TOM20_RAT
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 03-AUG-2022, entry version 165.
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 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 -!- 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 iPTMnet; Q62760; -.
DR PhosphoSitePlus; Q62760; -.
DR PaxDb; Q62760; -.
DR PRIDE; Q62760; -.
DR Ensembl; ENSRNOT00000027088; ENSRNOP00000027088; ENSRNOG00000019980.
DR GeneID; 266601; -.
DR KEGG; rno:266601; -.
DR UCSC; RGD:708467; rat.
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; VGYCFYF; -.
DR OrthoDB; 1316067at2759; -.
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 tissues.
DR Genevisible; Q62760; RN.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IBA:GO_Central.
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; IDA: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: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; -; 1.
DR InterPro; IPR002056; MAS20.
DR InterPro; IPR022422; MAS20_rcpt_metazoan.
DR InterPro; IPR023392; Tom20_dom_sf.
DR PANTHER; PTHR12430; PTHR12430; 1.
DR Pfam; PF02064; MAS20; 1.
DR PIRSF; PIRSF037707; MAS20_rcpt; 1.
DR PRINTS; PR01989; EUOM20RECPTR.
DR PRINTS; PR00351; OM20RECEPTOR.
DR SUPFAM; SSF47157; SSF47157; 1.
DR TIGRFAMs; TIGR00985; 3a0801s04tom; 1.
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
