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   27-MAR-2024, entry version 187.
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 a 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=0.01 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   GlyCosmos; P50172; 2 sites, 1 glycan.
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; 10090-ENSMUSP00000016338; -.
DR   PeptideAtlas; P50172; -.
DR   ProteomicsDB; 277334; -.
DR   Antibodypedia; 34595; 463 antibodies from 41 providers.
DR   DNASU; 15483; -.
DR   Ensembl; ENSMUST00000016338.15; ENSMUSP00000016338.9; ENSMUSG00000016194.15.
DR   Ensembl; ENSMUST00000161737.8; ENSMUSP00000125620.2; ENSMUSG00000016194.15.
DR   GeneID; 15483; -.
DR   KEGG; mmu:15483; -.
DR   UCSC; uc007eef.1; mouse.
DR   AGR; MGI:103562; -.
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; 2904540at2759; -.
DR   PhylomeDB; P50172; -.
DR   TreeFam; TF329114; -.
DR   BRENDA; 1.1.1.146; 3474.
DR   Reactome; R-MMU-194002; Glucocorticoid biosynthesis.
DR   Reactome; R-MMU-9757110; Prednisone ADME.
DR   BioGRID-ORCS; 15483; 1 hit in 80 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 198 other cell types or tissues.
DR   ExpressionAtlas; P50172; baseline and differential.
DR   GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0031965; C:nuclear membrane; 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: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   CDD; cd05332; 11beta-HSD1_like_SDR_c; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   PANTHER; PTHR44279:SF1; 11-BETA-HYDROXYSTEROID DEHYDROGENASE 1; 1.
DR   PANTHER; PTHR44279; HYDROXYSTEROID (11-BETA) DEHYDROGENASE 1-LIKE B-RELATED; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
DR   Genevisible; P50172; MM.
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
//