MDAR4_ORYSJ
ID MDAR4_ORYSJ Reviewed; 435 AA.
AC Q6ZJ08; Q9SXX0;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Monodehydroascorbate reductase 4, cytosolic {ECO:0000305};
DE Short=OsMADR4 {ECO:0000303|PubMed:25546583};
DE Short=OsMDHAR4 {ECO:0000303|PubMed:25546583};
DE EC=1.6.5.4 {ECO:0000250|UniProtKB:Q652L6};
GN Name=MDAR4 {ECO:0000303|PubMed:25546583};
GN Synonyms=MDHAR4 {ECO:0000303|PubMed:25546583};
GN OrderedLocusNames=Os08g0557600 {ECO:0000312|EMBL:BAF24400.1},
GN LOC_Os08g44340 {ECO:0000305};
GN ORFNames=OJ1150_A11.25 {ECO:0000312|EMBL:BAD09086.1};
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=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 [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-398.
RA Kaminaka H., Morita S., Tokumoto M., Masumura T., Tanaka K.;
RT "Cloning and characterization of two cDNAs for cytosolic
RT monodehydroascorbate reductase in rice.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY, AND INDUCTION BY
RP COLD.
RX PubMed=16263700; DOI=10.1074/mcp.m500242-mcp200;
RA Imin N., Kerim T., Weinman J.J., Rolfe B.G.;
RT "Low temperature treatment at the young microspore stage induces protein
RT changes in rice anthers.";
RL Mol. Cell. Proteomics 5:274-292(2006).
RN [7]
RP INDUCTION BY SENESCENCE.
RX PubMed=25546583; DOI=10.1016/j.jplph.2014.09.020;
RA Li Z., Su D., Lei B., Wang F., Geng W., Pan G., Cheng F.;
RT "Transcriptional profile of genes involved in ascorbate glutathione cycle
RT in senescing leaves for an early senescence leaf (esl) rice mutant.";
RL J. Plant Physiol. 176:1-15(2015).
CC -!- FUNCTION: Catalyzes the conversion of monodehydroascorbate to
CC ascorbate, oxidizing NADH in the process. Ascorbate is a major
CC antioxidant against reactive oxygen species (ROS) and nitric oxide
CC (NO). {ECO:0000250|UniProtKB:Q652L6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + 2 monodehydro-L-ascorbate radical + NADH = 2 L-
CC ascorbate + NAD(+); Xref=Rhea:RHEA:14581, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:59513; EC=1.6.5.4;
CC Evidence={ECO:0000250|UniProtKB:Q652L6};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q652L6};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in anthers.
CC {ECO:0000269|PubMed:16263700}.
CC -!- INDUCTION: Induced by cold stress (PubMed:16263700). Induced during
CC senescence (PubMed:25546583). {ECO:0000269|PubMed:16263700,
CC ECO:0000269|PubMed:25546583}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; AP003928; BAD09086.1; -; Genomic_DNA.
DR EMBL; AP008214; BAF24400.1; -; Genomic_DNA.
DR EMBL; AP014964; BAT06666.1; -; Genomic_DNA.
DR EMBL; AK102459; BAG95564.1; -; mRNA.
DR EMBL; AB026731; BAA77282.1; -; mRNA.
DR RefSeq; XP_015649937.1; XM_015794451.1.
DR AlphaFoldDB; Q6ZJ08; -.
DR SMR; Q6ZJ08; -.
DR STRING; 4530.OS08T0557600-01; -.
DR PaxDb; Q6ZJ08; -.
DR PRIDE; Q6ZJ08; -.
DR EnsemblPlants; Os08t0557600-01; Os08t0557600-01; Os08g0557600.
DR GeneID; 4346299; -.
DR Gramene; Os08t0557600-01; Os08t0557600-01; Os08g0557600.
DR KEGG; osa:4346299; -.
DR eggNOG; KOG1336; Eukaryota.
DR HOGENOM; CLU_003291_4_1_1; -.
DR InParanoid; Q6ZJ08; -.
DR OMA; IHHFWTF; -.
DR OrthoDB; 405030at2759; -.
DR Proteomes; UP000000763; Chromosome 8.
DR Proteomes; UP000059680; Chromosome 8.
DR ExpressionAtlas; Q6ZJ08; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016656; F:monodehydroascorbate reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IBA:GO_Central.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 2.
DR SUPFAM; SSF55424; SSF55424; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; FAD; Flavoprotein; NAD; NADP; Oxidoreductase;
KW Redox-active center; Reference proteome.
FT CHAIN 1..435
FT /note="Monodehydroascorbate reductase 4, cytosolic"
FT /id="PRO_0000442022"
FT BINDING 14..17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 41
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 48
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 53
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 96
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 147..148
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 172..178
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 174..178
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 196
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 202
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 202
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 261
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 261
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 298
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 314..315
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 314..315
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 316
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 320
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 349
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 349
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 349
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 351
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT CONFLICT 125
FT /note="S -> F (in Ref. 5; BAA77282)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 435 AA; 46685 MW; 6080EF22D770F4C4 CRC64;
MAAAKHFTYV ILGGGVAAGY AAREFAKQGV KPGELAIISK ESVAPYERPA LSKGYLFPQN
AARLPGFHTC VGSGGERLLP EWYSEKGIEL ILSTEIVKAD LASKTLTSSA DATFTYDTLL
IATGSSVIKL TDFGVQGAEA NDILYLRDIE DADKLVAAMQ AKKDGKAVIV GGGYIGLELS
AALKTNNFDV TMVYPEPWCM PRLFTSGLAA FYEGYYANKG IHIIKGTVAV GFDADANGDV
TAVKLKNGNV LEADIVIVGV GGRPLTHLFK GQVAEEKGGI KTDAFFETSV PGVYAIADVA
AFPMKLYNEI RRVEHVDHAR KSAEQAVKAI KAKEAGESVP EYDYLPYFYS RSFDLSWQFY
GDNVGEDVLF GDNDPTAAKP KFGSYWIKDG KVVGVFLEGG SAEENQVIAK VARAQPPVAD
VEALKKEGLD FAAKV
