TRXO2_ARATH
ID TRXO2_ARATH Reviewed; 159 AA.
AC Q93VQ9; Q9FYJ3;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Thioredoxin O2, mitochondrial;
DE Short=AtTrxo2;
DE Flags: Precursor;
GN OrderedLocusNames=At1g31020; ORFNames=F17F8.6;
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], AND FUNCTION.
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 [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=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).
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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. Plant O-type subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF98203.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF396650; AAK83918.1; -; mRNA.
DR EMBL; AC000107; AAF98203.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31307.1; -; Genomic_DNA.
DR EMBL; AY050435; AAK91451.1; -; mRNA.
DR EMBL; AY093796; AAM10412.1; -; mRNA.
DR RefSeq; NP_564371.1; NM_102840.5.
DR PDB; 6G62; X-ray; 1.50 A; A=48-159.
DR PDBsum; 6G62; -.
DR AlphaFoldDB; Q93VQ9; -.
DR SMR; Q93VQ9; -.
DR STRING; 3702.AT1G31020.1; -.
DR PaxDb; Q93VQ9; -.
DR PRIDE; Q93VQ9; -.
DR ProteomicsDB; 232419; -.
DR EnsemblPlants; AT1G31020.1; AT1G31020.1; AT1G31020.
DR GeneID; 839988; -.
DR Gramene; AT1G31020.1; AT1G31020.1; AT1G31020.
DR KEGG; ath:AT1G31020; -.
DR Araport; AT1G31020; -.
DR TAIR; locus:2015736; AT1G31020.
DR eggNOG; KOG0907; Eukaryota.
DR HOGENOM; CLU_090389_6_1_1; -.
DR InParanoid; Q93VQ9; -.
DR OMA; HQIGRNS; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; Q93VQ9; -.
DR PRO; PR:Q93VQ9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q93VQ9; baseline and differential.
DR Genevisible; Q93VQ9; AT.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..159
FT /note="Thioredoxin O2, mitochondrial"
FT /id="PRO_0000394538"
FT DOMAIN 43..159
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 83
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 86
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 84
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 85
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C9Y6"
FT DISULFID 83..86
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:6G62"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:6G62"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:6G62"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:6G62"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:6G62"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:6G62"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:6G62"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:6G62"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:6G62"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:6G62"
FT STRAND 126..134
FT /evidence="ECO:0007829|PDB:6G62"
FT STRAND 137..145
FT /evidence="ECO:0007829|PDB:6G62"
FT HELIX 147..158
FT /evidence="ECO:0007829|PDB:6G62"
SQ SEQUENCE 159 AA; 17623 MW; 92444196B6A1374C CRC64;
MKSQWSNFHQ IGRNSFLAAS TVYVSNEFNF LNTSLLNRRS FCFAEGDRSS FVVLKSEAEF
NSALSKARDG SLPSVFYFTA AWCGPCRLIS PVILELSNKY PDVTTYKVDI DEGGLSNAIG
KLNVSAVPTL QFFKGGVKKA EIVGVDVVRL KSVMEQLYK
