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TRXX_ORYSJ
ID   TRXX_ORYSJ              Reviewed;         180 AA.
AC   Q7XKD0; A0A0P0WGM0; Q2MCJ3;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Thioredoxin X, chloroplastic;
DE            Short=OsTrxx;
DE   AltName: Full=OsTrx16;
DE   Flags: Precursor;
GN   Name=TRX-X; OrderedLocusNames=Os04g0676100, LOC_Os04g57930;
GN   ORFNames=OSJNBa0064G10.1;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447439; DOI=10.1038/nature01183;
RA   Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA   Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA   Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA   Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA   Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA   Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA   Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA   Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA   Li J., Hong G., Xue Y., Han B.;
RT   "Sequence and analysis of rice chromosome 4.";
RL   Nature 420:316-320(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RG   The rice full-length cDNA consortium;
RT   "Oryza sativa full length cDNA.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 66-180, AND FUNCTION.
RC   TISSUE=Leaf;
RX   PubMed=16891402; DOI=10.1105/tpc.106.041541;
RA   Perez-Ruiz J.M., Spinola M.C., Kirchsteiger K., Moreno J., Sahrawy M.,
RA   Cejudo F.J.;
RT   "Rice NTRC is a high-efficiency redox system for chloroplast protection
RT   against oxidative damage.";
RL   Plant Cell 18:2356-2368(2006).
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: Thiol-disulfide oxidoreductase that may participate in
CC       various redox reactions. Possesses insulin disulfide bonds reducing
CC       activity. {ECO:0000269|PubMed:16891402}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR   EMBL; AL606668; CAE05750.1; -; Genomic_DNA.
DR   EMBL; AP008210; BAF16167.1; -; Genomic_DNA.
DR   EMBL; AP014960; BAS91621.1; -; Genomic_DNA.
DR   EMBL; AK288094; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AM183298; CAJ66078.1; -; mRNA.
DR   RefSeq; XP_015636655.1; XM_015781169.1.
DR   AlphaFoldDB; Q7XKD0; -.
DR   SMR; Q7XKD0; -.
DR   IntAct; Q7XKD0; 2.
DR   MINT; Q7XKD0; -.
DR   STRING; 4530.OS04T0676100-01; -.
DR   PaxDb; Q7XKD0; -.
DR   PRIDE; Q7XKD0; -.
DR   EnsemblPlants; Os04t0676100-01; Os04t0676100-01; Os04g0676100.
DR   GeneID; 4337394; -.
DR   Gramene; Os04t0676100-01; Os04t0676100-01; Os04g0676100.
DR   KEGG; osa:4337394; -.
DR   eggNOG; KOG0910; Eukaryota.
DR   HOGENOM; CLU_090389_0_3_1; -.
DR   InParanoid; Q7XKD0; -.
DR   OMA; ASTIRCG; -.
DR   OrthoDB; 1482186at2759; -.
DR   Proteomes; UP000000763; Chromosome 4.
DR   Proteomes; UP000059680; Chromosome 4.
DR   Genevisible; Q7XKD0; OS.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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   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   Chloroplast; Disulfide bond; Electron transport; Plastid;
KW   Redox-active center; Reference proteome; Transit peptide; Transport.
FT   TRANSIT         1..64
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           65..180
FT                   /note="Thioredoxin X, chloroplastic"
FT                   /id="PRO_0000394835"
FT   DOMAIN          65..175
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   ACT_SITE        97
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        100
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            91
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000250"
FT   SITE            98
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   SITE            99
FT                   /note="Contributes to redox potential value"
FT                   /evidence="ECO:0000250"
FT   DISULFID        97..100
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   CONFLICT        50
FT                   /note="A -> T (in Ref. 5; AK288094)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   180 AA;  19121 MW;  CAD7FCD5AC2D33D3 CRC64;
     MASAPSTTAS GLAPPPFSSA RGARLLPGAL LRLPPPPASV GSFRVVGPAA APPGGRRIAS
     ARVRCGAAVR FIGQSEFEAE VLQSDLPVLV DFVADWCGPC RLIAPVVDWA AEEYEGRLKI
     VKIDHDANPQ LIEEYKVYGL PSLILFKDGK EVPGSRREGA ITKAKFKEYL EPLLSTSTVA
 
 
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