SDR3A_ARATH
ID SDR3A_ARATH Reviewed; 257 AA.
AC O80713;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Short-chain dehydrogenase reductase 3a;
DE Short=AtSDR3a;
DE EC=1.1.1.-;
GN Name=SDR3a; Synonyms=SDR3, SDR4; OrderedLocusNames=At2g47130;
GN ORFNames=F14M4;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12417697; DOI=10.1105/tpc.006494;
RA Cheng W.-H., Endo A., Zhou L., Penney J., Chen H.-C., Arroyo A., Leon P.,
RA Nambara E., Asami T., Seo M., Koshiba T., Sheen J.;
RT "A unique short-chain dehydrogenase/reductase in Arabidopsis glucose
RT signaling and abscisic acid biosynthesis and functions.";
RL Plant Cell 14:2723-2743(2002).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION BY
RP PSEUDOMONAS SYRINGAE.
RX PubMed=22153241; DOI=10.1016/j.plaphy.2011.10.013;
RA Hwang S.-G., Lin N.-C., Hsiao Y.-Y., Kuo C.-H., Chang P.-F., Deng W.-L.,
RA Chiang M.-H., Shen H.-L., Chen C.-Y., Cheng W.-H.;
RT "The Arabidopsis short-chain dehydrogenase/reductase 3, an abscisic acid
RT deficient 2 homolog, is involved in plant defense responses but not in ABA
RT biosynthesis.";
RL Plant Physiol. Biochem. 51:63-73(2012).
CC -!- FUNCTION: Confers resistance to the incompatible pathogenic bacteria
CC P.syringae pv. tomato DC3000 in a PR1-dependent manner. Seems not
CC involved in abscisic acid (ABA) biosynthesis.
CC {ECO:0000269|PubMed:22153241}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the radicle tip, lateral root
CC primordia and tips, and the area surrounding the cotyledon hydathode of
CC young seedlings. {ECO:0000269|PubMed:22153241}.
CC -!- INDUCTION: Accumulates upon Pseudomonas syringae infection and after
CC treatment with systemic acquired resistance (SAR)-inducing chemicals,
CC 1,2-benzisothiazol-3(2H)-one1,1-dioxide (BIT) and benzo-
CC (1,2,3)thiadiazole-7-carbothioic acid S-methyl ester (BTH).
CC {ECO:0000269|PubMed:22153241}.
CC -!- DISRUPTION PHENOTYPE: No phenotype regarding abiotic stresses. Enhanced
CC susceptibility to the incompatible pathogenic bacteria Pseudomonas
CC syringae pv. tomato DC3000. {ECO:0000269|PubMed:22153241}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AC004411; AAC34217.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10805.1; -; Genomic_DNA.
DR EMBL; BT010410; AAQ62411.1; -; mRNA.
DR EMBL; AK175374; BAD43137.1; -; mRNA.
DR PIR; T02175; T02175.
DR RefSeq; NP_182235.1; NM_130281.5.
DR AlphaFoldDB; O80713; -.
DR SMR; O80713; -.
DR BioGRID; 4661; 2.
DR IntAct; O80713; 1.
DR STRING; 3702.AT2G47130.1; -.
DR PaxDb; O80713; -.
DR PRIDE; O80713; -.
DR ProteomicsDB; 232953; -.
DR EnsemblPlants; AT2G47130.1; AT2G47130.1; AT2G47130.
DR GeneID; 819326; -.
DR Gramene; AT2G47130.1; AT2G47130.1; AT2G47130.
DR KEGG; ath:AT2G47130; -.
DR Araport; AT2G47130; -.
DR TAIR; locus:2041439; AT2G47130.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_1_0_1; -.
DR OMA; NAGIFMM; -.
DR OrthoDB; 1373099at2759; -.
DR PhylomeDB; O80713; -.
DR BioCyc; ARA:AT2G47130-MON; -.
DR PRO; PR:O80713; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80713; baseline and differential.
DR Genevisible; O80713; AT.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0009626; P:plant-type hypersensitive response; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW Hypersensitive response; Oxidoreductase; Plant defense; Reference proteome.
FT CHAIN 1..257
FT /note="Short-chain dehydrogenase reductase 3a"
FT /id="PRO_0000419511"
FT ACT_SITE 157
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 12..36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 257 AA; 26901 MW; F2853B98034728A8 CRC64;
MSGLRLDGKI AIITGGASGI GAEAVRLFTD HGAKVVIVDF QEELGQNVAV SVGKDKASFY
RCDVTNEKEV ENAVKFTVEK YGKLDVLFSN AGVMEQPGSF LDLNLEQFDR TMAVNVRGAA
AFIKHAARAM VEKGTRGSIV CTTSVASEIG GPGPHAYTAS KHALLGLVKS ACGGLGKYGI
RVNGVAPYAV ATAINSRDEE TVRMVEEYSA ATGILKGVVL KARHVAEAAL FLASDDSAYV
SGQNLAVDGG YSVVKPI
