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HSD4A_ARATH
ID   HSD4A_ARATH             Reviewed;         299 AA.
AC   P0DKC7; Q9FGP2;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2013, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=11-beta-hydroxysteroid dehydrogenase-like 4A;
DE            EC=1.1.1.-;
DE   AltName: Full=17-beta-hydroxysteroid dehydrogenase-like 4A;
DE            EC=1.1.1.-;
DE   AltName: Full=Hydroxysteroid dehydrogenase 4;
DE            Short=AtHSD4;
GN   Name=HSD4; OrderedLocusNames=At5g50590; ORFNames=MBA10.15;
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;
RA   Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA   Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   GENE FAMILY.
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   [6]
RP   GENE FAMILY.
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000305}.
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DR   EMBL; AB025619; BAB09144.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95966.1; -; Genomic_DNA.
DR   EMBL; DQ056713; AAY78859.1; -; mRNA.
DR   EMBL; BT026066; ABG48422.1; -; mRNA.
DR   RefSeq; NP_199871.1; NM_124447.2.
DR   RefSeq; NP_680417.1; NM_148112.2.
DR   AlphaFoldDB; P0DKC7; -.
DR   SMR; P0DKC7; -.
DR   BioGRID; 20374; 1.
DR   BioGRID; 20386; 1.
DR   STRING; 3702.AT5G50590.1; -.
DR   PaxDb; P0DKC7; -.
DR   PRIDE; P0DKC7; -.
DR   EnsemblPlants; AT5G50590.1; AT5G50590.1; AT5G50590.
DR   EnsemblPlants; AT5G50690.1; AT5G50690.1; AT5G50690.
DR   GeneID; 835128; -.
DR   GeneID; 835140; -.
DR   Gramene; AT5G50590.1; AT5G50590.1; AT5G50590.
DR   Gramene; AT5G50690.1; AT5G50690.1; AT5G50690.
DR   KEGG; ath:AT5G50590; -.
DR   KEGG; ath:AT5G50690; -.
DR   Araport; AT5G50590; -.
DR   eggNOG; KOG1205; Eukaryota.
DR   HOGENOM; CLU_010194_2_1_1; -.
DR   InParanoid; P0DKC7; -.
DR   OrthoDB; 906746at2759; -.
DR   PhylomeDB; P0DKC7; -.
DR   PRO; PR:P0DKC7; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   Genevisible; P0DKC7; 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:0072582; F:17-beta-hydroxysteroid dehydrogenase (NADP+) activity; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Lipid biosynthesis; Lipid metabolism; Membrane; NADP; Oxidoreductase;
KW   Reference proteome; Signal-anchor; Steroid biosynthesis; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..299
FT                   /note="11-beta-hydroxysteroid dehydrogenase-like 4A"
FT                   /id="PRO_0000422282"
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   299 AA;  33248 MW;  77F6AC14AD01DD9D CRC64;
     MDLNNKIFNI LLPIVTVSFL LVFMPFSIFF KLLQFIRGCK ESEKVNGKVV IITGSSSGIG
     EHLAYEYARR GAYLTLVARR EDRLQVVADR CRKLGSPDVA VVRGDVSVIK DCKRFVQETI
     SRFGRLDHLV NNAGIAEAKF FEDYSEISDV LPIVNTNFWG PVYATHFAIP HLKKTKGKII
     AVASPAGWSG VPRMSIYAAS KAAMINFYET LRIELHPEVG VTIVFPGLIE NGNTNPDLLA
     EKQDWSQVVT IESAAECAKA VVNGICRGKT FVAEPSWVRV LFWLSAICPE LLISKPKRN
 
 
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