TO401_ARATH
ID TO401_ARATH Reviewed; 309 AA.
AC Q9LHE5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=Mitochondrial import receptor subunit TOM40-1;
DE AltName: Full=Translocase of outer membrane 40 kDa subunit homolog 1;
DE Contains:
DE RecName: Full=Mitochondrial import receptor subunit TOM40-1, N-terminally processed;
GN Name=TOM40-1; OrderedLocusNames=At3g20000; ORFNames=MZE19.5;
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;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
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 PROTEIN SEQUENCE OF 2-16; 22-43; 64-81; 208-220 AND 246-259.
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 [5]
RP PROTEIN SEQUENCE OF 2-16 AND 247-259, AND SUBCELLULAR LOCATION.
RC TISSUE=Leaf, and Stem;
RX PubMed=11743114; DOI=10.1104/pp.010474;
RA Kruft V., Eubel H., Jaensch L., Werhahn W., Braun H.-P.;
RT "Proteomic approach to identify novel mitochondrial proteins in
RT Arabidopsis.";
RL Plant Physiol. 127:1694-1710(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 IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
RN [8]
RP TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR
RP LOCATION, 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
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 Directly involved in the pore formation.
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|Ref.6}.
CC -!- INTERACTION:
CC Q9LHE5; O64471: MTX1; NbExp=2; IntAct=EBI-2124038, EBI-2123898;
CC Q9LHE5; F4KCL7: OM64; NbExp=2; IntAct=EBI-2124038, EBI-2124066;
CC Q9LHE5; P82805: TOM20-4; NbExp=2; IntAct=EBI-2124038, EBI-2351908;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:11743114, ECO:0000269|PubMed:14671022,
CC ECO:0000269|PubMed:14730085}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11743114, ECO:0000269|PubMed:14671022,
CC ECO:0000269|PubMed:14730085}.
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 -!- SIMILARITY: Belongs to the Tom40 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB03165.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP002050; BAB03165.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76317.1; -; Genomic_DNA.
DR EMBL; AY050925; AAK93602.1; -; mRNA.
DR EMBL; AY117216; AAM51291.1; -; mRNA.
DR RefSeq; NP_188634.1; NM_112890.5.
DR AlphaFoldDB; Q9LHE5; -.
DR SMR; Q9LHE5; -.
DR BioGRID; 6870; 6.
DR IntAct; Q9LHE5; 6.
DR MINT; Q9LHE5; -.
DR STRING; 3702.AT3G20000.1; -.
DR iPTMnet; Q9LHE5; -.
DR PaxDb; Q9LHE5; -.
DR PRIDE; Q9LHE5; -.
DR ProteomicsDB; 234360; -.
DR DNASU; 821538; -.
DR EnsemblPlants; AT3G20000.1; AT3G20000.1; AT3G20000.
DR GeneID; 821538; -.
DR Gramene; AT3G20000.1; AT3G20000.1; AT3G20000.
DR KEGG; ath:AT3G20000; -.
DR Araport; AT3G20000; -.
DR TAIR; locus:2095355; AT3G20000.
DR eggNOG; KOG3296; Eukaryota.
DR HOGENOM; CLU_042174_1_0_1; -.
DR InParanoid; Q9LHE5; -.
DR OMA; SHQFAMG; -.
DR OrthoDB; 1346842at2759; -.
DR PhylomeDB; Q9LHE5; -.
DR PRO; PR:Q9LHE5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LHE5; baseline and differential.
DR Genevisible; Q9LHE5; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015450; F:protein-transporting ATPase activity; ISS:TAIR.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0006626; P:protein targeting to mitochondrion; ISS:TAIR.
DR CDD; cd07305; Porin3_Tom40; 1.
DR Gene3D; 2.40.160.10; -; 1.
DR InterPro; IPR023614; Porin_dom_sf.
DR InterPro; IPR027246; Porin_Euk/Tom40.
DR InterPro; IPR037930; Tom40.
DR PANTHER; PTHR10802; PTHR10802; 1.
DR Pfam; PF01459; Porin_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Ion transport; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Porin; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane beta strand; Transport.
FT CHAIN 1..309
FT /note="Mitochondrial import receptor subunit TOM40-1"
FT /id="PRO_0000425793"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000269|PubMed:11161051,
FT ECO:0000269|PubMed:11743114, ECO:0007744|PubMed:22223895"
FT CHAIN 2..309
FT /note="Mitochondrial import receptor subunit TOM40-1, N-
FT terminally processed"
FT /id="PRO_0000051531"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9SX55"
FT MOD_RES 2
FT /note="N-acetylalanine; in Mitochondrial import receptor
FT subunit TOM40-1, N-terminally processed"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 309 AA; 34250 MW; 60F108524F91E1E4 CRC64;
MADLLPPLTA AQVDAKTKVD EKVDYSNLPS PVPYEELHRE ALMSLKSDNF EGLRFDFTRA
LNQKFSLSHS VMMGPTEVPA QSPETTIKIP TAHYEFGANY YDPKLLLIGR VMTDGRLNAR
LKADLTDKLV VKANALITNE EHMSQAMFNF DYMGSDYRAQ LQLGQSALIG ATYIQSVTNH
LSLGGEIFWA GVPRKSGIGY AARYETDKMV ASGQVASTGA VVMNYVQKIS DKVSLATDFM
YNYFSRDVTA SVGYDYMLRQ ARVRGKIDSN GVASALLEER LSMGLNFLLS AELDHKKKDY
KFGFGLTVG
