HSDB_ARAHY
ID HSDB_ARAHY Reviewed; 353 AA.
AC A7LB59;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=11-beta-hydroxysteroid dehydrogenase B {ECO:0000305};
DE EC=1.1.1.146 {ECO:0000250|UniProtKB:Q8LKV5};
DE AltName: Full=17-beta-hydroxysteroid dehydrogenase B {ECO:0000305};
DE EC=1.1.1.- {ECO:0000250|UniProtKB:Q8LKV5};
DE AltName: Full=Steroleosin-B {ECO:0000303|PubMed:25860789, ECO:0000312|EMBL:ABS28873.1};
GN Name=STO-B {ECO:0000312|EMBL:ABS28873.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000312|EMBL:ABS28873.1};
RN [1] {ECO:0000312|EMBL:ABS28873.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Shanyou 523 {ECO:0000303|Ref.1};
RA Fu G., Li C., Wang L., Huang S.;
RT "Cloning and characterization of two genes encoding peanut seed
RT steroleosins.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 86-92; 114-125; 115-125; 238-252; 253-266; 281-292;
RP 305-313 AND 324-337, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Seed {ECO:0000269|PubMed:25860789};
RX PubMed=25860789; DOI=10.1371/journal.pone.0123419;
RA Schwager C., Kull S., Krause S., Schocker F., Petersen A., Becker W.M.,
RA Jappe U.;
RT "Development of a novel strategy to isolate lipophilic allergens (oleosins)
RT from peanuts.";
RL PLoS ONE 10:E0123419-E0123419(2015).
CC -!- FUNCTION: Has dehydrogenase activity against 11 beta-hydroxysteroid and
CC 17 beta-hydroxysteroid. May be involved in signal transduction
CC regulated by various sterols. {ECO:0000250|UniProtKB:Q8LKV5}.
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:0000250|UniProtKB:Q8LKV5};
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:25860789}.
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 seeds (at protein level).
CC {ECO:0000269|PubMed:25860789}.
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; EF695403; ABS28873.1; -; mRNA.
DR AlphaFoldDB; A7LB59; -.
DR SMR; A7LB59; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0012511; C:monolayer-surrounded lipid storage body; IDA:UniProtKB.
DR GO; GO:0070524; F:11-beta-hydroxysteroid dehydrogenase (NADP+) activity; ISS:UniProtKB.
DR GO; GO:0072582; F:17-beta-hydroxysteroid dehydrogenase (NADP+) activity; ISS:UniProtKB.
DR GO; GO:0102196; F:cortisol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; ISS: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 Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..353
FT /note="11-beta-hydroxysteroid dehydrogenase B"
FT /id="PRO_5002712241"
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..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 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 353 AA; 39598 MW; 9170A1DB52B5B290 CRC64;
MDLINSVLNL FVPPASLITL AFSWPALCFP HACEWLYNTV YGDNMDGKVV IITGASSGIG
EQIAYEYALR RACLVLVARR EHRLRGIAEN ARRMGARHVM IVAADVVKED ECRRFVNETI
NFYGRVDHLV NTVSLGHTFY FEEVTDTSVF PVLLDINFWG NIYPTLVALP YLHRTNGRVI
INASVESWLP LPRMSLYAAA KAALVNFYET LRFELRDEVG VTIATHGWIG SEMTSGKFML
EEGAEMQWKE EREMNVIGGP VEEFARLMVA GACRGDAYVK YPSWYDVFLL YRVFAPNVLN
WAFRLLIAPQ GTKRTSSYVG TGRSLEGRPM LEAPSPRTAL LAPYSFSGGG QLS
