HSDA_ARAHY
ID HSDA_ARAHY Reviewed; 349 AA.
AC A7LB60;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=11-beta-hydroxysteroid dehydrogenase A {ECO:0000305};
DE EC=1.1.1.146 {ECO:0000250|UniProtKB:Q93W57};
DE AltName: Full=17-beta-hydroxysteroid dehydrogenase A {ECO:0000305};
DE EC=1.1.1.- {ECO:0000250|UniProtKB:Q93W57};
DE AltName: Full=Steroleosin-A {ECO:0000303|PubMed:25860789, ECO:0000312|EMBL:ABS28874.1, ECO:0000312|EMBL:ABX38844.1};
GN Name=STO-A {ECO:0000312|EMBL:ABS28874.1};
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:ABS28874.1};
RN [1] {ECO:0000312|EMBL:ABS28874.1}
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] {ECO:0000312|EMBL:ABX38844.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Fu G., Li C., Zhong Y., Yan Y., Wang L., Huang S.;
RT "Cloning and characterization of one novel gene encoding peanut
RT steroleosin.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 1-10; 49-70; 81-92; 93-103; 115-125; 167-173; 202-212;
RP 238-252; 308-324 AND 334-347, 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:Q93W57}.
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:Q93W57};
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:0000255|RuleBase:RU000363}.
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DR EMBL; EF695404; ABS28874.1; -; mRNA.
DR EMBL; EU250375; ABX38844.1; -; Genomic_DNA.
DR AlphaFoldDB; A7LB60; -.
DR SMR; A7LB60; -.
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 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..349
FT /note="11-beta-hydroxysteroid dehydrogenase A"
FT /id="PRO_0000449960"
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 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 349 AA; 38692 MW; 8949998A0503DCF6 CRC64;
MDLIHTFLNL VAPPFTFFFL CLFLPPYWGL KFMVSILSWL LSENVAGKVV HITGASSGIG
EYLAYEYAKR GACLALSARR ETALHQVADT ARHLGSPDVI VMRADVSKPE DCMRLIDQTV
NHFGRLDHLV NNAAISIATL FEETPDISNL RPIMETNFWG SVYTTRYALQ HLRKSRGKIV
VMSSVDSWLP APRRHIYSAS KAALVSLYET LRVEVGSEIG ITIVTPGYIE SEITKGKFLS
AQGEVDVDQD LRDVEVSAVP VGSVSGCAES IIKSTLRGDR CLTVPSWFRM TYLIKLLCPE
LLEWTFRLLY LTAPGTPTSD ALSKKILDAT GAKNLFYPPS IQSPDVKTD
