HSD1A_ARATH
ID HSD1A_ARATH Reviewed; 349 AA.
AC P0DKC5; Q9LUF1;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=11-beta-hydroxysteroid dehydrogenase 1A;
DE EC=1.1.1.146 {ECO:0000269|PubMed:17074428};
DE AltName: Full=17-beta-hydroxysteroid dehydrogenase 1A;
DE EC=1.1.1.-;
DE AltName: Full=Hydroxysteroid dehydrogenase 1;
DE Short=AtHSD1;
GN Name=HSD1; OrderedLocusNames=At5g50600; ORFNames=MBA10.16;
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=15246063; DOI=10.1016/j.plaphy.2004.04.006;
RA Jolivet P., Roux E., D'Andrea S., Davanture M., Negroni L., Zivy M.,
RA Chardot T.;
RT "Protein composition of oil bodies in Arabidopsis thaliana ecotype WS.";
RL Plant Physiol. Biochem. 42:501-509(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=17074428; DOI=10.1016/j.biochi.2006.09.013;
RA d'Andrea S., Canonge M., Beopoulos A., Jolivet P., Hartmann M.A.,
RA Miquel M., Lepiniec L., Chardot T.;
RT "At5g50600 encodes a member of the short-chain dehydrogenase reductase
RT superfamily with 11beta- and 17beta-hydroxysteroid dehydrogenase activities
RT associated with Arabidopsis thaliana seed oil bodies.";
RL Biochimie 89:222-229(2007).
RN [7]
RP GENE FAMILY, DISRUPTION PHENOTYPE, FUNCTION, INDUCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=17616511; DOI=10.1104/pp.107.100560;
RA Li F., Asami T., Wu X., Tsang E.W., Cutler A.J.;
RT "A putative hydroxysteroid dehydrogenase involved in regulating plant
RT growth and development.";
RL Plant Physiol. 145:87-97(2007).
RN [8]
RP GENE FAMILY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION,
RP INDUCTION BY LEC2, AND FUNCTION.
RX PubMed=19542545; DOI=10.1093/pcp/pcp092;
RA Baud S., Dichow N.R., Kelemen Z., d'Andrea S., To A., Berger N.,
RA Canonge M., Kronenberger J., Viterbo D., Dubreucq B., Lepiniec L.,
RA Chardot T., Miquel M.;
RT "Regulation of HSD1 in seeds of Arabidopsis thaliana.";
RL Plant Cell Physiol. 50:1463-1478(2009).
CC -!- FUNCTION: Catalyzes 11-beta, 17-beta-hydroxysteroid and reduces 17-
CC beta-ketosteroids. Involved in regulating plant growth and development,
CC probably promoting or mediating brassinosteroid effects. Plays a role
CC during seed maturation. {ECO:0000269|PubMed:17074428,
CC ECO:0000269|PubMed:17616511, ECO:0000269|PubMed:19542545}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an 11beta-hydroxysteroid + NADP(+) = an 11-oxosteroid + H(+) +
CC NADPH; Xref=Rhea:RHEA:11388, ChEBI:CHEBI:15378, ChEBI:CHEBI:35346,
CC ChEBI:CHEBI:47787, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.146; Evidence={ECO:0000269|PubMed:17074428};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11389;
CC Evidence={ECO:0000269|PubMed:17074428};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol + NADP(+) = estrone + H(+) + NADPH;
CC Xref=Rhea:RHEA:24616, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469,
CC ChEBI:CHEBI:17263, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:17074428};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24617;
CC Evidence={ECO:0000269|PubMed:17074428};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=corticosterone + NADP(+) = 11-dehydrocorticosterone + H(+) +
CC NADPH; Xref=Rhea:RHEA:42200, ChEBI:CHEBI:15378, ChEBI:CHEBI:16827,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78600;
CC Evidence={ECO:0000269|PubMed:17074428};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42201;
CC Evidence={ECO:0000269|PubMed:17074428};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cortisone + H(+) + NADPH = cortisol + NADP(+);
CC Xref=Rhea:RHEA:68616, ChEBI:CHEBI:15378, ChEBI:CHEBI:16962,
CC ChEBI:CHEBI:17650, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000269|PubMed:17074428};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68617;
CC Evidence={ECO:0000269|PubMed:17074428};
CC -!- SUBCELLULAR LOCATION: Lipid droplet. Membrane; Single-pass type II
CC membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in the above-ground part of seedlings,
CC especially in the vascular tissues. Also detected in the buds and
CC silique pedicels. Highly induced in oil-accumulating tissues of
CC maturing seeds. {ECO:0000269|PubMed:17616511,
CC ECO:0000269|PubMed:19542545}.
CC -!- DEVELOPMENTAL STAGE: Firstly detected during early seed maturation, at
CC 9 days after anthesis (DAA), peaking at 18 DAA, before falling sharply
CC during late maturation. {ECO:0000269|PubMed:19542545}.
CC -!- INDUCTION: By brassinosteroids (BRs). Up-regulated by LEC2.
CC {ECO:0000269|PubMed:17616511, ECO:0000269|PubMed:19542545}.
CC -!- DISRUPTION PHENOTYPE: Semidwarf phenotype with reduced sensitivity to
CC brassinosteroids (BRs) and enhanced sensitivity to abscisic acid (ABA)
CC during germination. {ECO:0000269|PubMed:17616511}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AB025619; BAB09145.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95967.1; -; Genomic_DNA.
DR EMBL; AF446888; AAL38621.1; -; mRNA.
DR EMBL; AY052660; AAK96564.1; -; mRNA.
DR EMBL; AY062768; AAL32846.1; -; mRNA.
DR EMBL; AY081653; AAM10215.1; -; mRNA.
DR EMBL; AK221698; BAD95411.1; -; mRNA.
DR RefSeq; NP_568742.1; NM_124448.5.
DR RefSeq; NP_680418.1; NM_148113.3.
DR AlphaFoldDB; P0DKC5; -.
DR SMR; P0DKC5; -.
DR BioGRID; 20375; 2.
DR BioGRID; 20387; 1.
DR STRING; 3702.AT5G50600.1; -.
DR iPTMnet; P0DKC5; -.
DR PaxDb; P0DKC5; -.
DR PRIDE; P0DKC5; -.
DR ProteomicsDB; 228810; -.
DR EnsemblPlants; AT5G50600.1; AT5G50600.1; AT5G50600.
DR EnsemblPlants; AT5G50700.1; AT5G50700.1; AT5G50700.
DR GeneID; 835129; -.
DR GeneID; 835141; -.
DR Gramene; AT5G50600.1; AT5G50600.1; AT5G50600.
DR Gramene; AT5G50700.1; AT5G50700.1; AT5G50700.
DR KEGG; ath:AT5G50600; -.
DR KEGG; ath:AT5G50700; -.
DR Araport; AT5G50600; -.
DR eggNOG; KOG1205; Eukaryota.
DR HOGENOM; CLU_010194_2_1_1; -.
DR InParanoid; P0DKC5; -.
DR OMA; CWEVDVT; -.
DR OrthoDB; 906746at2759; -.
DR PhylomeDB; P0DKC5; -.
DR BioCyc; MetaCyc:AT5G50600-MON; -.
DR PRO; PR:P0DKC5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P0DKC5; baseline and differential.
DR Genevisible; P0DKC5; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0070524; F:11-beta-hydroxysteroid dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR GO; GO:0072582; F:17-beta-hydroxysteroid dehydrogenase (NADP+) activity; IBA:GO_Central.
DR GO; GO:0102196; F:cortisol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008202; P:steroid metabolic process; IBA:GO_Central.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 1: Evidence at protein level;
KW Lipid biosynthesis; Lipid droplet; Lipid metabolism; Membrane; NADP;
KW Oxidoreductase; Reference proteome; Signal-anchor; Steroid biosynthesis;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..349
FT /note="11-beta-hydroxysteroid dehydrogenase 1A"
FT /id="PRO_0000422278"
FT TRANSMEM 10..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT ACT_SITE 197
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 54..80
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 197..201
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 349 AA; 39087 MW; 60447F99A6B60323 CRC64;
MELINDFLNL TAPFFTFFGL CFFLPPFYFF KFLQSIFSTI FSENLYGKVV LITGASSGIG
EQLAYEYACR GACLALTARR KNRLEEVAEI ARELGSPNVV TVHADVSKPD DCRRIVDDTI
THFGRLDHLV NNAGMTQISM FENIEDITRT KAVLDTNFWG SVYTTRAALP YLRQSNGKIV
AMSSSAAWLT APRMSFYNAS KAALLSFFET MRIELGGDVH ITIVTPGYIE SELTQGKYFS
GEGELIVNQD MRDVQVGPFP VASASGCAKS IVNGVCRKQR YVTEPSWFKV TYLWKVLCPE
LIEWGCRLLY MTGTGMSEDT ALNKRIMDIP GVRSTLYPES IRTPEIKSD
