HSD3_ARATH
ID HSD3_ARATH Reviewed; 309 AA.
AC Q9STY7;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=11-beta-hydroxysteroid dehydrogenase-like 3;
DE EC=1.1.1.-;
DE AltName: Full=17-beta-hydroxysteroid dehydrogenase-like 3;
DE EC=1.1.1.-;
DE AltName: Full=Hydroxysteroid dehydrogenase 3;
DE Short=AtHSD3;
GN Name=HSD3; OrderedLocusNames=At3g47360; ORFNames=T21L8.110;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 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 [4]
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; AL096860; CAB51208.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78270.1; -; Genomic_DNA.
DR PIR; T12991; T12991.
DR RefSeq; NP_190320.1; NM_114604.2.
DR AlphaFoldDB; Q9STY7; -.
DR SMR; Q9STY7; -.
DR STRING; 3702.AT3G47360.1; -.
DR PaxDb; Q9STY7; -.
DR PRIDE; Q9STY7; -.
DR ProteomicsDB; 232108; -.
DR EnsemblPlants; AT3G47360.1; AT3G47360.1; AT3G47360.
DR GeneID; 823890; -.
DR Gramene; AT3G47360.1; AT3G47360.1; AT3G47360.
DR KEGG; ath:AT3G47360; -.
DR Araport; AT3G47360; -.
DR TAIR; locus:2099515; AT3G47360.
DR eggNOG; KOG1205; Eukaryota.
DR HOGENOM; CLU_010194_2_1_1; -.
DR InParanoid; Q9STY7; -.
DR OMA; SMEDMTF; -.
DR OrthoDB; 906746at2759; -.
DR PhylomeDB; Q9STY7; -.
DR BioCyc; ARA:AT3G47360-MON; -.
DR PRO; PR:Q9STY7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9STY7; baseline and differential.
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 3: Inferred from homology;
KW Lipid biosynthesis; Lipid metabolism; Membrane; NADP; Oxidoreductase;
KW Reference proteome; Signal-anchor; Steroid biosynthesis; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..309
FT /note="11-beta-hydroxysteroid dehydrogenase-like 3"
FT /id="PRO_0000422281"
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 309 AA; 34947 MW; F56171D075B8BCB0 CRC64;
MDILTTILNL LLPPLTIIFL FLFYPFYLLI KLVLCLRKNL HFENVARKVV LITGASSGIG
EHVAYEYAKK GAYLALVARR RDRLEIVAET SRQLGSGNVI IIPGDVSNVE DCKKFIDETI
RHFGKLDHLI NNAGVFQTVL FEDFTQIQDA NPIMDINFWG TTYITYFAIP HLRKSKGKIV
AITSGSANIP LPLASIYAAS KAALLRFFET LRIELSPDIK ITIVLPGVVS TDMTTPHCIE
KYGSDFILSE SVSKCAKAIF RGIGRGETYI EEPSWMKWLF IMKNVCPEIV DYGLNYLFVS
YLKPYFKRD
