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TCLOT_ARATH
ID   TCLOT_ARATH             Reviewed;         134 AA.
AC   Q9FMN4; Q8LD10;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Thioredoxin-like protein Clot;
DE   AltName: Full=Thioredoxin Clot;
DE            Short=AtClot;
GN   OrderedLocusNames=At5g42850; ORFNames=MBD2.4;
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=9501997; DOI=10.1093/dnares/4.6.401;
RA   Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT   features of the regions of 1,191,918 bp covered by seventeen physically
RT   assigned P1 clones.";
RL   DNA Res. 4:401-414(1997).
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;
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   [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   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).
CC   -!- FUNCTION: Probable thiol-disulfide oxidoreductase that may participate
CC       in various redox reactions.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
CC   -!- CAUTION: The active site contains a CPDC motif wich differs from the
CC       conserved CGPC motif. {ECO:0000305}.
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DR   EMBL; AB008264; BAB09186.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94874.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94875.1; -; Genomic_DNA.
DR   EMBL; AK118124; BAC42750.1; -; mRNA.
DR   EMBL; BT005444; AAO63864.1; -; mRNA.
DR   EMBL; AY086278; AAM64350.1; -; mRNA.
DR   RefSeq; NP_568614.1; NM_123650.3.
DR   RefSeq; NP_974872.1; NM_203143.2.
DR   AlphaFoldDB; Q9FMN4; -.
DR   SMR; Q9FMN4; -.
DR   BioGRID; 19546; 1.
DR   IntAct; Q9FMN4; 1.
DR   STRING; 3702.AT5G42850.1; -.
DR   iPTMnet; Q9FMN4; -.
DR   PaxDb; Q9FMN4; -.
DR   PRIDE; Q9FMN4; -.
DR   ProteomicsDB; 234228; -.
DR   EnsemblPlants; AT5G42850.1; AT5G42850.1; AT5G42850.
DR   EnsemblPlants; AT5G42850.2; AT5G42850.2; AT5G42850.
DR   GeneID; 834296; -.
DR   Gramene; AT5G42850.1; AT5G42850.1; AT5G42850.
DR   Gramene; AT5G42850.2; AT5G42850.2; AT5G42850.
DR   KEGG; ath:AT5G42850; -.
DR   Araport; AT5G42850; -.
DR   TAIR; locus:2160021; AT5G42850.
DR   eggNOG; KOG3425; Eukaryota.
DR   HOGENOM; CLU_120161_1_0_1; -.
DR   InParanoid; Q9FMN4; -.
DR   OMA; EWRTKEN; -.
DR   OrthoDB; 1624076at2759; -.
DR   PhylomeDB; Q9FMN4; -.
DR   PRO; PR:Q9FMN4; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FMN4; baseline and differential.
DR   Genevisible; Q9FMN4; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR   GO; GO:0047134; F:protein-disulfide reductase (NAD(P)) activity; IBA:GO_Central.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR045108; TXNDC17-like.
DR   InterPro; IPR010357; TXNDC17_dom.
DR   PANTHER; PTHR12452; PTHR12452; 1.
DR   Pfam; PF06110; DUF953; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Electron transport; Redox-active center;
KW   Reference proteome; Transport.
FT   CHAIN           1..134
FT                   /note="Thioredoxin-like protein Clot"
FT                   /id="PRO_0000394546"
FT   DOMAIN          1..134
FT                   /note="Thioredoxin"
FT   ACT_SITE        48
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        51
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   DISULFID        48..51
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        6
FT                   /note="V -> L (in Ref. 5; AAM64350)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        16
FT                   /note="S -> I (in Ref. 5; AAM64350)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        26
FT                   /note="S -> N (in Ref. 5; AAM64350)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        70
FT                   /note="K -> N (in Ref. 5; AAM64350)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   134 AA;  15206 MW;  9E9EDDB40E59B2A0 CRC64;
     MTLKKVDANP STLESSLQEL KSDETSRSKI NFILFLADND PTTGQSWCPD CVRAEPVIYK
     TLEEFPEEVK LIRAYAGDRP TWRTPAHPWR VDSRFKLTGV PTLVRWDGDS VKGRLEDHQA
     HLPHLILPLL APST
 
 
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