CDSP_ARATH
ID CDSP_ARATH Reviewed; 302 AA.
AC Q9SGS4; Q8LDJ9; Q95GH8;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=Thioredoxin-like protein CDSP32, chloroplastic;
DE AltName: Full=Chloroplastic drought-induced stress protein of 32 KDa;
DE Short=AtCDSP32;
DE Flags: Precursor;
GN Name=CDSP32; OrderedLocusNames=At1g76080; ORFNames=T23E18.2;
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], SUBCELLULAR LOCATION, INDUCTION, AND
RP INTERACTION WITH BAS1.
RX PubMed=12084836; DOI=10.1105/tpc.001644;
RA Broin M., Cuine S., Eymery F., Rey P.;
RT "The plastidic 2-cysteine peroxiredoxin is a target for a thioredoxin
RT involved in the protection of the photosynthetic apparatus against
RT oxidative damage.";
RL Plant Cell 14:1417-1432(2002).
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;
RA Kim C.J., Chen H., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [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).
RN [7]
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).
RN [8]
RP FUNCTION.
RX PubMed=20236937; DOI=10.1074/jbc.m110.108373;
RA Tarrago L., Laugier E., Zaffagnini M., Marchand C.H., Le Marechal P.,
RA Lemaire S.D., Rey P.;
RT "Plant thioredoxin CDSP32 regenerates 1-Cys methionine sulfoxide reductase
RT B activity through the direct reduction of sulfenic acid.";
RL J. Biol. Chem. 285:14964-14972(2010).
CC -!- FUNCTION: Probable thiol-disulfide oxidoreductase involved in
CC resistance to oxidative stress. May participate in the reduction of
CC alkyl hydroperoxides derived from oxidative stress by acting as a
CC physiological electron donor to the BAS1 peroxiredoxin. May regenerate
CC methionine sulfoxide reductase B1 (MSRB1) activity through sulfenic
CC acid reduction. {ECO:0000269|PubMed:20236937}.
CC -!- SUBUNIT: Interacts with the plastidial peroxiredoxin BAS1.
CC {ECO:0000269|PubMed:12084836}.
CC -!- INTERACTION:
CC Q9SGS4; Q8L765: BPM1; NbExp=3; IntAct=EBI-25517863, EBI-540891;
CC Q9SGS4; Q17TI5: BRX; NbExp=3; IntAct=EBI-25517863, EBI-4426649;
CC Q9SGS4; Q9FDW1: MYB44; NbExp=3; IntAct=EBI-25517863, EBI-15192813;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:12084836, ECO:0000269|PubMed:19259774}.
CC -!- INDUCTION: By drought stress and photooxidative conditions.
CC {ECO:0000269|PubMed:12084836}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR EMBL; AJ318055; CAC39419.1; -; mRNA.
DR EMBL; AC009978; AAF17651.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35794.1; -; Genomic_DNA.
DR EMBL; BT024860; ABD65591.1; -; mRNA.
DR EMBL; AY085972; AAM63182.1; -; mRNA.
DR PIR; A96789; A96789.
DR RefSeq; NP_177735.1; NM_106257.3.
DR AlphaFoldDB; Q9SGS4; -.
DR SMR; Q9SGS4; -.
DR BioGRID; 29159; 4.
DR IntAct; Q9SGS4; 3.
DR STRING; 3702.AT1G76080.1; -.
DR iPTMnet; Q9SGS4; -.
DR PaxDb; Q9SGS4; -.
DR PRIDE; Q9SGS4; -.
DR ProteomicsDB; 220523; -.
DR EnsemblPlants; AT1G76080.1; AT1G76080.1; AT1G76080.
DR GeneID; 843940; -.
DR Gramene; AT1G76080.1; AT1G76080.1; AT1G76080.
DR KEGG; ath:AT1G76080; -.
DR Araport; AT1G76080; -.
DR TAIR; locus:2199803; AT1G76080.
DR eggNOG; KOG0907; Eukaryota.
DR HOGENOM; CLU_064180_0_0_1; -.
DR InParanoid; Q9SGS4; -.
DR OMA; KVPHFTF; -.
DR OrthoDB; 1088692at2759; -.
DR PhylomeDB; Q9SGS4; -.
DR PRO; PR:Q9SGS4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SGS4; baseline and differential.
DR Genevisible; Q9SGS4; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
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; IEA:EnsemblPlants.
DR GO; GO:0045454; P:cell redox homeostasis; IDA:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0010286; P:heat acclimation; IMP:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; TAS:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; TAS:UniProtKB.
DR InterPro; IPR044192; CDSP32.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR47578; PTHR47578; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF52833; SSF52833; 2.
PE 1: Evidence at protein level;
KW Chloroplast; Disulfide bond; Electron transport; Plastid;
KW Redox-active center; Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..56
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 57..302
FT /note="Thioredoxin-like protein CDSP32, chloroplastic"
FT /id="PRO_0000394544"
FT DOMAIN 163..298
FT /note="Thioredoxin"
FT ACT_SITE 219
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 222
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 213
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000250"
FT SITE 220
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 221
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT DISULFID 219..222
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT CONFLICT 86
FT /note="V -> E (in Ref. 5; AAM63182)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="K -> R (in Ref. 5; AAM63182)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="A -> T (in Ref. 5; AAM63182)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 302 AA; 33685 MW; B62A2D9D73B07908 CRC64;
MATVANFLAK PISTVVPRPS SAVASTSSFV FFNHKTNPLF RRKNLPKRLF SAVKIKAGAA
SPGKVGTPPA NDEKVQKIHS GEEFDVALKN AKSKLVVAEF ATSKSDQSNK IYPFMVELSR
TCNDVVFLLV MGDESDKTRE LCRREKIEKV PHFSFYKSME KIHEEEGIEP DQLMGDVLYY
GDNHSAVVQL HGRPDVEKLI DENRTGGKLI VLDVGLKHCG PCVKVYPTVL KLSRSMSETV
VFARMNGDEN DSCMEFLKDM NVIEVPTFLF IRDGEIRGRY VGSGKGELIG EILRYSGVRV
TY
