DHI1_MOUSE
ID DHI1_MOUSE Reviewed; 292 AA.
AC P50172;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=11-beta-hydroxysteroid dehydrogenase 1 {ECO:0000303|PubMed:7873449};
DE Short=11-DH;
DE Short=11-beta-HSD1 {ECO:0000303|PubMed:7873449};
DE EC=1.1.1.146 {ECO:0000269|PubMed:23415904, ECO:0000269|PubMed:30902677};
DE AltName: Full=11-beta-hydroxysteroid dehydrogenase/microsomal carbonyl reductase {ECO:0000303|PubMed:7851387};
DE Short=11-beta-HSD1A/MCR {ECO:0000303|PubMed:7851387};
DE AltName: Full=11beta-HSD1A {ECO:0000303|PubMed:7851387};
DE AltName: Full=7-oxosteroid reductase;
DE EC=1.1.1.201 {ECO:0000269|PubMed:23415904};
DE AltName: Full=Corticosteroid 11-beta-dehydrogenase isozyme 1;
DE AltName: Full=liver-type 11-beta-HSD {ECO:0000303|PubMed:7873449};
GN Name=Hsd11b1 {ECO:0000312|EMBL:AAB33601.1}; Synonyms=Hsd11;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RX PubMed=7873449; DOI=10.1016/0960-0760(94)00159-j;
RA Rajan V., Chapman K.E., Lyons V., Jamieson P., Mullins J.J., Edwards C.R.,
RA Seckl J.R.;
RT "Cloning, sequencing and tissue-distribution of mouse 11 beta-
RT hydroxysteroid dehydrogenase-1 cDNA.";
RL J. Steroid Biochem. Mol. Biol. 52:141-147(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=7851387; DOI=10.1111/j.1432-1033.1995.tb20377.x;
RA Oppermann U.C.T., Netter K.J., Maser E.;
RT "Cloning and primary structure of murine 11 beta-hydroxysteroid
RT dehydrogenase/microsomal carbonyl reductase.";
RL Eur. J. Biochem. 227:202-208(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
RX PubMed=8973338; DOI=10.1016/s0378-1119(96)00490-8;
RA Voice M.W., Seckl J.R., Chapman K.E.;
RT "The sequence of 5' flanking DNA from the mouse 11 beta-hydroxysteroid
RT dehydrogenase type 1 gene and analysis of putative transcription factor
RT binding sites.";
RL Gene 181:233-235(1996).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=9405715; DOI=10.1073/pnas.94.26.14924;
RA Kotelevtsev Y., Holmes M.C., Burchell A., Houston P.M., Schmoll D.,
RA Jamieson P., Best R., Brown R., Edwards C.R., Seckl J.R., Mullins J.J.;
RT "11beta-hydroxysteroid dehydrogenase type 1 knockout mice show attenuated
RT glucocorticoid-inducible responses and resist hyperglycemia on obesity or
RT stress.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:14924-14929(1997).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, and
RC Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=23415904; DOI=10.1016/j.bcp.2013.02.002;
RA Mitic T., Shave S., Semjonous N., McNae I., Cobice D.F., Lavery G.G.,
RA Webster S.P., Hadoke P.W., Walker B.R., Andrew R.;
RT "11beta-Hydroxysteroid dehydrogenase type 1 contributes to the balance
RT between 7-keto- and 7-hydroxy-oxysterols in vivo.";
RL Biochem. Pharmacol. 86:146-153(2013).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=30902677; DOI=10.1016/j.jsbmb.2019.03.011;
RA Beck K.R., Kanagaratnam S., Kratschmar D.V., Birk J., Yamaguchi H.,
RA Sailer A.W., Seuwen K., Odermatt A.;
RT "Enzymatic interconversion of the oxysterols 7beta,25-dihydroxycholesterol
RT and 7-keto,25-hydroxycholesterol by 11beta-hydroxysteroid dehydrogenase
RT type 1 and 2.";
RL J. Steroid Biochem. Mol. Biol. 190:19-28(2019).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 24-291 IN COMPLEXES WITH NADP AND
RP CORTICOSTERONE, AND SUBUNIT.
RX PubMed=15865440; DOI=10.1021/bi047599q;
RA Zhang J., Osslund T.D., Plant M.H., Clogston C.L., Nybo R.E., Xiong F.,
RA Delaney J.M., Jordan S.R.;
RT "Crystal structure of murine 11 beta-hydroxysteroid dehydrogenase 1: an
RT important therapeutic target for diabetes.";
RL Biochemistry 44:6948-6957(2005).
CC -!- FUNCTION: Controls the reversible conversion of biologically active
CC glucocorticoids such as 11-dehydrocorticosterone to corticosterone in
CC the presence of NADP(H) (PubMed:9405715, PubMed:23415904,
CC PubMed:30902677). Participates in the corticosteroid receptor-mediated
CC anti-inflammatory response, as well as metabolic and homeostatic
CC processes (PubMed:9405715). Bidirectional in vitro, predominantly
CC functions as a reductase in vivo, thereby increasing the concentration
CC of active glucocorticoids (PubMed:23415904). It has broad substrate
CC specificity, besides glucocorticoids, it accepts other steroid and
CC sterol substrates (PubMed:23415904). Interconverts 7-oxo- and 7-
CC hydroxy-neurosteroids such as 7-oxopregnenolone and 7beta-
CC hydroxypregnenolone, 7-oxodehydroepiandrosterone (3beta-hydroxy-5-
CC androstene-7,17-dione) and 7beta-hydroxydehydroepiandrosterone
CC (3beta,7beta-dihydroxyandrost-5-en-17-one), among others (By
CC similarity). Catalyzes the stereo-specific conversion of the major
CC dietary oxysterol, 7-ketocholesterol (7-oxocholesterol), into the more
CC polar 7-beta-hydroxycholesterol metabolite (PubMed:23415904). 7-
CC oxocholesterol is one of the most important oxysterols, it participates
CC in several events such as induction of apoptosis, accumulation in
CC atherosclerotic lesions, lipid peroxidation, and induction of foam cell
CC formation (By similarity). Mediates the 7-oxo reduction of 7-
CC oxolithocholate mainly to chenodeoxycholate, and to a lesser extent to
CC ursodeoxycholate, both in its free form and when conjugated to glycine
CC or taurine, providing a link between glucocorticoid activation and bile
CC acid metabolism (By similarity). Catalyzes the synthesis of 7-beta-25-
CC dihydroxycholesterol from 7-oxo-25-hydroxycholesterol in vitro, which
CC acts as ligand for the G-protein-coupled receptor (GPCR) Epstein-Barr
CC virus-induced gene 2 (EBI2) and may thereby regulate immune cell
CC migration (PubMed:30902677). {ECO:0000250|UniProtKB:P28845,
CC ECO:0000269|PubMed:23415904, ECO:0000269|PubMed:30902677,
CC ECO:0000269|PubMed:9405715, ECO:0000303|PubMed:23415904,
CC ECO:0000303|PubMed:9405715}.
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:23415904,
CC ECO:0000269|PubMed:30902677, ECO:0000269|PubMed:9405715};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11389;
CC Evidence={ECO:0000269|PubMed:23415904, ECO:0000269|PubMed:30902677};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11390;
CC Evidence={ECO:0000269|PubMed:23415904, ECO:0000269|PubMed:30902677,
CC ECO:0000269|PubMed:9405715};
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:23415904, ECO:0000269|PubMed:30902677,
CC ECO:0000269|PubMed:9405715};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42201;
CC Evidence={ECO:0000269|PubMed:23415904, ECO:0000269|PubMed:30902677};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42202;
CC Evidence={ECO:0000269|PubMed:23415904, ECO:0000269|PubMed:30902677,
CC ECO:0000269|PubMed:9405715};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 7beta-hydroxysteroid + NADP(+) = a 7-oxosteroid + H(+) +
CC NADPH; Xref=Rhea:RHEA:20233, ChEBI:CHEBI:15378, ChEBI:CHEBI:35349,
CC ChEBI:CHEBI:47789, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.201; Evidence={ECO:0000269|PubMed:23415904};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20235;
CC Evidence={ECO:0000269|PubMed:23415904};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-oxocholesterol + H(+) + NADPH = 7beta-hydroxycholesterol +
CC NADP(+); Xref=Rhea:RHEA:68656, ChEBI:CHEBI:15378, ChEBI:CHEBI:42989,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:64294;
CC Evidence={ECO:0000269|PubMed:23415904};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68657;
CC Evidence={ECO:0000269|PubMed:23415904};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chenodeoxycholate + NADP(+) = 7-oxolithocholate + H(+) +
CC NADPH; Xref=Rhea:RHEA:53820, ChEBI:CHEBI:15378, ChEBI:CHEBI:36234,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78605;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53822;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-oxolithocholate + H(+) + NADPH = NADP(+) + ursodeoxycholate;
CC Xref=Rhea:RHEA:47540, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:78604, ChEBI:CHEBI:78605;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47541;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycochenodeoxycholate + NADP(+) = 7-oxoglycolithocholate +
CC H(+) + NADPH; Xref=Rhea:RHEA:65056, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:36252, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:137818; Evidence={ECO:0000250|UniProtKB:P28845};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:65058;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + taurochenodeoxycholate = 7-oxotaurolithocholate +
CC H(+) + NADPH; Xref=Rhea:RHEA:65060, ChEBI:CHEBI:9407,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:137724; Evidence={ECO:0000250|UniProtKB:P28845};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:65062;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + tauroursodeoxycholate = 7-oxotaurolithocholate +
CC H(+) + NADPH; Xref=Rhea:RHEA:68980, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132028,
CC ChEBI:CHEBI:137724; Evidence={ECO:0000250|UniProtKB:P28845};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68982;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycoursodeoxycholate + NADP(+) = 7-oxoglycolithocholate +
CC H(+) + NADPH; Xref=Rhea:RHEA:68976, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132030,
CC ChEBI:CHEBI:137818; Evidence={ECO:0000250|UniProtKB:P28845};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68978;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-oxopregnenolone + H(+) + NADPH = 7beta-hydroxypregnenolone +
CC NADP(+); Xref=Rhea:RHEA:69436, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:183806, ChEBI:CHEBI:183807;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69437;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3beta,7alpha-dihydroxyandrost-5-en-17-one + NADP(+) = 3beta-
CC hydroxy-5-androstene-7,17-dione + H(+) + NADPH; Xref=Rhea:RHEA:69440,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:81471, ChEBI:CHEBI:183808;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69441;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3beta-hydroxy-5-androstene-7,17-dione + H(+) + NADPH =
CC 3beta,7beta-dihydroxyandrost-5-en-17-one + NADP(+);
CC Xref=Rhea:RHEA:69452, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:183368, ChEBI:CHEBI:183808;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69453;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3beta-hydroxy-5alpha-androstane-7,17-dione + H(+) + NADPH =
CC 3beta,7beta-dihydroxy-5alpha-androstan-17-one + NADP(+);
CC Xref=Rhea:RHEA:69456, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:79834, ChEBI:CHEBI:183809;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69457;
CC Evidence={ECO:0000250|UniProtKB:P28845};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=120 nM for 11-dehydrocorticosterone {ECO:0000269|PubMed:9405715};
CC KM=0.2 uM for 11-dehydrocorticosterone {ECO:0000269|PubMed:23415904};
CC KM=1269 uM for 7-oxocholesterol {ECO:0000269|PubMed:23415904};
CC KM=1.78 uM for corticosterone {ECO:0000269|PubMed:23415904};
CC KM=327.6 uM for 7-beta-hydroxycholesterol
CC {ECO:0000269|PubMed:23415904};
CC Vmax=8.56 pmol/min/ug enzyme with 11-dehydrocorticosterone as
CC substrate {ECO:0000269|PubMed:23415904};
CC Vmax=4.82 pmol/min/ug enzyme with corticosterone as substrate
CC {ECO:0000269|PubMed:23415904};
CC Vmax=0.12 pmol/min/ug enzyme with 7-oxocholesterol as substrate
CC {ECO:0000269|PubMed:23415904};
CC Vmax=0.010 pmol/min/ug enzyme with 7-beta-hydroxycholesterol as
CC substrate {ECO:0000269|PubMed:23415904};
CC -!- PATHWAY: Steroid metabolism. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15865440}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC II membrane protein.
CC -!- TISSUE SPECIFICITY: Widely expressed. Highest levels (mRNA) in liver,
CC kidney and lung, lower levels in the cerebellum, cortex, hippocampus,
CC ovary, testis and thymus, no expression in colon.
CC {ECO:0000269|PubMed:7873449}.
CC -!- DISRUPTION PHENOTYPE: In null mice, 11-keto corticosteroids cannot be
CC reduced to active 11-hydroxy forms (PubMed:9405715). Plasma
CC corticosterone levels actually are elevated at the diurnal nadir
CC (PubMed:9405715). Males display adrenocortical hyperplasia
CC (PubMed:9405715). During starvation, induction of hepatic glucose-6-
CC phosphatase (G6Pase) mRNA and enzyme activity is lost and the induction
CC of phosphoenolpyruvate carboxykinase (PEPCK) is attenuated
CC (PubMed:9405715). Liver glycogen levels significantly increase in the
CC fed state (PubMed:9405715). The liver shows a phenotype of partial
CC glucocorticoid deficiency, despite somewhat increased basal plasma
CC corticosterone levels (PubMed:9405715). {ECO:0000269|PubMed:9405715}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; S75207; AAB33601.1; -; mRNA.
DR EMBL; X83202; CAA58209.1; -; mRNA.
DR EMBL; X92186; CAA63096.1; -; Genomic_DNA.
DR CCDS; CCDS15635.1; -.
DR PIR; I56604; I56604.
DR RefSeq; NP_001038216.1; NM_001044751.1.
DR RefSeq; NP_032314.2; NM_008288.2.
DR PDB; 1Y5M; X-ray; 2.30 A; A/B=24-292.
DR PDB; 1Y5R; X-ray; 3.00 A; A/B=24-292.
DR PDB; 3GMD; X-ray; 2.28 A; A/B/C/D/E/F/G/H=26-289.
DR PDB; 4K26; X-ray; 2.21 A; A/B=24-292.
DR PDB; 4NMH; X-ray; 2.90 A; A/B/C/D=24-292.
DR PDB; 5PGZ; X-ray; 2.90 A; A/B=24-292.
DR PDB; 5QIJ; X-ray; 2.65 A; A/B=24-292.
DR PDBsum; 1Y5M; -.
DR PDBsum; 1Y5R; -.
DR PDBsum; 3GMD; -.
DR PDBsum; 4K26; -.
DR PDBsum; 4NMH; -.
DR PDBsum; 5PGZ; -.
DR PDBsum; 5QIJ; -.
DR AlphaFoldDB; P50172; -.
DR SMR; P50172; -.
DR IntAct; P50172; 5.
DR STRING; 10090.ENSMUSP00000016338; -.
DR BindingDB; P50172; -.
DR ChEMBL; CHEMBL3910; -.
DR DrugCentral; P50172; -.
DR GlyConnect; 2235; 1 N-Linked glycan (1 site).
DR GlyGen; P50172; 2 sites, 1 N-linked glycan (1 site).
DR iPTMnet; P50172; -.
DR PhosphoSitePlus; P50172; -.
DR SwissPalm; P50172; -.
DR jPOST; P50172; -.
DR PaxDb; P50172; -.
DR PeptideAtlas; P50172; -.
DR PRIDE; P50172; -.
DR ProteomicsDB; 277334; -.
DR Antibodypedia; 34595; 427 antibodies from 41 providers.
DR DNASU; 15483; -.
DR Ensembl; ENSMUST00000016338; ENSMUSP00000016338; ENSMUSG00000016194.
DR Ensembl; ENSMUST00000161737; ENSMUSP00000125620; ENSMUSG00000016194.
DR GeneID; 15483; -.
DR KEGG; mmu:15483; -.
DR UCSC; uc007eef.1; mouse.
DR CTD; 3290; -.
DR MGI; MGI:103562; Hsd11b1.
DR VEuPathDB; HostDB:ENSMUSG00000016194; -.
DR eggNOG; KOG1205; Eukaryota.
DR GeneTree; ENSGT00940000160097; -.
DR InParanoid; P50172; -.
DR OMA; SMEDMTF; -.
DR OrthoDB; 906746at2759; -.
DR PhylomeDB; P50172; -.
DR TreeFam; TF329114; -.
DR BRENDA; 1.1.1.146; 3474.
DR Reactome; R-MMU-194002; Glucocorticoid biosynthesis.
DR BioGRID-ORCS; 15483; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Hsd11b1; mouse.
DR EvolutionaryTrace; P50172; -.
DR PRO; PR:P50172; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P50172; protein.
DR Bgee; ENSMUSG00000016194; Expressed in left lobe of liver and 197 other tissues.
DR ExpressionAtlas; P50172; baseline and differential.
DR Genevisible; P50172; MM.
DR GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
DR GO; GO:0070524; F:11-beta-hydroxysteroid dehydrogenase (NADP+) activity; IDA:MGI.
DR GO; GO:0047022; F:7-beta-hydroxysteroid dehydrogenase (NADP+) activity; IEA:RHEA.
DR GO; GO:0102196; F:cortisol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; ISO:MGI.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0005496; F:steroid binding; ISO:MGI.
DR GO; GO:0006704; P:glucocorticoid biosynthetic process; ISO:MGI.
DR GO; GO:0006713; P:glucocorticoid catabolic process; ISO:MGI.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0008212; P:mineralocorticoid metabolic process; ISO:MGI.
DR GO; GO:0043456; P:regulation of pentose-phosphate shunt; ISO:MGI.
DR GO; GO:0006706; P:steroid catabolic process; IBA:GO_Central.
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 3D-structure; Endoplasmic reticulum; Glycoprotein; Lipid metabolism;
KW Membrane; NADP; Oxidoreductase; Reference proteome; Signal-anchor;
KW Steroid metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..292
FT /note="11-beta-hydroxysteroid dehydrogenase 1"
FT /id="PRO_0000054621"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..24
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..292
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 183
FT /note="Proton acceptor"
FT BINDING 41..67
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 92..93
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 119..121
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 170
FT /ligand="substrate"
FT BINDING 183..187
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 218..222
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28845"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 15
FT /note="F -> S (in Ref. 2; CAA58209)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="N -> D (in Ref. 2; CAA58209)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="Q -> L (in Ref. 2; CAA58209)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="S -> L (in Ref. 2; CAA58209)"
FT /evidence="ECO:0000305"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:4K26"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:4K26"
FT HELIX 45..56
FT /evidence="ECO:0007829|PDB:4K26"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:4K26"
FT HELIX 68..81
FT /evidence="ECO:0007829|PDB:4K26"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:4K26"
FT HELIX 96..110
FT /evidence="ECO:0007829|PDB:4K26"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:4K26"
FT HELIX 133..143
FT /evidence="ECO:0007829|PDB:4K26"
FT HELIX 145..161
FT /evidence="ECO:0007829|PDB:4K26"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:4K26"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:4K26"
FT HELIX 181..203
FT /evidence="ECO:0007829|PDB:4K26"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:4K26"
FT HELIX 221..227
FT /evidence="ECO:0007829|PDB:4K26"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:4K26"
FT HELIX 238..250
FT /evidence="ECO:0007829|PDB:4K26"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:4K26"
FT HELIX 264..268
FT /evidence="ECO:0007829|PDB:4K26"
FT HELIX 271..280
FT /evidence="ECO:0007829|PDB:4K26"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:4K26"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:4K26"
SQ SEQUENCE 292 AA; 32364 MW; ADE42B11D82DD6CD CRC64;
MAVMKNYLLP ILVLFLAYYY YSTNEEFRPE MLQGKKVIVT GASKGIGREM AYHLSKMGAH
VVLTARSEEG LQKVVSRCLE LGAASAHYIA GTMEDMTFAE QFIVKAGKLM GGLDMLILNH
ITQTSLSLFH DDIHSVRRVM EVNFLSYVVM STAALPMLKQ SNGSIAVISS LAGKMTQPMI
APYSASKFAL DGFFSTIRTE LYITKVNVSI TLCVLGLIDT ETAMKEISGI INAQASPKEE
CALEIIKGTA LRKSEVYYDK SPLTPILLGN PGRKIMEFFS LRYYNKDMFV SN
