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Protein

Corticosteroid 11-beta-dehydrogenase isozyme 1

Gene

Hsd11b1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes reversibly the conversion of cortisol to the inactive metabolite cortisone.

Catalytic activityi

An 11-beta-hydroxysteroid + NADP+ = an 11-oxosteroid + NADPH.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei170Substrate1
Active sitei183Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi41 – 67NADPAdd BLAST27
Nucleotide bindingi92 – 93NADP2
Nucleotide bindingi119 – 121NADP3
Nucleotide bindingi183 – 187NADP5
Nucleotide bindingi216 – 222NADP7

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processLipid metabolism, Steroid metabolism
LigandNADP

Enzyme and pathway databases

BRENDAi1.1.1.146 3474
ReactomeiR-MMU-194002 Glucocorticoid biosynthesis

Names & Taxonomyi

Protein namesi
Recommended name:
Corticosteroid 11-beta-dehydrogenase isozyme 1 (EC:1.1.1.146)
Alternative name(s):
11-beta-hydroxysteroid dehydrogenase 1
Short name:
11-DH
Short name:
11-beta-HSD1
11beta-HSD1A
Gene namesi
Name:Hsd11b1
Synonyms:Hsd11
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:103562 Hsd11b1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 7CytoplasmicSequence analysis7
Transmembranei8 – 24Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST17
Topological domaini25 – 292LumenalSequence analysisAdd BLAST268

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3910

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000546211 – 292Corticosteroid 11-beta-dehydrogenase isozyme 1Add BLAST292

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi162N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi207N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP50172
PeptideAtlasiP50172
PRIDEiP50172

PTM databases

iPTMnetiP50172
PhosphoSitePlusiP50172
SwissPalmiP50172

Expressioni

Tissue specificityi

Widely expressed. Highest expression in liver.

Gene expression databases

BgeeiENSMUSG00000016194
CleanExiMM_HSD11B1
ExpressionAtlasiP50172 baseline and differential
GenevisibleiP50172 MM

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

IntActiP50172, 7 interactors
MINTiP50172
STRINGi10090.ENSMUSP00000016338

Chemistry databases

BindingDBiP50172

Structurei

Secondary structure

1292
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi29 – 32Combined sources4
Beta strandi36 – 41Combined sources6
Helixi45 – 56Combined sources12
Beta strandi60 – 63Combined sources4
Helixi68 – 81Combined sources14
Beta strandi84 – 88Combined sources5
Helixi96 – 110Combined sources15
Beta strandi114 – 118Combined sources5
Helixi133 – 143Combined sources11
Helixi145 – 161Combined sources17
Beta strandi164 – 170Combined sources7
Helixi171 – 173Combined sources3
Helixi181 – 203Combined sources23
Beta strandi209 – 215Combined sources7
Helixi221 – 227Combined sources7
Turni228 – 230Combined sources3
Helixi238 – 250Combined sources13
Beta strandi254 – 258Combined sources5
Helixi264 – 268Combined sources5
Helixi271 – 280Combined sources10
Helixi281 – 283Combined sources3
Helixi286 – 288Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y5MX-ray2.30A/B24-292[»]
1Y5RX-ray3.00A/B24-292[»]
3GMDX-ray2.28A/B/C/D/E/F/G/H26-289[»]
4K26X-ray2.21A/B24-292[»]
4NMHX-ray2.90A/B/C/D24-292[»]
5PGZX-ray2.90A/B24-292[»]
ProteinModelPortaliP50172
SMRiP50172
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP50172

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1205 Eukaryota
COG1028 LUCA
GeneTreeiENSGT00880000138008
HOGENOMiHOG000010276
HOVERGENiHBG005481
InParanoidiP50172
KOiK15680
OMAiIGREMAY
OrthoDBiEOG091G0H0R
PhylomeDBiP50172
TreeFamiTF329114

Family and domain databases

InterProiView protein in InterPro
IPR036291 NAD(P)-bd_dom_sf
IPR020904 Sc_DH/Rdtase_CS
IPR002347 SDR_fam
PfamiView protein in Pfam
PF00106 adh_short, 1 hit
PRINTSiPR00081 GDHRDH
SUPFAMiSSF51735 SSF51735, 1 hit
PROSITEiView protein in PROSITE
PS00061 ADH_SHORT, 1 hit

Sequencei

Sequence statusi: Complete.

P50172-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVMKNYLLP ILVLFLAYYY YSTNEEFRPE MLQGKKVIVT GASKGIGREM
60 70 80 90 100
AYHLSKMGAH VVLTARSEEG LQKVVSRCLE LGAASAHYIA GTMEDMTFAE
110 120 130 140 150
QFIVKAGKLM GGLDMLILNH ITQTSLSLFH DDIHSVRRVM EVNFLSYVVM
160 170 180 190 200
STAALPMLKQ SNGSIAVISS LAGKMTQPMI APYSASKFAL DGFFSTIRTE
210 220 230 240 250
LYITKVNVSI TLCVLGLIDT ETAMKEISGI INAQASPKEE CALEIIKGTA
260 270 280 290
LRKSEVYYDK SPLTPILLGN PGRKIMEFFS LRYYNKDMFV SN
Length:292
Mass (Da):32,364
Last modified:January 23, 2007 - v3
Checksum:iADE42B11D82DD6CD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti15F → S in CAA58209 (PubMed:7851387).Curated1
Sequence conflicti232N → D in CAA58209 (PubMed:7851387).Curated1
Sequence conflicti234Q → L in CAA58209 (PubMed:7851387).Curated1
Sequence conflicti261S → L in CAA58209 (PubMed:7851387).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S75207 mRNA Translation: AAB33601.1
X83202 mRNA Translation: CAA58209.1
X92186 Genomic DNA Translation: CAA63096.1
CCDSiCCDS15635.1
PIRiI56604
RefSeqiNP_001038216.1, NM_001044751.1
NP_032314.2, NM_008288.2
UniGeneiMm.28328

Genome annotation databases

EnsembliENSMUST00000016338; ENSMUSP00000016338; ENSMUSG00000016194
ENSMUST00000161737; ENSMUSP00000125620; ENSMUSG00000016194
GeneIDi15483
KEGGimmu:15483
UCSCiuc007eef.1 mouse

Similar proteinsi

Entry informationi

Entry nameiDHI1_MOUSE
AccessioniPrimary (citable) accession number: P50172
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: June 20, 2018
This is version 156 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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