TRXH3_ARATH
ID TRXH3_ARATH Reviewed; 118 AA.
AC Q42403;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 177.
DE RecName: Full=Thioredoxin H3;
DE Short=AtTrxh3;
DE AltName: Full=Thioredoxin 3;
DE Short=AtTRX3;
GN Name=TRX3; OrderedLocusNames=At5g42980; ORFNames=MBD2.18;
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].
RC STRAIN=cv. Columbia; TISSUE=Callus;
RX PubMed=7777559; DOI=10.1073/pnas.92.12.5620;
RA Rivera-Madrid R., Mestres D., Marinho P., Jacquot J.-P., Decottignies P.,
RA Miginiac-Maslow M., Meyer Y.;
RT "Evidence for five divergent thioredoxin h sequences in Arabidopsis
RT thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:5620-5624(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=8642611; DOI=10.1007/bf02498636;
RA Sahrawy M., Hecht V., Lopez Jaramillo J., Chueca A., Chartier Y., Meyer Y.;
RT "Intron position as an evolutionary marker of thioredoxins and thioredoxin
RT domains.";
RL J. Mol. Evol. 42:422-431(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 33-105.
RC STRAIN=cv. Columbia;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
RN [8]
RP FUNCTION.
RX PubMed=14749482; DOI=10.1093/pcp/pch019;
RA Yamazaki D., Motohashi K., Kasama T., Hara Y., Hisabori T.;
RT "Target proteins of the cytosolic thioredoxins in Arabidopsis thaliana.";
RL Plant Cell Physiol. 45:18-27(2004).
RN [9]
RP INTERACTION WITH FBA5 AND FBA8.
RX PubMed=15352244; DOI=10.1002/pmic.200400805;
RA Marchand C., Le Marechal P., Meyer Y., Miginiac-Maslow M.,
RA Issakidis-Bourguet E., Decottignies P.;
RT "New targets of Arabidopsis thioredoxins revealed by proteomic analysis.";
RL Proteomics 4:2696-2706(2004).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [11]
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 [12]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP CYS-39 AND CYS-42.
RX PubMed=19339505; DOI=10.1104/pp.109.135426;
RA Park S.K., Jung Y.J., Lee J.R., Lee Y.M., Jang H.H., Lee S.S., Park J.H.,
RA Kim S.Y., Moon J.C., Lee S.Y., Chae H.B., Shin M.R., Jung J.H., Kim M.G.,
RA Kim W.Y., Yun D.J., Lee K.O., Lee S.Y.;
RT "Heat-shock and redox-dependent functional switching of an h-type
RT Arabidopsis thioredoxin from a disulfide reductase to a molecular
RT chaperone.";
RL Plant Physiol. 150:552-561(2009).
RN [13]
RP INTERACTION WITH FBA6.
RX PubMed=21782461; DOI=10.1016/j.plaphy.2011.06.009;
RA van der Linde K., Gutsche N., Leffers H.M., Lindermayr C., Mueller B.,
RA Holtgrefe S., Scheibe R.;
RT "Regulation of plant cytosolic aldolase functions by redox-modifications.";
RL Plant Physiol. Biochem. 49:946-957(2011).
RN [14]
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).
RN [15]
RP INTERACTION WITH MDH1.
RX PubMed=29194485; DOI=10.1093/jxb/erx396;
RA Huang J., Niazi A.K., Young D., Rosado L.A., Vertommen D., Bodra N.,
RA Abdelgawwad M.R., Vignols F., Wei B., Wahni K., Bashandy T., Bariat L.,
RA Van Breusegem F., Messens J., Reichheld J.P.;
RT "Self-protection of cytosolic malate dehydrogenase against oxidative stress
RT in Arabidopsis.";
RL J. Exp. Bot. 69:3491-3505(2018).
CC -!- FUNCTION: Thiol-disulfide oxidoreductase that possesses disulfide
CC reductase and insulin disulfide bonds reducing activities. Heat shock
CC causes oligomerization and formation of high molecular weight (HMW)
CC complexes with concomitant functional switching from a disulfide
CC reductase to chaperone. {ECO:0000269|PubMed:14749482,
CC ECO:0000269|PubMed:19339505}.
CC -!- SUBUNIT: Interacts with FBA5 and FBA8 (PubMed:15352244). Interacts with
CC FBA6 (PubMed:21782461). Interacts with MDH1 (PubMed:29194485).
CC {ECO:0000269|PubMed:15352244, ECO:0000269|PubMed:21782461,
CC ECO:0000269|PubMed:29194485}.
CC -!- INTERACTION:
CC Q42403; Q05431: APX1; NbExp=2; IntAct=EBI-449157, EBI-449365;
CC Q42403; Q9SRZ6: CICDH; NbExp=2; IntAct=EBI-449157, EBI-449319;
CC Q42403; Q9C5T4: WRKY18; NbExp=3; IntAct=EBI-449157, EBI-1993349;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19339505}.
CC -!- DISRUPTION PHENOTYPE: High sensitivity to heat shock.
CC {ECO:0000269|PubMed:19339505}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. Plant H-type subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: The active site contains a CPPC motif wich differs from the
CC conserved CGPC motif. {ECO:0000305}.
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DR EMBL; Z35474; CAA84611.1; -; mRNA.
DR EMBL; U35640; AAC49351.1; -; Genomic_DNA.
DR EMBL; AB008264; BAB09200.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94897.1; -; Genomic_DNA.
DR EMBL; AY059870; AAL24352.1; -; mRNA.
DR EMBL; AY065098; AAL38274.1; -; mRNA.
DR EMBL; AY093318; AAM13317.1; -; mRNA.
DR EMBL; AY114566; AAM47885.1; -; mRNA.
DR EMBL; AY085117; AAM61671.1; -; mRNA.
DR EMBL; Z35335; CAA84560.1; -; mRNA.
DR PIR; S58118; S58118.
DR RefSeq; NP_199112.1; NM_123664.4.
DR AlphaFoldDB; Q42403; -.
DR SMR; Q42403; -.
DR BioGRID; 19563; 21.
DR DIP; DIP-32720N; -.
DR IntAct; Q42403; 69.
DR STRING; 3702.AT5G42980.1; -.
DR iPTMnet; Q42403; -.
DR MetOSite; Q42403; -.
DR SwissPalm; Q42403; -.
DR PaxDb; Q42403; -.
DR PRIDE; Q42403; -.
DR ProteomicsDB; 234646; -.
DR EnsemblPlants; AT5G42980.1; AT5G42980.1; AT5G42980.
DR GeneID; 834313; -.
DR Gramene; AT5G42980.1; AT5G42980.1; AT5G42980.
DR KEGG; ath:AT5G42980; -.
DR Araport; AT5G42980; -.
DR TAIR; locus:2159971; AT5G42980.
DR eggNOG; KOG0907; Eukaryota.
DR HOGENOM; CLU_090389_14_1_1; -.
DR InParanoid; Q42403; -.
DR OMA; INTHEEF; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; Q42403; -.
DR PRO; PR:Q42403; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q42403; baseline and differential.
DR Genevisible; Q42403; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IDA:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
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 GO; GO:0009408; P:response to heat; IMP:UniProtKB.
DR GO; GO:0010188; P:response to microbial phytotoxin; IMP:TAIR.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Cytoplasm; Disulfide bond; Electron transport;
KW Redox-active center; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..118
FT /note="Thioredoxin H3"
FT /id="PRO_0000120048"
FT DOMAIN 2..113
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 39
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT ACT_SITE 42
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT DISULFID 39..42
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MUTAGEN 39
FT /note="C->S: Loss of disulfide reductase activity."
FT /evidence="ECO:0000269|PubMed:19339505"
FT MUTAGEN 42
FT /note="C->S: Loss of disulfide reductase activity."
FT /evidence="ECO:0000269|PubMed:19339505"
SQ SEQUENCE 118 AA; 13109 MW; 7AFCE291C3EB8FE2 CRC64;
MAAEGEVIAC HTVEDWTEKL KAANESKKLI VIDFTATWCP PCRFIAPVFA DLAKKHLDVV
FFKVDVDELN TVAEEFKVQA MPTFIFMKEG EIKETVVGAA KEEIIANLEK HKTVVAAA
