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TRXY2_ARATH
ID   TRXY2_ARATH             Reviewed;         167 AA.
AC   Q8L7S9; Q9XIG4;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 139.
DE   RecName: Full=Thioredoxin Y2, chloroplastic;
DE            Short=AtTrxy2;
DE   Flags: Precursor;
GN   OrderedLocusNames=At1g43560; ORFNames=T10P12.4;
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=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   [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=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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   AND INDUCTION.
RX   PubMed=15531707; DOI=10.1104/pp.104.052233;
RA   Collin V., Lamkemeyer P., Miginiac-Maslow M., Hirasawa M., Knaff D.B.,
RA   Dietz K.J., Issakidis-Bourguet E.;
RT   "Characterization of plastidial thioredoxins from Arabidopsis belonging to
RT   the new y-type.";
RL   Plant Physiol. 136:4088-4095(2004).
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).
CC   -!- FUNCTION: Thiol-disulfide oxidoreductase that poorly activates
CC       chloroplastic malate dehydrogenase (NADP-MDH) and fructose-1,6-
CC       bisphosphatase. Provides reducing equivalents for peroxiredoxin Q.
CC       {ECO:0000269|PubMed:15531707}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC       {ECO:0000269|PubMed:15531707, ECO:0000269|PubMed:19259774}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves. {ECO:0000269|PubMed:15531707}.
CC   -!- DEVELOPMENTAL STAGE: Expression decreases in developing seeds and
CC       increases during seed germination. {ECO:0000269|PubMed:15531707}.
CC   -!- INDUCTION: By light in leaves. {ECO:0000269|PubMed:15531707}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. Plant Y-type subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD39273.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC007203; AAD39273.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE31970.1; -; Genomic_DNA.
DR   EMBL; AY128276; AAM91085.1; -; mRNA.
DR   EMBL; BT014871; AAT41854.1; -; mRNA.
DR   PIR; A96499; A96499.
DR   RefSeq; NP_175021.2; NM_103481.4.
DR   AlphaFoldDB; Q8L7S9; -.
DR   SMR; Q8L7S9; -.
DR   IntAct; Q8L7S9; 72.
DR   STRING; 3702.AT1G43560.1; -.
DR   PaxDb; Q8L7S9; -.
DR   PRIDE; Q8L7S9; -.
DR   ProteomicsDB; 232349; -.
DR   EnsemblPlants; AT1G43560.1; AT1G43560.1; AT1G43560.
DR   GeneID; 840939; -.
DR   Gramene; AT1G43560.1; AT1G43560.1; AT1G43560.
DR   KEGG; ath:AT1G43560; -.
DR   Araport; AT1G43560; -.
DR   TAIR; locus:2194661; AT1G43560.
DR   eggNOG; KOG0910; Eukaryota.
DR   HOGENOM; CLU_090389_0_3_1; -.
DR   InParanoid; Q8L7S9; -.
DR   OMA; CQLMVPI; -.
DR   OrthoDB; 1482186at2759; -.
DR   PhylomeDB; Q8L7S9; -.
DR   PRO; PR:Q8L7S9; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8L7S9; baseline and differential.
DR   Genevisible; Q8L7S9; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR   GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0008047; F:enzyme activator activity; IDA:UniProtKB.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IDA:UniProtKB.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   GO; GO:0043085; P:positive regulation of catalytic activity; IDA:UniProtKB.
DR   GO; GO:0009416; P:response to light stimulus; IEP:UniProtKB.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR01068; thioredoxin; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Disulfide bond; Electron transport; Plastid;
KW   Redox-active center; Reference proteome; Transit peptide; Transport.
FT   TRANSIT         1..58
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           59..167
FT                   /note="Thioredoxin Y2, chloroplastic"
FT                   /id="PRO_0000394540"
FT   DOMAIN          59..164
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        88
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        91
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            82
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000250"
FT   SITE            89
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            90
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   DISULFID        88..91
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   167 AA;  18592 MW;  B8E58A7844505A07 CRC64;
     MAISLATAYI SPCFTPESSN SASPSRTLSS VRLPSQIRRF GSVQSPSSST RFAPLTVRAA
     KKQTFNSFDD LLQNSDKPVL VDFYATWCGP CQLMVPILNE VSETLKDIIA VVKIDTEKYP
     SLANKYQIEA LPTFILFKDG KLWDRFEGAL PANQLVERIE NSLQVKQ
 
 
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