TRXH4_ARATH
ID TRXH4_ARATH Reviewed; 119 AA.
AC Q39239; Q38880; Q541W4; Q8L907; Q9FXH2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 25-MAY-2022, entry version 158.
DE RecName: Full=Thioredoxin H4;
DE Short=AtTrxh4;
DE AltName: Full=Thioredoxin 4;
DE Short=AtTRX4;
GN Name=TRX4; OrderedLocusNames=At1g19730; ORFNames=F14P1.32, F6F9.21;
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=Flower bud;
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 [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;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 [GENOMIC DNA] OF 1-110.
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 [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 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 [10]
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA84610.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z35473; CAA84610.1; ALT_FRAME; mRNA.
DR EMBL; AC007797; AAG12565.1; -; Genomic_DNA.
DR EMBL; AC024609; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE29892.1; -; Genomic_DNA.
DR EMBL; AK118542; BAC43145.1; -; mRNA.
DR EMBL; BT004710; AAO42956.1; -; mRNA.
DR EMBL; AY088698; AAM67018.1; -; mRNA.
DR EMBL; U35828; AAC49355.1; -; Genomic_DNA.
DR PIR; D86330; D86330.
DR PIR; S58119; S58119.
DR RefSeq; NP_173403.1; NM_101829.4.
DR AlphaFoldDB; Q39239; -.
DR SMR; Q39239; -.
DR BioGRID; 23801; 1.
DR STRING; 3702.AT1G19730.1; -.
DR SwissPalm; Q39239; -.
DR PaxDb; Q39239; -.
DR PRIDE; Q39239; -.
DR ProteomicsDB; 228705; -.
DR EnsemblPlants; AT1G19730.1; AT1G19730.1; AT1G19730.
DR GeneID; 838562; -.
DR Gramene; AT1G19730.1; AT1G19730.1; AT1G19730.
DR KEGG; ath:AT1G19730; -.
DR Araport; AT1G19730; -.
DR TAIR; locus:2013169; AT1G19730.
DR eggNOG; KOG0907; Eukaryota.
DR HOGENOM; CLU_090389_14_1_1; -.
DR InParanoid; Q39239; -.
DR OMA; MKEWIKQ; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; Q39239; -.
DR PRO; PR:Q39239; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q39239; baseline and differential.
DR Genevisible; Q39239; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; 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; Redox-active center;
KW Reference proteome; Transport.
FT CHAIN 1..119
FT /note="Thioredoxin H4"
FT /id="PRO_0000120049"
FT DOMAIN 2..115
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 40
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT ACT_SITE 43
FT /note="Nucleophile"
FT /evidence="ECO:0000255"
FT DISULFID 40..43
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT CONFLICT 10
FT /note="G -> S (in Ref. 6; AAM67018)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="A -> VVNQFEA (in Ref. 1; CAA84610)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 119 AA; 13063 MW; E2A37655F889FB24 CRC64;
MAAEEGQVIG CHTNDVWTVQ LDKAKESNKL IVIDFTASWC PPCRMIAPIF NDLAKKFMSS
AIFFKVDVDE LQSVAKEFGV EAMPTFVFIK AGEVVDKLVG ANKEDLQAKI VKHTGVTTA
