HSDB_SESIN
ID HSDB_SESIN Reviewed; 362 AA.
AC Q8LKV5;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=11-beta-hydroxysteroid dehydrogenase B {ECO:0000305};
DE EC=1.1.1.146 {ECO:0000269|PubMed:15331088};
DE AltName: Full=17-beta-hydroxysteroid dehydrogenase B {ECO:0000305};
DE EC=1.1.1.62 {ECO:0000269|PubMed:15331088};
DE AltName: Full=Seed oil body protein 3 {ECO:0000303|PubMed:15331088};
DE AltName: Full=Steroleosin-B {ECO:0000303|PubMed:15331088, ECO:0000312|EMBL:AAM46847.1};
GN Name=SOP3 {ECO:0000303|PubMed:15331088, 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:AAM46847.1};
RN [1] {ECO:0000312|EMBL:AAM46847.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-32 AND 94-104, FUNCTION,
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Seed {ECO:0000303|PubMed:15331088};
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).
RN [2]
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).
CC -!- FUNCTION: Has dehydrogenase activity against corticosterone (11 beta-
CC hydroxysteroid) and estradiol (17 beta-hydroxysteroid), with similar
CC activities to both sterols in the presence of NADP(+), but negligible
CC activity to either sterol in the presence of NAD(+). May be involved in
CC signal transduction regulated by various sterols.
CC {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 EC=1.1.1.146; Evidence={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: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:15331088};
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:15331088,
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:15331088, PubMed:9816677). Not expressed in stem, leaf or root
CC (at protein level) (PubMed:9816677). {ECO:0000269|PubMed:15331088,
CC ECO:0000269|PubMed:9816677}.
CC -!- DEVELOPMENTAL STAGE: Expressed during seed maturation (PubMed:15331088,
CC PubMed:9816677). Appears in maturing seeds approximately 3 weeks after
CC flowering and thereafter the level is maintained at a steady level till
CC the late stage of seed maturation (at protein level). Detected in
CC maturing seeds 2-3 weeks after flowering, progressively increasing to
CC the maximal level in the following 2 weeks, and diminishing thereafter
CC to a relatively low level at the late stage of seed maturation
CC (PubMed:15331088). {ECO:0000269|PubMed:15331088,
CC ECO:0000269|PubMed:9816677}.
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:0000305}.
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DR EMBL; AF498264; AAM46847.1; -; mRNA.
DR RefSeq; NP_001291330.1; NM_001304401.1.
DR AlphaFoldDB; Q8LKV5; -.
DR SMR; Q8LKV5; -.
DR GeneID; 105175113; -.
DR KEGG; sind:105175113; -.
DR OrthoDB; 906746at2759; -.
DR Proteomes; UP000504604; Linkage group LG2.
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; IDA:UniProtKB.
DR GO; GO:0072582; F:17-beta-hydroxysteroid dehydrogenase (NADP+) activity; IDA:UniProtKB.
DR GO; GO:0102196; F:cortisol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IDA:UniProtKB.
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 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..362
FT /note="11-beta-hydroxysteroid dehydrogenase B"
FT /id="PRO_0000449959"
FT TRANSMEM 10..30
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT REGION 321..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 13..26
FT /note="Proline-knob"
FT /evidence="ECO:0000250|UniProtKB:Q93W57"
FT COMPBIAS 322..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 198
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 55..81
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P14061"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14061"
FT BINDING 198..202
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28845"
FT BINDING 202
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P14061"
SQ SEQUENCE 362 AA; 41137 MW; BEB69C2E2E8C4A0A CRC64;
MDLINSLLNF VVPPASLLML AFTWPTLFFI TTCEWLYNTY LNSENMENKV VLITGASSGI
GEQIAYQYAK RGANLVLVAR REHRLRGISE NARRLGAPNV LIMAADVVKE EECRRFINET
INYYGRVDHL VNTVSLGHTF YFEEASDSSV FPILMDINFW GNVYPTYVAL PYLRESNGRI
IVNASVENWL PLPRMSLYSA AKSALINFYE TLRFEVKNEV GITVATHGWI GTEMTRGKFM
VEEGAEMQWK EEREVHVTGG PVEEFAKQIV SGACRGDPYV KYPSWYDIFF LYRVFAPKVL
DWTFRFLLTN GGARRTSFIG TGRPLLETSS PRRSAVMEGS SPRRLPPGPL TFSPAFQQQK
SE
