HSD_PINMS
ID HSD_PINMS Reviewed; 356 AA.
AC A0A140FAN3;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=11-beta-hydroxysteroid dehydrogenase {ECO:0000305};
DE EC=1.1.1.146 {ECO:0000269|PubMed:26897709};
DE AltName: Full=17-beta-hydroxysteroid dehydrogenase {ECO:0000305};
DE EC=1.1.1.62 {ECO:0000269|PubMed:26897709};
DE AltName: Full=Steroleosin {ECO:0000303|PubMed:26897709, ECO:0000312|EMBL:AML81109.1};
OS Pinus massoniana (Chinese red pine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC Pinus subgen. Pinus.
OX NCBI_TaxID=88730;
RN [1] {ECO:0000312|EMBL:AML81109.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 32-38; 72-79; 194-201;
RP 253-269 AND 270-277, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF 206-SER--GLU-356.
RC TISSUE=Megagametophyte {ECO:0000303|PubMed:26897709};
RX PubMed=26897709; DOI=10.1016/j.plaphy.2016.02.008;
RA Pasaribu B., Chen C.-S., Liao Y.K., Jiang P.-L., Tzen J.T.C.;
RT "Identification of steroleosin in oil bodies of pine megagametophytes.";
RL Plant Physiol. Biochem. 101:173-181(2016).
CC -!- FUNCTION: Has dehydrogenase activity against corticosterone (11 beta-
CC hydroxysteroid) and estradiol (17 beta-hydroxysteroid) in the presence
CC of NADP(+). May be involved in signal transduction regulated by various
CC sterols. {ECO:0000269|PubMed:26897709}.
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:26897709};
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:26897709};
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; EC=1.1.1.62;
CC Evidence={ECO:0000269|PubMed:26897709};
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:26897709}.
CC Membrane {ECO:0000255}; Single-pass type II membrane protein
CC {ECO:0000305}. Note=Surface of oil bodies. Exists at a monolayer
CC lipid/water interface. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in megagametophytes (at protein level).
CC {ECO:0000269|PubMed:26897709}.
CC -!- DOMAIN: The proline-knob motif may be involved in the targeting to oil
CC bodies. {ECO:0000250|UniProtKB:Q93W57}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000255|RuleBase:RU000363}.
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DR EMBL; KT731102; AML81109.1; -; mRNA.
DR AlphaFoldDB; A0A140FAN3; -.
DR SMR; A0A140FAN3; -.
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:0102196; F:cortisol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IEA:UniProtKB-EC.
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 Direct protein sequencing; Lipid droplet; Membrane; NADP; Oxidoreductase;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..356
FT /note="11-beta-hydroxysteroid dehydrogenase"
FT /id="PRO_0000449961"
FT TRANSMEM 10..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT MOTIF 13..26
FT /note="Proline-knob"
FT /evidence="ECO:0000250|UniProtKB:Q93W57"
FT ACT_SITE 197
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 54..85
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P14061"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P28845"
FT BINDING 197..201
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28845"
FT BINDING 201
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P14061"
FT MUTAGEN 206..356
FT /note="Missing: Loss of binding to plant derived
FT cholesterol, cholest-5-en-3beta-ol."
FT /evidence="ECO:0000269|PubMed:26897709"
SQ SEQUENCE 356 AA; 40691 MW; 9916D2FBF298B0C5 CRC64;
MDVMNFLLNL VVPPAGLLML AFAWPSLAFF RACEWALRII YGEDMEGKVV IITGASSGIG
EQIAYQYAKR RANLVLVARR EHRLRSIREK ARTLGAKNVL VIAADVVKEE DCKRFIDETI
NQYGHLDHLV NNAGLGHSFL FEEASDTSGF AHMMDINFWG SVYPTFFALP HLRRRNGRII
VNASVEGWLP MPRMSLYNAA KAAVVSFYET LRIEIGGAID ITIATPGWIE SDMTRGRFMT
EEGEVLFKEE PREMYVGPYP VAYTEECART IVSGACKGQR YVRFPMWYNV FFLYRVFVPD
LLDWTYRLLF LNHFITTASK DHTLHDFKGA RKKLLITPTS LQLLHHQQHQ SPKSSE
