TO204_ARATH
ID TO204_ARATH Reviewed; 187 AA.
AC P82805; Q541X7;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=Mitochondrial import receptor subunit TOM20-4;
DE AltName: Full=Translocase of outer membrane 20 kDa subunit 4;
GN Name=TOM20-4; OrderedLocusNames=At5g40930; ORFNames=MMG1.2;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP PROTEIN SEQUENCE OF 102-117.
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 [6]
RP 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, AND INDUCTION.
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, SUBUNIT, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH MITOCHONDRIAL PRECURSOR PROTEINS.
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [10]
RP INTERACTION WITH AKR2A.
RC STRAIN=cv. C24, and cv. Columbia;
RX PubMed=20215589; DOI=10.1105/tpc.109.065979;
RA Shen G., Kuppu S., Venkataramani S., Wang J., Yan J., Qiu X., Zhang H.;
RT "ANKYRIN REPEAT-CONTAINING PROTEIN 2A is an essential molecular chaperone
RT for peroxisomal membrane-bound ASCORBATE PEROXIDASE3 in Arabidopsis.";
RL Plant Cell 22:811-831(2010).
RN [11]
RP AKR2A-BINDING SEQUENCE, AND REVIEW.
RX PubMed=21057222; DOI=10.4161/psb.5.11.13714;
RA Zhang H., Li X., Zhang Y., Kuppu S., Shen G.;
RT "Is AKR2A an essential molecular chaperone for a class of membrane-bound
RT proteins in plants?";
RL Plant Signal. Behav. 5:1520-1522(2010).
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 Interacts with a variety of mitochondrial precursor proteins. Interacts
CC with AKR2A (PubMed:20215589). {ECO:0000269|PubMed:17981999,
CC ECO:0000269|PubMed:20215589, ECO:0000269|Ref.6}.
CC -!- INTERACTION:
CC P82805; Q9LHE5: TOM40-1; NbExp=2; IntAct=EBI-2351908, EBI-2124038;
CC P82805; O80413: 103627788; Xeno; NbExp=2; IntAct=EBI-2351908, EBI-2362258;
CC P82805; Q07185: AOX1; Xeno; NbExp=2; IntAct=EBI-2351908, EBI-2123914;
CC P82805; Q7DM06; Xeno; NbExp=2; IntAct=EBI-2351908, EBI-2124012;
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 -!- INDUCTION: Up-regulated after antimycin A or rotenone treatments.
CC {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB023040; BAB10523.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94616.1; -; Genomic_DNA.
DR EMBL; AF462861; AAL58947.1; -; mRNA.
DR EMBL; AY141998; AAM98262.1; -; mRNA.
DR EMBL; AK117822; BAC42464.1; -; mRNA.
DR RefSeq; NP_198909.1; NM_123458.5.
DR AlphaFoldDB; P82805; -.
DR SMR; P82805; -.
DR BioGRID; 19345; 9.
DR IntAct; P82805; 8.
DR MINT; P82805; -.
DR STRING; 3702.AT5G40930.1; -.
DR iPTMnet; P82805; -.
DR PaxDb; P82805; -.
DR PRIDE; P82805; -.
DR ProteomicsDB; 232431; -.
DR EnsemblPlants; AT5G40930.1; AT5G40930.1; AT5G40930.
DR GeneID; 834094; -.
DR Gramene; AT5G40930.1; AT5G40930.1; AT5G40930.
DR KEGG; ath:AT5G40930; -.
DR Araport; AT5G40930; -.
DR TAIR; locus:2167737; AT5G40930.
DR eggNOG; ENOG502QT42; Eukaryota.
DR HOGENOM; CLU_117357_0_0_1; -.
DR InParanoid; P82805; -.
DR OMA; MNIEGSS; -.
DR OrthoDB; 1560087at2759; -.
DR PhylomeDB; P82805; -.
DR PRO; PR:P82805; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P82805; baseline and differential.
DR Genevisible; P82805; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005742; C:mitochondrial outer membrane translocase complex; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009536; C:plastid; 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; TAS: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 Acetylation; Direct protein sequencing; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Protein transport; Reference proteome;
KW TPR repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..187
FT /note="Mitochondrial import receptor subunit TOM20-4"
FT /id="PRO_0000051546"
FT TOPO_DOM 1..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..187
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT REPEAT 84..117
FT /note="TPR"
FT MOTIF 179..187
FT /note="AKR2A-binding sequence (ABS) required for
FT mitochondrion outer membrane targeting"
FT /evidence="ECO:0000269|PubMed:21057222"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P82874"
SQ SEQUENCE 187 AA; 20973 MW; 156DF3D231EA286C CRC64;
MDMQNENERL MVFEHARKVA EATYVKNPLD AENLTRWAGA LLELSQFQTE PKQMILEAIL
KLGEALVIDP KKHDALWLIG NAHLSFGFLS SDQTEASDNF EKASQFFQLA VEEQPESELY
RKSLTLASKA PELHTGGTAG PSSNSAKTMK QKKTSEFKYD VFGWVILASY VVAWISFANS
QTPVSRQ
