TRXH2_ARATH
ID TRXH2_ARATH Reviewed; 133 AA.
AC Q38879; Q39240;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Thioredoxin H2;
DE Short=AtTrxh2;
DE AltName: Full=Thioredoxin 2;
DE Short=AtTRX2;
GN Name=TRX2; OrderedLocusNames=At5g39950; ORFNames=MYH19.14;
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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 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 [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 SUBCELLULAR LOCATION.
RX PubMed=20133584; DOI=10.1073/pnas.0913759107;
RA Meng L., Wong J.H., Feldman L.J., Lemaux P.G., Buchanan B.B.;
RT "A membrane-associated thioredoxin required for plant growth moves from
RT cell to cell, suggestive of a role in intercellular communication.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:3900-3905(2010).
RN [9]
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 probably involved in the redox
CC regulation of a number of cytosolic enzymes. Possesses insulin
CC disulfide bonds reducing activity. {ECO:0000269|PubMed:14749482}.
CC -!- SUBUNIT: Interacts with MDH1. {ECO:0000269|PubMed:29194485}.
CC -!- INTERACTION:
CC Q38879; Q3E9D5: SAMDC4; NbExp=3; IntAct=EBI-727983, EBI-25512418;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20133584}.
CC Mitochondrion {ECO:0000269|PubMed:20133584}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. Plant H-type subfamily.
CC {ECO:0000305}.
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DR EMBL; Z35475; CAA84612.1; -; mRNA.
DR EMBL; U35826; AAC49353.1; -; Genomic_DNA.
DR EMBL; AB010077; BAB10219.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94495.1; -; Genomic_DNA.
DR EMBL; AY048235; AAK82498.1; -; mRNA.
DR EMBL; AY113052; AAM47360.1; -; mRNA.
DR PIR; S58123; S58123.
DR RefSeq; NP_198811.1; NM_123358.4.
DR AlphaFoldDB; Q38879; -.
DR SMR; Q38879; -.
DR BioGRID; 19243; 1.
DR IntAct; Q38879; 1.
DR STRING; 3702.AT5G39950.1; -.
DR PaxDb; Q38879; -.
DR PRIDE; Q38879; -.
DR ProteomicsDB; 232421; -.
DR EnsemblPlants; AT5G39950.1; AT5G39950.1; AT5G39950.
DR GeneID; 833992; -.
DR Gramene; AT5G39950.1; AT5G39950.1; AT5G39950.
DR KEGG; ath:AT5G39950; -.
DR Araport; AT5G39950; -.
DR TAIR; locus:2178007; AT5G39950.
DR eggNOG; KOG0907; Eukaryota.
DR HOGENOM; CLU_090389_14_1_1; -.
DR InParanoid; Q38879; -.
DR OMA; HAMADKF; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; Q38879; -.
DR BioCyc; ARA:AT5G39950-MON; -.
DR PRO; PR:Q38879; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q38879; baseline and differential.
DR Genevisible; Q38879; AT.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IDA:TAIR.
DR GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IDA:TAIR.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR InterPro; IPR005746; Thioredoxin.
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 TIGRFAMs; TIGR01068; thioredoxin; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Disulfide bond; Electron transport; Mitochondrion;
KW Redox-active center; Reference proteome; Transport.
FT CHAIN 1..133
FT /note="Thioredoxin H2"
FT /id="PRO_0000120047"
FT DOMAIN 6..133
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 59
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 62
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 53
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000250"
FT SITE 60
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 61
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT DISULFID 59..62
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT CONFLICT 7
FT /note="T -> I (in Ref. 2; AAC49353)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="S -> SS (in Ref. 2; AAC49353)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="K -> Q (in Ref. 2; AAC49353)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 133 AA; 14676 MW; BC034E2BCD4D3CA3 CRC64;
MGGALSTVFG SGEDATAAGT ESEPSRVLKF SSSARWQLHF NEIKESNKLL VVDFSASWCG
PCRMIEPAIH AMADKFNDVD FVKLDVDELP DVAKEFNVTA MPTFVLVKRG KEIERIIGAK
KDELEKKVSK LRA
