TRXO1_ARATH
ID TRXO1_ARATH Reviewed; 194 AA.
AC O64764; Q8GW51;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 148.
DE RecName: Full=Thioredoxin O1, mitochondrial;
DE Short=AtTrxo1;
DE Flags: Precursor;
GN OrderedLocusNames=At2g35010; ORFNames=F19I3.24;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Quinitio C., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-194.
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11717467; DOI=10.1073/pnas.241340898;
RA Laloi C., Rayapuram N., Chartier Y., Grienenberger J.M., Bonnard G.,
RA Meyer Y.;
RT "Identification and characterization of a mitochondrial thioredoxin system
RT in plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:14144-14149(2001).
RN [6]
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).
CC -!- FUNCTION: Thiol-disulfide oxidoreductase that may participate in
CC various redox reactions. Possesses insulin disulfide bonds reducing
CC activity. Reduced by thioredoxin reductases NTRA and NTRB.
CC {ECO:0000269|PubMed:11717467}.
CC -!- INTERACTION:
CC O64764; Q17TI5: BRX; NbExp=3; IntAct=EBI-25519089, EBI-4426649;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:11717467}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. Plant O-type subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC43652.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC004238; AAC12840.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09048.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09049.1; -; Genomic_DNA.
DR EMBL; BT025773; ABF83663.1; -; mRNA.
DR EMBL; AK119076; BAC43652.1; ALT_INIT; mRNA.
DR PIR; T00482; T00482.
DR RefSeq; NP_001078006.1; NM_001084537.1.
DR RefSeq; NP_181046.1; NM_129053.6.
DR PDB; 6G61; X-ray; 1.80 A; A=83-194.
DR PDBsum; 6G61; -.
DR AlphaFoldDB; O64764; -.
DR SMR; O64764; -.
DR BioGRID; 3411; 1.
DR IntAct; O64764; 1.
DR STRING; 3702.AT2G35010.2; -.
DR SwissPalm; O64764; -.
DR PaxDb; O64764; -.
DR PRIDE; O64764; -.
DR ProteomicsDB; 228702; -.
DR EnsemblPlants; AT2G35010.1; AT2G35010.1; AT2G35010.
DR EnsemblPlants; AT2G35010.2; AT2G35010.2; AT2G35010.
DR GeneID; 818065; -.
DR Gramene; AT2G35010.1; AT2G35010.1; AT2G35010.
DR Gramene; AT2G35010.2; AT2G35010.2; AT2G35010.
DR KEGG; ath:AT2G35010; -.
DR Araport; AT2G35010; -.
DR TAIR; locus:2044772; AT2G35010.
DR eggNOG; KOG0907; Eukaryota.
DR HOGENOM; CLU_090389_6_1_1; -.
DR InParanoid; O64764; -.
DR OMA; GNWSIVR; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; O64764; -.
DR PRO; PR:O64764; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64764; baseline and differential.
DR Genevisible; O64764; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IDA:UniProtKB.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Electron transport; Mitochondrion;
KW Phosphoprotein; Redox-active center; Reference proteome; Transit peptide;
KW Transport.
FT TRANSIT 1..42
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 43..194
FT /note="Thioredoxin O1, mitochondrial"
FT /id="PRO_0000394537"
FT DOMAIN 89..194
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 118
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 121
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 119
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 120
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C9Y6"
FT DISULFID 118..121
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT CONFLICT 110
FT /note="V -> A (in Ref. 4; BAC43652)"
FT /evidence="ECO:0000305"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:6G61"
FT HELIX 92..102
FT /evidence="ECO:0007829|PDB:6G61"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:6G61"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:6G61"
FT HELIX 121..134
FT /evidence="ECO:0007829|PDB:6G61"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:6G61"
FT HELIX 151..155
FT /evidence="ECO:0007829|PDB:6G61"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:6G61"
FT STRAND 161..169
FT /evidence="ECO:0007829|PDB:6G61"
FT STRAND 172..180
FT /evidence="ECO:0007829|PDB:6G61"
FT HELIX 182..193
FT /evidence="ECO:0007829|PDB:6G61"
SQ SEQUENCE 194 AA; 21191 MW; 1DA980E60614606D CRC64;
MKGNWSIVRK VLHRQFSTLR SSTPSSRLST SIRPLVLAPN SISSLIARNS LFTASNIGPS
IDFNFSNTSL PHRRSLCSEA GGENGVVLVK SEEEFINAMS KAQDGSLPSV FYFTAAWCGP
CRFISPVIVE LSKQYPDVTT YKVDIDEGGI SNTISKLNIT AVPTLHFFKG GSKKGEVVGA
DVTKLKNLME QLYK
