CXXS1_ARATH
ID CXXS1_ARATH Reviewed; 118 AA.
AC Q8LDI5; Q2HIL3; Q9SYX9; Q9XH49;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Thioredoxin-like protein CXXS1;
DE Short=AtCXXS1;
DE AltName: Full=Mono-cysteine thioredoxin 1;
GN Name=CXXS1; OrderedLocusNames=At1g11530; ORFNames=T23J18.19;
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 [GENOMIC DNA / 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=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 Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-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 FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18384502; DOI=10.1111/j.1399-3054.2008.01093.x;
RA Serrato A.J., Guilleminot J., Meyer Y., Vignols F.;
RT "AtCXXS: atypical members of the Arabidopsis thaliana thioredoxin h family
RT with a remarkably high disulfide isomerase activity.";
RL Physiol. Plantarum 133:611-622(2008).
RN [7]
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: Possesses low disulfide reductase activity, but efficient
CC protein disulfide isomerase activity. Does not possess
CC deglutathionylation activity. {ECO:0000269|PubMed:18384502}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18384502}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:18384502}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved cysteine (here Ser-39), present in the
CC redox-active center, which is one of the conserved features of the
CC thioredoxin family. {ECO:0000305}.
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DR EMBL; AF144390; AAD35008.1; -; mRNA.
DR EMBL; AF144392; AAD37583.1; -; Genomic_DNA.
DR EMBL; AC011661; AAF16634.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28748.1; -; Genomic_DNA.
DR EMBL; BT024568; ABD38907.1; -; mRNA.
DR EMBL; AY085990; AAM63200.1; -; mRNA.
DR PIR; F86248; F86248.
DR RefSeq; NP_172620.1; NM_101026.3.
DR AlphaFoldDB; Q8LDI5; -.
DR SMR; Q8LDI5; -.
DR STRING; 3702.AT1G11530.1; -.
DR PaxDb; Q8LDI5; -.
DR PRIDE; Q8LDI5; -.
DR ProteomicsDB; 220379; -.
DR EnsemblPlants; AT1G11530.1; AT1G11530.1; AT1G11530.
DR GeneID; 837696; -.
DR Gramene; AT1G11530.1; AT1G11530.1; AT1G11530.
DR KEGG; ath:AT1G11530; -.
DR Araport; AT1G11530; -.
DR TAIR; locus:2200141; AT1G11530.
DR eggNOG; KOG0907; Eukaryota.
DR HOGENOM; CLU_090389_14_1_1; -.
DR InParanoid; Q8LDI5; -.
DR OMA; AGNKHVL; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; Q8LDI5; -.
DR PRO; PR:Q8LDI5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LDI5; baseline and differential.
DR Genevisible; Q8LDI5; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IDA:TAIR.
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 2: Evidence at transcript level;
KW Cytoplasm; Isomerase; Reference proteome.
FT CHAIN 1..118
FT /note="Thioredoxin-like protein CXXS1"
FT /id="PRO_0000120065"
FT DOMAIN 2..110
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT CONFLICT 14
FT /note="N -> D (in Ref. 5; AAM63200)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="D -> G (in Ref. 1; AAD37583)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 118 AA; 13334 MW; 2D6994B3F03B039A CRC64;
MARVVKIDSA ESWNFYVSQA KNQNCPIVAH FTALWCIPSV FMNSFFEELA FNYKDALFLI
VDVDEVKEVA SQLEVKAMPT FLFLKDGNAM DKLVGANPDE IKKRVDGFVQ SSRVVHIA
