MDAR2_ORYSJ
ID MDAR2_ORYSJ Reviewed; 476 AA.
AC Q8S3R2;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Monodehydroascorbate reductase 2, peroxisomal {ECO:0000305};
DE Short=OsMDAR2 {ECO:0000303|PubMed:25546583};
DE Short=OsMDHAR2 {ECO:0000303|PubMed:25546583};
DE EC=1.6.5.4 {ECO:0000250|UniProtKB:Q652L6};
GN Name=MDAR2 {ECO:0000303|PubMed:25546583};
GN Synonyms=MDHAR2 {ECO:0000303|PubMed:25546583};
GN OrderedLocusNames=Os02g0707100 {ECO:0000312|EMBL:BAF09789.1},
GN LOC_Os02g47800 {ECO:0000305};
GN ORFNames=49D11.20a {ECO:0000312|EMBL:AAL87166.1},
GN OsJ_35954 {ECO:0000312|EMBL:EAZ20346.1},
GN P0680A05.39 {ECO:0000312|EMBL:BAD08054.1};
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 [GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15232225;
RA Park Y.-J., Dixit A., Yoo J.-W., Bennetzen J.;
RT "Further evidence of microcolinearity between barley and rice genomes at
RT two orthologous regions.";
RL Mol. Cells 17:492-502(2004).
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 GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
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 INDUCTION.
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: Peroxisome membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- INDUCTION: Down-regulated during senescence.
CC {ECO:0000269|PubMed:25546583}.
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; AF480496; AAL87166.1; -; Genomic_DNA.
DR EMBL; AP005323; BAD08054.1; -; Genomic_DNA.
DR EMBL; AP005844; BAD08098.1; -; Genomic_DNA.
DR EMBL; AP008208; BAF09789.1; -; Genomic_DNA.
DR EMBL; AP014958; BAS80528.1; -; Genomic_DNA.
DR EMBL; CM000149; EAZ20346.1; -; Genomic_DNA.
DR EMBL; AK065585; BAG89572.1; -; mRNA.
DR RefSeq; XP_015627040.1; XM_015771554.1.
DR AlphaFoldDB; Q8S3R2; -.
DR SMR; Q8S3R2; -.
DR STRING; 4530.OS02T0707100-01; -.
DR PaxDb; Q8S3R2; -.
DR PRIDE; Q8S3R2; -.
DR EnsemblPlants; Os02t0707100-01; Os02t0707100-01; Os02g0707100.
DR GeneID; 4330469; -.
DR Gramene; Os02t0707100-01; Os02t0707100-01; Os02g0707100.
DR KEGG; osa:4330469; -.
DR eggNOG; KOG1336; Eukaryota.
DR HOGENOM; CLU_003291_4_1_1; -.
DR InParanoid; Q8S3R2; -.
DR OMA; AWTVCWL; -.
DR OrthoDB; 405030at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 12.
DR Proteomes; UP000059680; Chromosome 2.
DR ExpressionAtlas; Q8S3R2; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
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 2: Evidence at transcript level;
KW FAD; Flavoprotein; Membrane; NAD; NADP; Oxidoreductase; Peroxisome;
KW Redox-active center; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..476
FT /note="Monodehydroascorbate reductase 2, peroxisomal"
FT /id="PRO_0000442020"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..447
FT /note="Peroxisomal"
FT /evidence="ECO:0000305"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..476
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT BINDING 12..15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 40
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 47
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 52
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 146..147
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 171..177
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 173..177
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 195
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 201
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 201
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 260
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 260
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 297
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 346
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 346
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 346
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
FT BINDING 348
FT /ligand="L-ascorbate"
FT /ligand_id="ChEBI:CHEBI:38290"
FT /evidence="ECO:0000250|UniProtKB:Q652L6"
SQ SEQUENCE 476 AA; 51864 MW; FF17CBDB72C0E873 CRC64;
MGRAFVHVIL GGGVAAGYAA LEFARRGGYS RGELCIISEE TVAPYERPAL SKGYLLPEGA
ARLPGFHTCV GANDELLTAK WYKENGIELV LGTKVITADV RMKTLLTATG ETISYKNLII
ATGARALKLE EFGISGSDAS NICYLRNLDD ADKLVNVMKS CPGGNAVVIG GGYIGMECAA
ALVTNRIKVT MVFPESHCMA RLFTPKIAEY YENYYTSKGV TFVKGTVLTS FEKDSTGKVT
SVILKDGKHL PADMVVVGIG IRASTGLFEG QLLMEQGGIK VNGQMLTSDG SVYAVGDVAA
FPIKLFDGVI RRLEHVDSAR RTARHAVAAI LEPSKTKDID YLPFFYSRVF TLSWQFYGNN
TGEVVHFGDF TNSSPRFGAY WVDKSRIRGA FLEGGSREEY EAISNVVRRK AKVINIAELE
KQGLMFAIQE SQKDLPDGGL ALGEKPTYVW HATAGVIAAA SIAAFGYWYG RKRRRW
