TDX_ARATH
ID TDX_ARATH Reviewed; 380 AA.
AC Q8VWG7; Q7XJ63; Q8LG82; Q9LVI2; Q9LVI3;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=TPR repeat-containing thioredoxin TDX;
DE AltName: Full=HSP70-interacting protein 2;
DE Short=AtHIP2;
DE AltName: Full=Tetratricoredoxin;
DE Short=AtTDX;
GN Name=TDX; OrderedLocusNames=At3g17880/At3g17870; ORFNames=MEB5.10/MEB5.9;
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 [GENOMIC DNA / MRNA] (ISOFORM 1), AND FUNCTION.
RX PubMed=12433921; DOI=10.1074/jbc.m210080200;
RA Vignols F., Mouaheb N., Thomas D., Meyer Y.;
RT "Redox control of Hsp70-Co-chaperone interaction revealed by expression of
RT a thioredoxin-like Arabidopsis protein.";
RL J. Biol. Chem. 278:4516-4523(2003).
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] (ISOFORM 1).
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] (ISOFORM 1).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 259-380.
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 [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19825616; DOI=10.1093/mp/ssn076;
RA Chibani K., Wingsle G., Jacquot J.P., Gelhaye E., Rouhier N.;
RT "Comparative genomic study of the thioredoxin family in photosynthetic
RT organisms with emphasis on Populus trichocarpa.";
RL Mol. Plant 2:308-322(2009).
RN [8]
RP FUNCTION, ACTIVITY REGULATION, SUBUNIT, IDENTIFICATION BY MASS
RP SPECTROMETRY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-304 AND CYS-307.
RX PubMed=19293385; DOI=10.1073/pnas.0811231106;
RA Lee J.R., Lee S.S., Jang H.H., Lee Y.M., Park J.H., Park S.C., Moon J.C.,
RA Park S.K., Kim S.Y., Lee S.Y., Chae H.B., Jung Y.J., Kim W.Y., Shin M.R.,
RA Cheong G.W., Kim M.G., Kang K.R., Lee K.O., Yun D.J., Lee S.Y.;
RT "Heat-shock dependent oligomeric status alters the function of a plant-
RT specific thioredoxin-like protein, AtTDX.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5978-5983(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-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: Thiol-disulfide oxidoreductase that possesses insulin
CC disulfide bonds reducing activity, disulfide reductase, foldase
CC chaperone and holdase chaperone activities. Heat shock causes
CC oligomerization and formation of high molecular weiht (HMW) complexes
CC with concomitant functional switching from a disulfide reductase and
CC foldase chaperone to a holdase chaperone. May interact with HSP70
CC proteins through the TPR repeats. {ECO:0000269|PubMed:12433921,
CC ECO:0000269|PubMed:19293385}.
CC -!- SUBUNIT: Oligomerization under high temperature.
CC {ECO:0000269|PubMed:19293385}.
CC -!- INTERACTION:
CC Q8VWG7; Q8VWG7: TDX; NbExp=5; IntAct=EBI-15764744, EBI-15764744;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VWG7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VWG7-2; Sequence=VSP_039289;
CC -!- DISRUPTION PHENOTYPE: High sensitivity to heat shock.
CC {ECO:0000269|PubMed:19293385}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02710.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At3g17870 and At3g17880.; Evidence={ECO:0000305};
CC Sequence=BAB02711.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At3g17870 and At3g17880.; Evidence={ECO:0000305};
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DR EMBL; AY064251; AAL54856.1; -; mRNA.
DR EMBL; AY064252; AAL54857.1; -; Genomic_DNA.
DR EMBL; AB019230; BAB02710.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB019230; BAB02711.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76019.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76020.1; -; Genomic_DNA.
DR EMBL; AK175494; BAD43257.1; -; mRNA.
DR EMBL; AK227340; BAE99351.1; -; mRNA.
DR EMBL; AY084415; AAM60989.1; -; mRNA.
DR EMBL; BT009704; AAP88338.1; -; mRNA.
DR RefSeq; NP_001078175.1; NM_001084706.1. [Q8VWG7-2]
DR RefSeq; NP_188415.2; NM_112669.4. [Q8VWG7-1]
DR AlphaFoldDB; Q8VWG7; -.
DR SMR; Q8VWG7; -.
DR BioGRID; 6389; 1.
DR DIP; DIP-48783N; -.
DR STRING; 3702.AT3G17880.1; -.
DR iPTMnet; Q8VWG7; -.
DR PaxDb; Q8VWG7; -.
DR PRIDE; Q8VWG7; -.
DR ProteomicsDB; 246432; -. [Q8VWG7-1]
DR EnsemblPlants; AT3G17880.1; AT3G17880.1; AT3G17880. [Q8VWG7-1]
DR EnsemblPlants; AT3G17880.2; AT3G17880.2; AT3G17880. [Q8VWG7-2]
DR GeneID; 821056; -.
DR Gramene; AT3G17880.1; AT3G17880.1; AT3G17880. [Q8VWG7-1]
DR Gramene; AT3G17880.2; AT3G17880.2; AT3G17880. [Q8VWG7-2]
DR KEGG; ath:AT3G17880; -.
DR Araport; AT3G17880; -.
DR TAIR; locus:2088560; AT3G17880.
DR eggNOG; KOG0907; Eukaryota.
DR eggNOG; KOG1308; Eukaryota.
DR InParanoid; Q8VWG7; -.
DR OMA; VAANWNI; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; Q8VWG7; -.
DR PRO; PR:Q8VWG7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8VWG7; baseline and differential.
DR Genevisible; Q8VWG7; AT.
DR GO; GO:0000118; C:histone deacetylase complex; IDA:TAIR.
DR GO; GO:0030544; F:Hsp70 protein binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IDA:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0010286; P:heat acclimation; IMP:UniProtKB.
DR GO; GO:0051259; P:protein complex oligomerization; IDA:UniProtKB.
DR GO; GO:0006457; P:protein folding; IDA:UniProtKB.
DR CDD; cd14438; Hip_N; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR034649; Hip_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF18253; HipN; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chaperone; Disulfide bond;
KW Electron transport; Redox-active center; Reference proteome; Repeat;
KW TPR repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..380
FT /note="TPR repeat-containing thioredoxin TDX"
FT /id="PRO_0000394548"
FT REPEAT 112..145
FT /note="TPR 1"
FT REPEAT 147..179
FT /note="TPR 2"
FT REPEAT 181..213
FT /note="TPR 3"
FT DOMAIN 252..378
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 49..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..87
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 304
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 307
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 305
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 306
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylvaline"
FT /evidence="ECO:0007744|PubMed:22223895"
FT DISULFID 304..307
FT /note="Redox-active"
FT /evidence="ECO:0000305"
FT VAR_SEQ 50..56
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_039289"
FT MUTAGEN 304
FT /note="C->S: Loss of disulfide reductase activity."
FT /evidence="ECO:0000269|PubMed:19293385"
FT MUTAGEN 307
FT /note="C->S: Loss of disulfide reductase activity."
FT /evidence="ECO:0000269|PubMed:19293385"
FT CONFLICT 324
FT /note="V -> F (in Ref. 5; AAM60989)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 380 AA; 42846 MW; C0181F1D74CD3AA4 CRC64;
MVDAIQVAEL RRFVEQLKLN PSILHDPSLV FFKEYLRSLG AQVPKIEKTE RDYEDKAETK
PSFSPKHDDD DDDIMESDVE LDNSDVVEPD NEPPQPMGDP TAEVTDENRD DAQSEKSKAM
EAISDGRFDE AIEHLTKAVM LNPTSAILYA TRASVFLKVK KPNAAIRDAN VALQFNSDSA
KGYKSRGMAK AMLGQWEEAA ADLHVASKLD YDEEIGTMLK KVEPNAKRIE EHRRKYQRLR
KEKELQRAER ERRKQQEAQE REAQAALNDG EVISIHSTSE LEAKTKAAKK ASRLLILYFT
ATWCGPCRYM SPLYSNLATQ HSRVVFLKVD IDKANDVAAS WNISSVPTFC FIRDGKEVDK
VVGADKGSLE QKIAQHSSSK
