TO203_ARATH
ID TO203_ARATH Reviewed; 202 AA.
AC P82874; Q8LBR8; Q9LSC8;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Mitochondrial import receptor subunit TOM20-3;
DE AltName: Full=Translocase of outer membrane 20 kDa subunit 3;
GN Name=TOM20-3; OrderedLocusNames=At3g27080; ORFNames=MOJ10.15;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 99-123.
RC STRAIN=cv. Columbia;
RX PubMed=11161051; DOI=10.1104/pp.125.2.943;
RA Werhahn W., Niemeyer A., Jaensch L., Kruft V., Schmitz U.K., Braun H.-P.;
RT "Purification and characterization of the preprotein translocase of the
RT outer mitochondrial membrane from Arabidopsis. Identification of multiple
RT forms of TOM20.";
RL Plant Physiol. 125:943-954(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 4-5, AND SUBUNIT.
RA Werhahn W., Jaensch L., Braun H.-P.;
RT "Identification of novel subunits of the TOM complex from Arabidopsis
RT thaliana.";
RL Plant Physiol. Biochem. 41:407-416(2003).
RN [7]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=14730085; DOI=10.1104/pp.103.033910;
RA Lister R., Chew O., Lee M.N., Heazlewood J.L., Clifton R., Parker K.L.,
RA Millar A.H., Whelan J.;
RT "A transcriptomic and proteomic characterization of the Arabidopsis
RT mitochondrial protein import apparatus and its response to mitochondrial
RT dysfunction.";
RL Plant Physiol. 134:777-789(2004).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBUNIT.
RX PubMed=17981999; DOI=10.1105/tpc.107.050534;
RA Lister R., Carrie C., Duncan O., Ho L.H., Howell K.A., Murcha M.W.,
RA Whelan J.;
RT "Functional definition of outer membrane proteins involved in preprotein
RT import into mitochondria.";
RL Plant Cell 19:3739-3759(2007).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [10]
RP STRUCTURE BY NMR OF 1-145.
RX PubMed=16461275; DOI=10.1016/j.cub.2005.12.034;
RA Perry A.J., Hulett J.M., Likic V.A., Lithgow T., Gooley P.R.;
RT "Convergent evolution of receptors for protein import into mitochondria.";
RL Curr. Biol. 16:221-229(2006).
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 translocation pore.
CC {ECO:0000269|PubMed:17981999}.
CC -!- SUBUNIT: Forms part of the preprotein translocase complex of the outer
CC mitochondrial membrane (TOM complex) which consists of at least 6
CC different proteins (TOM5, TOM6, TOM7, TOM20, TOM22/TOM9 and TOM40).
CC {ECO:0000269|PubMed:17981999, ECO:0000269|Ref.6}.
CC -!- INTERACTION:
CC P82874; Q94F58: NAC089; NbExp=2; IntAct=EBI-2352074, EBI-2319707;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000305};
CC Single-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, flowers, young cotyledons and
CC leaves. {ECO:0000269|PubMed:14730085}.
CC -!- PTM: The N-terminus is blocked.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Triple mutants tom20-2-
CC tom20-3-tom20-4 are vible but display a slightly delayed flowering
CC time. {ECO:0000269|PubMed:17981999}.
CC -!- MISCELLANEOUS: There are four genes (TOM20-1, TOM20-2, TOM20-3 and
CC TOM20-4) which encode mitochondrial import receptor subunits TOM20.
CC -!- MISCELLANEOUS: In mammals and fungi, the transmembrane domain is
CC located at the N-terminus while it is located at the C-terminus in
CC plants. The overall orientation of the protein in the membrane is
CC therefore inverted.
CC -!- SIMILARITY: Belongs to the Tom20 family. {ECO:0000305}.
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DR EMBL; AJ296025; CAC14430.1; -; mRNA.
DR EMBL; AB026649; BAB01089.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77264.1; -; Genomic_DNA.
DR EMBL; AY040027; AAK64184.1; -; mRNA.
DR EMBL; AY079411; AAL85142.1; -; mRNA.
DR EMBL; AY087037; AAM64598.1; -; mRNA.
DR RefSeq; NP_189344.1; NM_113622.4.
DR PDB; 1ZU2; NMR; -; A=1-145.
DR PDBsum; 1ZU2; -.
DR AlphaFoldDB; P82874; -.
DR BMRB; P82874; -.
DR SMR; P82874; -.
DR BioGRID; 7656; 16.
DR IntAct; P82874; 15.
DR STRING; 3702.AT3G27080.1; -.
DR iPTMnet; P82874; -.
DR SwissPalm; P82874; -.
DR PaxDb; P82874; -.
DR PRIDE; P82874; -.
DR ProteomicsDB; 234377; -.
DR EnsemblPlants; AT3G27080.1; AT3G27080.1; AT3G27080.
DR GeneID; 822326; -.
DR Gramene; AT3G27080.1; AT3G27080.1; AT3G27080.
DR KEGG; ath:AT3G27080; -.
DR Araport; AT3G27080; -.
DR TAIR; locus:2092045; AT3G27080.
DR eggNOG; ENOG502QT42; Eukaryota.
DR HOGENOM; CLU_117357_0_0_1; -.
DR InParanoid; P82874; -.
DR OMA; WCIGNAY; -.
DR OrthoDB; 1560087at2759; -.
DR PhylomeDB; P82874; -.
DR EvolutionaryTrace; P82874; -.
DR PRO; PR:P82874; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P82874; baseline and differential.
DR Genevisible; P82874; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:TAIR.
DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:TAIR.
DR GO; GO:0005742; C:mitochondrial outer membrane translocase complex; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; TAS:TAIR.
DR GO; GO:0015450; F:protein-transporting ATPase activity; IDA:TAIR.
DR GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; IEA:InterPro.
DR GO; GO:0006626; P:protein targeting to mitochondrion; IMP:TAIR.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR010547; TOM20_imprt_rcpt.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR32409; PTHR32409; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Protein transport;
KW Reference proteome; Repeat; TPR repeat; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..202
FT /note="Mitochondrial import receptor subunit TOM20-3"
FT /id="PRO_0000051545"
FT TOPO_DOM 1..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..202
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT REPEAT 38..74
FT /note="TPR 1"
FT REPEAT 86..119
FT /note="TPR 2"
FT REGION 146..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 12
FT /note="L -> F (in Ref. 5; AAM64598)"
FT /evidence="ECO:0000305"
FT HELIX 7..26
FT /evidence="ECO:0007829|PDB:1ZU2"
FT HELIX 31..47
FT /evidence="ECO:0007829|PDB:1ZU2"
FT HELIX 50..70
FT /evidence="ECO:0007829|PDB:1ZU2"
FT HELIX 75..91
FT /evidence="ECO:0007829|PDB:1ZU2"
FT HELIX 95..115
FT /evidence="ECO:0007829|PDB:1ZU2"
FT HELIX 120..130
FT /evidence="ECO:0007829|PDB:1ZU2"
FT HELIX 132..141
FT /evidence="ECO:0007829|PDB:1ZU2"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:1ZU2"
SQ SEQUENCE 202 AA; 22565 MW; F86A54F827F3A6D1 CRC64;
MDTETEFDRI LLFEQIRQDA ENTYKSNPLD ADNLTRWGGV LLELSQFHSI SDAKQMIQEA
ITKFEEALLI DPKKDEAVWC IGNAYTSFAF LTPDETEAKH NFDLATQFFQ QAVDEQPDNT
HYLKSLEMTA KAPQLHAEAY KQGLGSQPMG RVEAPAPPSS KAVKNKKSSD AKYDAMGWVI
LAIGVVAWIS FAKANVPVSP PR
