TRXF2_ARATH
ID TRXF2_ARATH Reviewed; 185 AA.
AC Q9XFH9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Thioredoxin F2, chloroplastic;
DE Short=AtTrxf2;
DE AltName: Full=Thioredoxin F1;
DE Short=AtTrxf1;
DE Flags: Precursor;
GN OrderedLocusNames=At5g16400; ORFNames=MQK4.13;
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].
RX PubMed=10498962; DOI=10.1016/s1360-1385(99)01475-2;
RA Meyer Y., Verdoucq L., Vignols F.;
RT "Plant thioredoxins and glutaredoxins: identity and putative roles.";
RL Trends Plant Sci. 4:388-394(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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=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 [5]
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=19259774; DOI=10.1007/s11103-009-9471-4;
RA Cain P., Hall M., Schroder W.P., Kieselbach T., Robinson C.;
RT "A novel extended family of stromal thioredoxins.";
RL Plant Mol. Biol. 70:273-281(2009).
CC -!- FUNCTION: Probable thiol-disulfide oxidoreductase involved in the redox
CC regulation of enzymes of both reductive pentose phosphate pathway
CC (Calvin-Benson cycle) and oxidative pentose phosphate pathway.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9XFH9; Q17TI5: BRX; NbExp=3; IntAct=EBI-25516100, EBI-4426649;
CC Q9XFH9; O23160: MYB73; NbExp=3; IntAct=EBI-25516100, EBI-25506855;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:19259774}.
CC -!- PTM: Glutathionylation at Cys-136 decreases its ability to be reduced
CC by ferredoxin-thioredoxin reductase and reduces its efficiency in
CC activating target chloroplastic enzymes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. Plant F-type subfamily.
CC {ECO:0000305}.
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DR EMBL; AF144386; AAD35004.1; -; mRNA.
DR EMBL; AB005242; BAB09607.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92288.1; -; Genomic_DNA.
DR EMBL; AF370356; AAK44171.1; -; mRNA.
DR EMBL; AY059086; AAL15192.1; -; mRNA.
DR RefSeq; NP_197144.1; NM_121645.5.
DR PDB; 7C2B; X-ray; 1.79 A; C=71-185.
DR PDBsum; 7C2B; -.
DR AlphaFoldDB; Q9XFH9; -.
DR SMR; Q9XFH9; -.
DR BioGRID; 16777; 4.
DR IntAct; Q9XFH9; 2.
DR STRING; 3702.AT5G16400.1; -.
DR MetOSite; Q9XFH9; -.
DR PaxDb; Q9XFH9; -.
DR PRIDE; Q9XFH9; -.
DR ProteomicsDB; 228704; -.
DR EnsemblPlants; AT5G16400.1; AT5G16400.1; AT5G16400.
DR GeneID; 831501; -.
DR Gramene; AT5G16400.1; AT5G16400.1; AT5G16400.
DR KEGG; ath:AT5G16400; -.
DR Araport; AT5G16400; -.
DR TAIR; locus:2171322; AT5G16400.
DR eggNOG; KOG0907; Eukaryota.
DR HOGENOM; CLU_090389_9_0_1; -.
DR InParanoid; Q9XFH9; -.
DR OMA; DCNEENK; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; Q9XFH9; -.
DR PRO; PR:Q9XFH9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9XFH9; baseline and differential.
DR Genevisible; Q9XFH9; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0008047; F:enzyme activator activity; IDA:TAIR.
DR GO; GO:0045454; P:cell redox homeostasis; IGI:TAIR.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IDA:TAIR.
DR GO; GO:0009642; P:response to light intensity; IGI: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 3D-structure; Chloroplast; Disulfide bond; Electron transport;
KW Glutathionylation; Plastid; Redox-active center; Reference proteome;
KW Transit peptide; Transport.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..185
FT /note="Thioredoxin F2, chloroplastic"
FT /id="PRO_0000034157"
FT DOMAIN 59..184
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 109
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 112
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 103
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000250"
FT SITE 110
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 111
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT MOD_RES 136
FT /note="S-glutathionyl cysteine; transient"
FT /evidence="ECO:0000250"
FT DISULFID 109..112
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:7C2B"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:7C2B"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:7C2B"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:7C2B"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:7C2B"
FT HELIX 110..125
FT /evidence="ECO:0007829|PDB:7C2B"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:7C2B"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:7C2B"
FT HELIX 141..147
FT /evidence="ECO:0007829|PDB:7C2B"
FT STRAND 151..159
FT /evidence="ECO:0007829|PDB:7C2B"
FT STRAND 162..170
FT /evidence="ECO:0007829|PDB:7C2B"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:7C2B"
SQ SEQUENCE 185 AA; 19999 MW; DB7EA3FAA35EDD5C CRC64;
MPLSLRLAPS PTSFRYSPIT STGAGGFSPV KQHCRIPNSG VATKIGFCSG GGGVLDSGRR
IGSCVVRCSL ETVNVTVGQV TEVDKDTFWP IVKAAGDKIV VLDMYTQWCG PCKVIAPKYK
ELSEKYQDMV FLKLDCNQDN KPLAKELGIR VVPTFKILKD NKVVKEVTGA KYEDLLAAIE
AARSG
