Q6QLL4 · DHI1_CAVPO

  • Protein
    11-beta-hydroxysteroid dehydrogenase 1
  • Gene
    HSD11B1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Controls the reversible conversion of biologically active glucocorticoids such as cortisone to cortisol, and 11-dehydrocorticosterone to corticosterone in the presence of NADP(H) (PubMed:10699594, PubMed:19507261).
Participates in the corticosteroid receptor-mediated anti-inflammatory response, as well as metabolic and homeostatic processes (By similarity).
Bidirectional in vitro, predominantly functions as a reductase in vivo, thereby increasing the concentration of active glucocorticoids. It has broad substrate specificity, besides glucocorticoids, it accepts other steroid and sterol substrates. Interconverts 7-oxo- and 7-hydroxy-neurosteroids such as 7-oxopregnenolone and 7beta-hydroxypregnenolone, 7-oxodehydroepiandrosterone (3beta-hydroxy-5-androstene-7,17-dione) and 7beta-hydroxydehydroepiandrosterone (3beta,7beta-dihydroxyandrost-5-en-17-one), among others (By similarity).
Catalyzes the stereo-specific conversion of the major dietary oxysterol, 7-ketocholesterol (7-oxocholesterol), into the more polar 7-beta-hydroxycholesterol metabolite (By similarity).
7-oxocholesterol is one of the most important oxysterols, it participates in several events such as induction of apoptosis, accumulation in atherosclerotic lesions, lipid peroxidation, and induction of foam cell formation (By similarity).
Mediates the 7-oxo reduction of 7-oxolithocholate mainly to chenodeoxycholate, and to a lesser extent to ursodeoxycholate, both in its free form and when conjugated to glycine or taurine, providing a link between glucocorticoid activation and bile acid metabolism (By similarity).
Catalyzes the synthesis of 7-beta-25-dihydroxycholesterol from 7-oxo-25-hydroxycholesterol in vitro, which acts as a ligand for the G-protein-coupled receptor (GPCR) Epstein-Barr virus-induced gene 2 (EBI2) and may thereby regulate immune cell migration (By similarity).

Catalytic activity

  • an 11beta-hydroxysteroid + NADP+ = an 11-oxosteroid + H+ + NADPH
    This reaction proceeds in the forward
    and the backward
    directions.
    EC:1.1.1.146 (UniProtKB | ENZYME | Rhea)
  • cortisone + H+ + NADPH = cortisol + NADP+
    This reaction proceeds in the forward
    and the backward
    directions.
  • corticosterone + NADP+ = 11-dehydrocorticosterone + H+ + NADPH
    This reaction proceeds in the forward
    and the backward
    directions.
  • a 7beta-hydroxysteroid + NADP+ = a 7-oxosteroid + H+ + NADPH
    This reaction proceeds in the backward direction.
    EC:1.1.1.201 (UniProtKB | ENZYME | Rhea)
  • 7-oxocholesterol + H+ + NADPH = 7beta-hydroxycholesterol + NADP+
    This reaction proceeds in the forward direction.
  • chenodeoxycholate + NADP+ = 7-oxolithocholate + H+ + NADPH
    This reaction proceeds in the backward direction.
  • 7-oxolithocholate + H+ + NADPH = NADP+ + ursodeoxycholate
    This reaction proceeds in the forward direction.
  • glycochenodeoxycholate + NADP+ = 7-oxoglycolithocholate + H+ + NADPH
    This reaction proceeds in the backward direction.
  • NADP+ + taurochenodeoxycholate = 7-oxotaurolithocholate + H+ + NADPH
    This reaction proceeds in the backward direction.
  • NADP+ + tauroursodeoxycholate = 7-oxotaurolithocholate + H+ + NADPH
    This reaction proceeds in the backward direction.
  • glycoursodeoxycholate + NADP+ = 7-oxoglycolithocholate + H+ + NADPH
    This reaction proceeds in the backward direction.
  • 7-oxopregnenolone + H+ + NADPH = 7beta-hydroxypregnenolone + NADP+
    This reaction proceeds in the forward direction.
  • 3beta,7alpha-dihydroxyandrost-5-en-17-one + NADP+ = 3beta-hydroxy-5-androstene-7,17-dione + H+ + NADPH
    This reaction proceeds in the forward direction.
  • 3beta-hydroxy-5-androstene-7,17-dione + H+ + NADPH = 3beta,7beta-dihydroxyandrost-5-en-17-one + NADP+
    This reaction proceeds in the forward direction.
  • 3beta-hydroxy-5alpha-androstane-7,17-dione + H+ + NADPH = 3beta,7beta-dihydroxy-5alpha-androstan-17-one + NADP+
    This reaction proceeds in the forward direction.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
2.85 μMcortisol
2.77 μMcortisone
4.09 μMcortisone

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site41-67NADP+ (UniProtKB | ChEBI)
Binding site92-93NADP+ (UniProtKB | ChEBI)
Binding site119-123NADP+ (UniProtKB | ChEBI)
Binding site170substrate
Active site183Proton acceptor
Binding site183-187NADP+ (UniProtKB | ChEBI)
Binding site218-222NADP+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum membrane
Molecular Function7-beta-hydroxysteroid dehydrogenase (NADP+) activity
Molecular Functioncortisol dehydrogenase activity
Molecular FunctionNADP binding
Molecular Functionprotein homodimerization activity
Molecular Functionsteroid binding
Biological Processlung development
Biological Processsteroid catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    11-beta-hydroxysteroid dehydrogenase 1
  • EC number
  • Short names
    11-DH; 11-beta-HSD1
  • Alternative names
    • 7-oxosteroid reductase (EC:1.1.1.201
      ) . EC:1.1.1.201 (UniProtKB | ENZYME | Rhea)
    • Corticosteroid 11-beta-dehydrogenase isozyme 1

Gene names

    • Name
      HSD11B1

Organism names

  • Taxonomic identifier
  • Strain
    • Hartley
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Hystricomorpha > Caviidae > Cavia

Accessions

  • Primary accession
    Q6QLL4
  • Secondary accessions
    • Q9QZE1

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-7Cytoplasmic
Transmembrane8-24Helical; Signal-anchor for type II membrane protein
Topological domain25-300Lumenal

Keywords

PTM/Processing

Features

Showing features for chain, glycosylation.

TypeIDPosition(s)Description
ChainPRO_00000546181-30011-beta-hydroxysteroid dehydrogenase 1
Glycosylation207N-linked (GlcNAc...) asparagine

Keywords

PTM databases

Expression

Tissue specificity

Widely expressed in all peripheral tissues, with highest expression in liver, followed by kidney and lung, and very low expression in heart, lung, spleen, stomach, small intestine, colon, skin, skeletal muscle, and ovary.

Gene expression databases

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    300
  • Mass (Da)
    33,226
  • Last updated
    2007-01-23 v3
  • Checksum
    8D8A9725F7A6D912
MAFLKKYLLTILMVFLAYYYYSANEKFRPEMLQGKKVIVTGASKGIGREIAYHLAKMGAHVVVTARSKEALQKVVARCLELGAASAHYIAGSMEDMTFAEEFVAEAGNLMGGLDMLILNHVLYNRLTFFHGEIDNVRKSMEVNFHSFVVLSVAAMPMLMQSQGSIAVVSSVAGKITYPLIAPYSASKFALDGFFSTLRSEFLVNKVNVSITLCILGLIDTETAIKATSGIYLGPASPKEECALEIIKGTALRQDEMYYVGSRWVPYLLGNPGRKIMEFLSAAEYNWDNVLSNEKLYGRWA

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict22in Ref. 1; AAF01249
Sequence conflict103in Ref. 1; AAF01249

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF188005
EMBL· GenBank· DDBJ
AAF01249.1
EMBL· GenBank· DDBJ
mRNA
AY535424
EMBL· GenBank· DDBJ
AAS47491.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp