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TO202_ARATH
ID   TO202_ARATH             Reviewed;         210 AA.
AC   P82873; Q2HIH9; Q9FZJ6;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 2.
DT   25-MAY-2022, entry version 147.
DE   RecName: Full=Mitochondrial import receptor subunit TOM20-2;
DE   AltName: Full=Translocase of outer membrane 20 kDa subunit 2;
GN   Name=TOM20-2; OrderedLocusNames=At1g27390; ORFNames=F17L21.18;
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 37-48; 105-114 AND
RP   132-147.
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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, 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   [9]
RP   FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, AND SUBCELLULAR LOCATION.
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   [10]
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).
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   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:14730085,
CC       ECO:0000269|PubMed:17981999}; Single-pass membrane protein
CC       {ECO:0000269|PubMed:14671022, ECO:0000269|PubMed:14730085,
CC       ECO:0000269|PubMed:17981999}.
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: Slightly delayed flowering time. Triple mutants
CC       tom20-2-tom20-3-tom20-4 are viable. {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   -!- SEQUENCE CAUTION:
CC       Sequence=AAF99745.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AJ296024; CAC14429.1; -; mRNA.
DR   EMBL; AC004557; AAF99745.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE30824.1; -; Genomic_DNA.
DR   EMBL; AK228213; BAF00166.1; -; mRNA.
DR   EMBL; BT024602; ABD43000.1; -; mRNA.
DR   PIR; D86399; D86399.
DR   RefSeq; NP_174059.2; NM_102502.3.
DR   AlphaFoldDB; P82873; -.
DR   SMR; P82873; -.
DR   BioGRID; 24864; 6.
DR   IntAct; P82873; 5.
DR   MINT; P82873; -.
DR   STRING; 3702.AT1G27390.1; -.
DR   iPTMnet; P82873; -.
DR   MetOSite; P82873; -.
DR   PaxDb; P82873; -.
DR   PRIDE; P82873; -.
DR   ProteomicsDB; 234310; -.
DR   EnsemblPlants; AT1G27390.1; AT1G27390.1; AT1G27390.
DR   GeneID; 839629; -.
DR   Gramene; AT1G27390.1; AT1G27390.1; AT1G27390.
DR   KEGG; ath:AT1G27390; -.
DR   Araport; AT1G27390; -.
DR   TAIR; locus:2015904; AT1G27390.
DR   eggNOG; ENOG502QT42; Eukaryota.
DR   HOGENOM; CLU_117357_0_0_1; -.
DR   InParanoid; P82873; -.
DR   OMA; CIGNAHT; -.
DR   OrthoDB; 1560087at2759; -.
DR   PhylomeDB; P82873; -.
DR   PRO; PR:P82873; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; P82873; baseline and differential.
DR   Genevisible; P82873; AT.
DR   GO; GO:0022626; C:cytosolic ribosome; 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; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; TAS:TAIR.
DR   GO; GO:0046872; F:metal ion binding; IDA: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   Repeat; TPR repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..210
FT                   /note="Mitochondrial import receptor subunit TOM20-2"
FT                   /id="PRO_0000051544"
FT   TOPO_DOM        1..178
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        200..210
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   REPEAT          42..75
FT                   /note="TPR 1"
FT   REPEAT          83..120
FT                   /note="TPR 2"
FT   REGION          151..172
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        11
FT                   /note="L -> F (in Ref. 1; CAC14429)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   210 AA;  23170 MW;  022DF12F83586A46 CRC64;
     MEFSTADFER LIMFEHARKN SEAQYKNDPL DSENLLKWGG ALLELSQFQP IPEAKLMLND
     AISKLEEALT INPGKHQALW CIANAYTAHA FYVHDPEEAK EHFDKATEYF QRAENEDPGN
     DTYRKSLDSS LKAPELHMQF MNQGMGQQIL GGGGGGGGGG MASSNVSQSS KKKKRNTEFT
     YDVCGWIILA CGIVAWVGMA KSLGPPPPAR
 
 
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