TRXM5_ORYSJ
ID TRXM5_ORYSJ Reviewed; 172 AA.
AC Q9ZP20; A0A0P0Y7N8; B7E6Q6; Q2QWN9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Thioredoxin M5, chloroplastic;
DE Short=OsTrxm5;
DE Flags: Precursor;
GN Name=TRXM; OrderedLocusNames=Os12g0188700, LOC_Os12g08730;
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 [MRNA].
RA Dyer T.A., Catley M.A., Robertson E.J., Dunford R.P.;
RT "The thioredoxins m and f of plants and their role in the redox regulation
RT of chloroplast enxymes.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=18723667; DOI=10.1104/pp.108.123547;
RA Chi Y.H., Moon J.C., Park J.H., Kim H.S., Zulfugarov I.S., Fanata W.I.,
RA Jang H.H., Lee J.R., Lee Y.M., Kim S.T., Chung Y.Y., Lim C.O., Kim J.Y.,
RA Yun D.J., Lee C.H., Lee K.O., Lee S.Y.;
RT "Abnormal chloroplast development and growth inhibition in rice thioredoxin
RT m knock-down plants.";
RL Plant Physiol. 148:808-817(2008).
RN [8]
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 probably involved in the redox
CC regulation of chloroplastic enzymes. Required for chloroplast
CC biogenesis and differentiation. Functions as an electron donor for
CC plastidial 2-Cys peroxiredoxins and participates in hydrogen peroxide
CC scavenging system in chloroplasts. Possesses reducing activity towards
CC insulin disulfide bonds. {ECO:0000269|PubMed:18723667}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:18723667}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and at lower levels in flowers.
CC {ECO:0000269|PubMed:18723667}.
CC -!- INDUCTION: By de-etiolation. {ECO:0000269|PubMed:18723667}.
CC -!- DISRUPTION PHENOTYPE: Semi-dwarf plants with pale-green leaves,
CC abnormal chloroplasts, reduced carotenoid and chlorophyll content and
CC increased hydrogen peroxide levels. {ECO:0000269|PubMed:18723667}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. Plant M-type subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ005841; CAA06736.1; -; mRNA.
DR EMBL; DP000011; ABA96018.2; -; Genomic_DNA.
DR EMBL; AP008218; BAH95554.1; -; Genomic_DNA.
DR EMBL; AP014968; BAT16187.1; -; Genomic_DNA.
DR EMBL; AK061678; BAG88053.1; -; mRNA.
DR RefSeq; XP_015620324.1; XM_015764838.1.
DR AlphaFoldDB; Q9ZP20; -.
DR SMR; Q9ZP20; -.
DR STRING; 4530.OS12T0188700-02; -.
DR PaxDb; Q9ZP20; -.
DR PRIDE; Q9ZP20; -.
DR EnsemblPlants; Os12t0188700-02; Os12t0188700-02; Os12g0188700.
DR GeneID; 9270622; -.
DR Gramene; Os12t0188700-02; Os12t0188700-02; Os12g0188700.
DR KEGG; osa:9270622; -.
DR eggNOG; KOG0910; Eukaryota.
DR HOGENOM; CLU_090389_0_2_1; -.
DR InParanoid; Q9ZP20; -.
DR OMA; CSIGAKS; -.
DR OrthoDB; 1482186at2759; -.
DR Proteomes; UP000000763; Chromosome 12.
DR Proteomes; UP000059680; Chromosome 12.
DR ExpressionAtlas; Q9ZP20; baseline and differential.
DR Genevisible; Q9ZP20; OS.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
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 GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IMP:UniProtKB.
DR GO; GO:0009657; P:plastid organization; IMP: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..59
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 60..172
FT /note="Thioredoxin M5, chloroplastic"
FT /id="PRO_0000034176"
FT DOMAIN 60..171
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 17..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 95
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 98
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 96
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 97
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT DISULFID 95..98
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 172 AA; 18529 MW; B421134F94A2AA3A CRC64;
MALETCFRAW ATLHAPQPPS SGGSRDRLLL SGAGSSQSKP RLSVASPSPL RPASRFACQC
SNVVDEVVVA DEKNWDSMVL GSEAPVLVEF WAPWCGPCRM IAPVIDELAK EYVGKIKCCK
VNTDDSPNIA TNYGIRSIPT VLMFKNGEKK ESVIGAVPKT TLATIIDKYV SS
