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Protein

Corticosteroid 11-beta-dehydrogenase isozyme 1

Gene

Hsd11b1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

  • lung development Source: MGI
  • steroid metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lipid metabolism, Steroid metabolism

Keywords - Ligandi

NADP

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:103562. Hsd11b1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 7CytoplasmicSequence analysis6
Transmembranei8 – 24Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST17
Topological domaini25 – 292LumenalSequence analysisAdd BLAST268

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3910.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000546212 – 292Corticosteroid 11-beta-dehydrogenase isozyme 1Add BLAST291

Amino acid modifications

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

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP50172.
PeptideAtlasiP50172.
PRIDEiP50172.

PTM databases

iPTMnetiP50172.
PhosphoSitePlusiP50172.

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.
MINTiMINT-1863132.
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[»]
ProteinModelPortaliP50172.
SMRiP50172.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP50172.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1205. Eukaryota.
COG1028. LUCA.
GeneTreeiENSGT00860000133821.
HOGENOMiHOG000010276.
HOVERGENiHBG005481.
InParanoidiP50172.
KOiK15680.
OMAiSLRHEFI.
OrthoDBiEOG091G0H0R.
PhylomeDBiP50172.
TreeFamiTF329114.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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.

Cross-referencesi

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.

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[»]
ProteinModelPortaliP50172.
SMRiP50172.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP50172. 7 interactors.
MINTiMINT-1863132.
STRINGi10090.ENSMUSP00000016338.

Chemistry databases

BindingDBiP50172.
ChEMBLiCHEMBL3910.

PTM databases

iPTMnetiP50172.
PhosphoSitePlusiP50172.

Proteomic databases

PaxDbiP50172.
PeptideAtlasiP50172.
PRIDEiP50172.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3290.
MGIiMGI:103562. Hsd11b1.

Phylogenomic databases

eggNOGiKOG1205. Eukaryota.
COG1028. LUCA.
GeneTreeiENSGT00860000133821.
HOGENOMiHOG000010276.
HOVERGENiHBG005481.
InParanoidiP50172.
KOiK15680.
OMAiSLRHEFI.
OrthoDBiEOG091G0H0R.
PhylomeDBiP50172.
TreeFamiTF329114.

Enzyme and pathway databases

BRENDAi1.1.1.146. 3474.
ReactomeiR-MMU-194002. Glucocorticoid biosynthesis.

Miscellaneous databases

EvolutionaryTraceiP50172.
PROiP50172.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000016194.
CleanExiMM_HSD11B1.
ExpressionAtlasiP50172. baseline and differential.
GenevisibleiP50172. MM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
IPR002347. SDR_fam.
[Graphical view]
PANTHERiPTHR24322. PTHR24322. 2 hits.
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDHI1_MOUSE
AccessioniPrimary (citable) accession number: P50172
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 146 of the entry and version 3 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.