HSDA_SESIN
ID HSDA_SESIN Reviewed; 348 AA.
AC Q93W57;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=11-beta-hydroxysteroid dehydrogenase A {ECO:0000305};
DE EC=1.1.1.- {ECO:0000269|PubMed:11950969, ECO:0000269|PubMed:15331088};
DE AltName: Full=17-beta-hydroxysteroid dehydrogenase A {ECO:0000305};
DE EC=1.1.1.62 {ECO:0000269|PubMed:11950969, ECO:0000269|PubMed:15331088};
DE AltName: Full=Seed oil body protein 2 {ECO:0000303|PubMed:11950969, ECO:0000303|PubMed:15331088};
DE AltName: Full=Steroleosin-A {ECO:0000303|PubMed:15331088};
GN Name=SOP2 {ECO:0000303|PubMed:11950969, ECO:0000303|PubMed:15331088,
GN ECO:0000303|PubMed:9816677};
OS Sesamum indicum (Oriental sesame) (Sesamum orientale).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Pedaliaceae; Sesamum.
OX NCBI_TaxID=4182 {ECO:0000312|EMBL:AAL13315.1};
RN [1] {ECO:0000312|EMBL:AAL13315.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 1-12; 194-204
RP AND 230-250, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, DOMAIN, AND 3D-STRUCTURE MODELING OF THE
RP DEHYDROGENASE DOMAIN.
RC TISSUE=Leaf {ECO:0000303|PubMed:11950969}, and
RC Seed {ECO:0000303|PubMed:11950969};
RX PubMed=11950969; DOI=10.1104/pp.010928;
RA Lin L.J., Tai S.S., Peng C.C., Tzen J.T.;
RT "Steroleosin, a sterol-binding dehydrogenase in seed oil bodies.";
RL Plant Physiol. 128:1200-1211(2002).
RN [2]
RP ERRATUM OF PUBMED:11950969.
RA Lin L.J., Tai S.S., Peng C.C., Tzen J.T.;
RL Plant Physiol. 129:1930-1930(2002).
RN [3]
RP GENE NAME, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=9816677; DOI=10.1093/oxfordjournals.pcp.a029457;
RA Chen E.C., Tai S.S., Peng C.C., Tzen J.T.;
RT "Identification of three novel unique proteins in seed oil bodies of
RT sesame.";
RL Plant Cell Physiol. 39:935-941(1998).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15331088; DOI=10.1016/j.plaphy.2004.06.006;
RA Lin L.J., Tzen J.T.;
RT "Two distinct steroleosins are present in seed oil bodies.";
RL Plant Physiol. Biochem. 42:601-608(2004).
CC -!- FUNCTION: Has dehydrogenase activity against corticosterone (11 beta-
CC hydroxysteroid) and estradiol (17 beta-hydroxysteroid), with higher
CC activity against estradiol. Possesses higher dehydrogenase activity
CC with NADP(+) than NAD(+) regardless of the sterol substrate. May be
CC involved in signal transduction regulated by various sterols.
CC {ECO:0000269|PubMed:11950969, ECO:0000269|PubMed:15331088}.
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 Evidence={ECO:0000269|PubMed:11950969, ECO:0000269|PubMed:15331088};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an 11beta-hydroxysteroid + NAD(+) = an 11-oxosteroid + H(+) +
CC NADH; Xref=Rhea:RHEA:53116, ChEBI:CHEBI:15378, ChEBI:CHEBI:35346,
CC ChEBI:CHEBI:47787, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000269|PubMed:11950969, ECO:0000269|PubMed:15331088};
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:11950969, ECO:0000269|PubMed:15331088};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=corticosterone + NAD(+) = 11-dehydrocorticosterone + H(+) +
CC NADH; Xref=Rhea:RHEA:42204, ChEBI:CHEBI:15378, ChEBI:CHEBI:16827,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78600;
CC Evidence={ECO:0000269|PubMed:11950969, ECO:0000269|PubMed:15331088};
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:11950969, ECO:0000269|PubMed:15331088};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol + NAD(+) = estrone + H(+) + NADH;
CC Xref=Rhea:RHEA:24612, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469,
CC ChEBI:CHEBI:17263, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.62;
CC Evidence={ECO:0000269|PubMed:11950969, ECO:0000269|PubMed:15331088};
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:11950969,
CC ECO:0000269|PubMed:9816677}. Membrane {ECO:0000255}; Single-pass type
CC II membrane protein {ECO:0000305}. Note=Surface of oil bodies. Exists
CC at a monolayer lipid/water interface. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in seeds (at protein level)
CC (PubMed:11950969, PubMed:9816677). Not expressed in stem, leaf or root
CC (at protein level) (PubMed:9816677). {ECO:0000269|PubMed:11950969,
CC ECO:0000269|PubMed:9816677}.
CC -!- DEVELOPMENTAL STAGE: Expressed during seed maturation (PubMed:11950969,
CC PubMed:9816677, PubMed:15331088). Appears in maturing seeds
CC approximately 3 weeks after flowering and thereafter the level is
CC continuously increased till the late stage of seed maturation (at
CC protein level) (PubMed:15331088). Detected in maturing seeds
CC approximately 2 weeks after flowering and expression is maintained at a
CC substantial level thereafter until the late stage of seed maturation
CC (PubMed:11950969). {ECO:0000269|PubMed:11950969,
CC ECO:0000269|PubMed:15331088, ECO:0000269|PubMed:9816677}.
CC -!- DOMAIN: The proline-knob motif may be involved in the targeting to oil
CC bodies. {ECO:0000305|PubMed:11950969}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000255|RuleBase:RU000363}.
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DR EMBL; AF302806; AAL09328.1; -; mRNA.
DR EMBL; AF421889; AAL13315.1; -; Genomic_DNA.
DR RefSeq; NP_001291322.1; NM_001304393.1.
DR AlphaFoldDB; Q93W57; -.
DR SMR; Q93W57; -.
DR EnsemblPlants; SIN_1022131.t; SIN_1022131.t; SIN_1022131.
DR GeneID; 105158152; -.
DR Gramene; SIN_1022131.t; SIN_1022131.t; SIN_1022131.
DR KEGG; sind:105158152; -.
DR OrthoDB; 906746at2759; -.
DR Proteomes; UP000504604; Linkage group LG3.
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:0070523; F:11-beta-hydroxysteroid dehydrogenase (NAD+) activity; IEA:RHEA.
DR GO; GO:0070524; F:11-beta-hydroxysteroid dehydrogenase (NADP+) activity; IEA:RHEA.
DR GO; GO:0044594; F:17-beta-hydroxysteroid dehydrogenase (NAD+) activity; IEA:RHEA.
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 Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..348
FT /note="11-beta-hydroxysteroid dehydrogenase A"
FT /id="PRO_0000449958"
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:0000305|PubMed:11950969"
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|UniProtKB:P14061"
FT BINDING 105
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P14061"
FT BINDING 132..135
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28845"
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"
SQ SEQUENCE 348 AA; 39568 MW; 53A0C6DF804CB59B CRC64;
MDLIHTFLNL IAPPFTFFFL LFFLPPFQIF KFFLSILGTL FSEDVAGKVV VITGASSGIG
ESLAYEYAKR GACLVLAARR ERSLQEVAER ARDLGSPDVV VVRADVSKAE DCRKVVDQTM
NRFGRLDHLV NNAGIMSVSM LEEVEDITGY RETMDINFWG YVYMTRFAAP YLRNSRGRIV
VLSSSSSWMP TPRMSFYNAS KAAISQFFET LRVEFGPDIG ITLVTPGFIE SELTQGKFYN
AGERVIDQDM RDVQVSTTPI LRVESAARSI VRSAIRGERY VTEPAWFRVT YWWKLFCPEV
MEWVFRLMYL ASPGEPEKET FGKKVLDYTG VKSLLYPETV QVPEPKND
