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Database: UniProt
Entry: P82805
LinkDB: P82805
Original site: P82805 
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   27-MAR-2024, entry version 154.
DE   RecName: Full=Mitochondrial import receptor subunit TOM20-4 {ECO:0000303|PubMed:11161051};
DE   AltName: Full=Translocase of outer membrane 20 kDa subunit 4 {ECO:0000303|PubMed:11161051};
GN   Name=TOM20-4 {ECO:0000303|PubMed:11161051};
GN   OrderedLocusNames=At5g40930 {ECO:0000312|Araport:AT5G40930};
GN   ORFNames=MMG1.2 {ECO:0000312|EMBL:BAB10523.1};
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       (PubMed:17981999, Ref.6). Interacts with a variety of mitochondrial
CC       precursor proteins. Interacts with AKR2A (PubMed:20215589). Component
CC       of a mitochondrial large protein complex that contains, at least,
CC       MIC60, DGS1, TOM40, TOM20 proteins, and petC/RISP (By similarity).
CC       {ECO:0000250|UniProtKB:P82873, 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}.
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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.P82805; -.
DR   iPTMnet; P82805; -.
DR   PaxDb; 3702-AT5G40930-1; -.
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; AT5G40930; TOM20-4.
DR   eggNOG; ENOG502QT42; Eukaryota.
DR   HOGENOM; CLU_117357_0_0_1; -.
DR   InParanoid; P82805; -.
DR   OMA; LEMTDKA; -.
DR   OrthoDB; 443432at2759; -.
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: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; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR010547; TOM20_imprt_rcpt.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR32409; MITOCHONDRIAL IMPORT RECEPTOR SUBUNIT TOM20-1-RELATED; 1.
DR   PANTHER; PTHR32409:SF3; MITOCHONDRIAL IMPORT RECEPTOR SUBUNIT TOM20-1-RELATED; 1.
DR   Pfam; PF06552; TOM20_plant; 1.
DR   SUPFAM; SSF48452; TPR-like; 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
//
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