion targeting sequence binding; IDA:RGD.
DR   GO; GO:0015450; F:protein-transporting ATPase activity; ISO:RGD.
DR   GO; GO:0051082; F:unfolded protein binding; ISO:RGD.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0006626; P:protein targeting to mitochondrion; IMP:UniProtKB.
DR   GO; GO:1905242; P:response to 3,3',5-triiodo-L-thyronine; IEP:RGD.
DR   GO; GO:0014850; P:response to muscle activity; IEP:RGD.
DR   GO; GO:0016031; P:tRNA import into mitochondrion; IBA:GO_Central.
DR   Gene3D; 1.20.960.10; Mitochondrial outer membrane translocase complex, subunit Tom20 domain; 1.
DR   InterPro; IPR002056; MAS20.
DR   InterPro; IPR022422; MAS20_rcpt_metazoan.
DR   InterPro; IPR023392; Tom20_dom_sf.
DR   NCBIfam; TIGR00985; 3a0801s04tom; 1.
DR   PANTHER; PTHR12430; MITOCHONDRIAL IMPORT RECEPTOR SUBUNIT TOM20; 1.
DR   PANTHER; PTHR12430:SF2; MITOCHONDRIAL IMPORT RECEPTOR SUBUNIT TOM20 HOMOLOG; 1.
DR   Pfam; PF02064; MAS20; 1.
DR   PIRSF; PIRSF037707; MAS20_rcpt; 1.
DR   PRINTS; PR01989; EUOM20RECPTR.
DR   PRINTS; PR00351; OM20RECEPTOR.
DR   SUPFAM; SSF47157; Mitochondrial import receptor subunit Tom20; 1.
DR   Genevisible; Q62760; RN.
PE   1: Evidence at protein level;
KW   3D-structure; Isopeptide bond; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Phosphoprotein; Protein transport;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW   Ubl conjugation.
FT   CHAIN           1..145
FT                   /note="Mitochondrial import receptor subunit TOM20 homolog"
FT                   /id="PRO_0000051541"
FT   TOPO_DOM        1..6
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        25..145
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         135
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         138
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   CROSSLNK        35
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q15388"
FT   CROSSLNK        56
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q15388"
FT   CROSSLNK        61
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q15388"
FT   CROSSLNK        68
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q15388"
FT   CONFLICT        12
FT                   /note="V -> L (in Ref. 1; AAB01506)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        30
FT                   /note="S -> G (in Ref. 1; AAB01506)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        36
FT                   /note="N -> D (in Ref. 2; BAA09714)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        140
FT                   /note="A -> G (in Ref. 2; BAA09714)"
FT                   /evidence="ECO:0000305"
FT   STRAND          56..58
FT                   /evidence="ECO:0007829|PDB:1OM2"
FT   STRAND          60..62
FT                   /evidence="ECO:0007829|PDB:1OM2"
FT   HELIX           65..82
FT                   /evidence="ECO:0007829|PDB:5AZ8"
FT   HELIX           86..98
FT                   /evidence="ECO:0007829|PDB:5AZ8"
FT   HELIX           104..113
FT                   /evidence="ECO:0007829|PDB:5AZ8"
FT   HELIX           116..123
FT                   /evidence="ECO:0007829|PDB:5AZ8"
FT   HELIX           129..134
FT                   /evidence="ECO:0007829|PDB:1OM2"
FT   TURN            135..140
FT                   /evidence="ECO:0007829|PDB:1OM2"
SQ   SEQUENCE   145 AA;  16284 MW;  50E3BD25AD5C9B3B CRC64;
     MVGRNSAIAA GVCGALFIGY CIYFDRKRRS DPNFKNRLRE RRKKQKLAKE RAGLSKLPDL
     KDAEAVQKFF LEEIQLGEEL LAQGDYEKGV DHLTNAIAVC GQPQQLLQVL QQTLPPPVFQ
     MLLTKLPTIS QRIVSAQSLA EDDVE
//