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Database: UniProt
Entry: Q8LDI5
LinkDB: Q8LDI5
Original site: Q8LDI5 
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   01-OCT-2014, entry version 85.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   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.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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
RT   family 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
CC       efficient 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   -!- SIMILARITY: Contains 1 thioredoxin domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00691}.
CC   -!- CAUTION: Lacks the conserved cysteine (here Ser-39), present in
CC       the redox-active center, which is one of the conserved features of
CC       the 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_101026.2.
DR   UniGene; At.11326; -.
DR   UniGene; At.63949; -.
DR   ProteinModelPortal; Q8LDI5; -.
DR   SMR; Q8LDI5; 27-105.
DR   PaxDb; Q8LDI5; -.
DR   PRIDE; Q8LDI5; -.
DR   EnsemblPlants; AT1G11530.1; AT1G11530.1; AT1G11530.
DR   GeneID; 837696; -.
DR   KEGG; ath:AT1G11530; -.
DR   GeneFarm; 4193; -.
DR   TAIR; AT1G11530; -.
DR   eggNOG; COG0526; -.
DR   HOGENOM; HOG000292977; -.
DR   InParanoid; Q8LDI5; -.
DR   KO; K03671; -.
DR   OMA; SWCVTSL; -.
DR   PhylomeDB; Q8LDI5; -.
DR   Genevestigator; Q8LDI5; -.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IDA:TAIR.
DR   GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IDA:GOC.
DR   Gene3D; 3.40.30.10; -; 1.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10438; PTHR10438; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PIRSF; PIRSF000077; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Cytoplasm; Isomerase; Reference proteome.
FT   CHAIN         1    118       Thioredoxin-like protein CXXS1.
FT                                /FTId=PRO_0000120065.
FT   DOMAIN        2    110       Thioredoxin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00691}.
FT   CONFLICT     14     14       N -> D (in Ref. 5; AAM63200).
FT                                {ECO:0000305}.
FT   CONFLICT     86     86       D -> G (in Ref. 1; AAD37583).
FT                                {ECO:0000305}.
SQ   SEQUENCE   118 AA;  13334 MW;  2D6994B3F03B039A CRC64;
     MARVVKIDSA ESWNFYVSQA KNQNCPIVAH FTALWCIPSV FMNSFFEELA FNYKDALFLI
     VDVDEVKEVA SQLEVKAMPT FLFLKDGNAM DKLVGANPDE IKKRVDGFVQ SSRVVHIA
//
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