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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei170 – 1701Substrate
Active sitei183 – 1831Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi41 – 6727NADPAdd
BLAST
Nucleotide bindingi92 – 932NADP
Nucleotide bindingi119 – 1213NADP
Nucleotide bindingi183 – 1875NADP
Nucleotide bindingi216 – 2227NADP

GO - Molecular functioni

  1. 11-beta-hydroxysteroid dehydrogenase (NADP+) activity Source: UniProtKB-EC
  2. 11-beta-hydroxysteroid dehydrogenase [NAD(P)] activity Source: MGI

GO - Biological processi

  1. lung development Source: MGI
  2. 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.
ReactomeiREACT_297756. 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
ProteomesiUP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:103562. Hsd11b1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 76CytoplasmicSequence Analysis
Transmembranei8 – 2417Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini25 – 292268LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
  3. membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 292291Corticosteroid 11-beta-dehydrogenase isozyme 1PRO_0000054621Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi162 – 1621N-linked (GlcNAc...)Sequence Analysis
Glycosylationi207 – 2071N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP50172.
PaxDbiP50172.
PRIDEiP50172.

PTM databases

PhosphoSiteiP50172.

Expressioni

Tissue specificityi

Widely expressed. Highest expression in liver.

Gene expression databases

BgeeiP50172.
CleanExiMM_HSD11B1.
ExpressionAtlasiP50172. baseline and differential.
GenevestigatoriP50172.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

IntActiP50172. 7 interactions.
MINTiMINT-1863132.

Structurei

Secondary structure

1
292
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi29 – 324Combined sources
Beta strandi36 – 416Combined sources
Helixi45 – 5612Combined sources
Beta strandi60 – 634Combined sources
Helixi68 – 8114Combined sources
Beta strandi84 – 885Combined sources
Helixi96 – 11015Combined sources
Beta strandi114 – 1185Combined sources
Helixi133 – 14311Combined sources
Helixi145 – 16117Combined sources
Beta strandi164 – 1707Combined sources
Helixi171 – 1733Combined sources
Helixi181 – 20323Combined sources
Beta strandi209 – 2157Combined sources
Helixi221 – 2277Combined sources
Turni228 – 2303Combined sources
Helixi238 – 25013Combined sources
Beta strandi254 – 2585Combined sources
Helixi264 – 2685Combined sources
Helixi271 – 28010Combined sources
Helixi281 – 2833Combined sources
Helixi286 – 2883Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 25-289.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP50172.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1028.
HOGENOMiHOG000010276.
HOVERGENiHBG005481.
InParanoidiP50172.
KOiK15680.
OMAiGLFMAYY.
OrthoDBiEOG7353X9.
PhylomeDBiP50172.
TreeFamiTF329114.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151F → S in CAA58209 (PubMed:7851387).Curated
Sequence conflicti232 – 2321N → D in CAA58209 (PubMed:7851387).Curated
Sequence conflicti234 – 2341Q → L in CAA58209 (PubMed:7851387).Curated
Sequence conflicti261 – 2611S → L in CAA58209 (PubMed:7851387).Curated

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
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. Positions 25-289.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP50172. 7 interactions.
MINTiMINT-1863132.

Chemistry

BindingDBiP50172.
ChEMBLiCHEMBL3910.

PTM databases

PhosphoSiteiP50172.

Proteomic databases

MaxQBiP50172.
PaxDbiP50172.
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

eggNOGiCOG1028.
HOGENOMiHOG000010276.
HOVERGENiHBG005481.
InParanoidiP50172.
KOiK15680.
OMAiGLFMAYY.
OrthoDBiEOG7353X9.
PhylomeDBiP50172.
TreeFamiTF329114.

Enzyme and pathway databases

BRENDAi1.1.1.146. 3474.
ReactomeiREACT_297756. Glucocorticoid biosynthesis.

Miscellaneous databases

EvolutionaryTraceiP50172.
NextBioi288336.
PROiP50172.
SOURCEiSearch...

Gene expression databases

BgeeiP50172.
CleanExiMM_HSD11B1.
ExpressionAtlasiP50172. baseline and differential.
GenevestigatoriP50172.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamiPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning, sequencing and tissue-distribution of mouse 11 beta-hydroxysteroid dehydrogenase-1 cDNA."
    Rajan V., Chapman K.E., Lyons V., Jamieson P., Mullins J.J., Edwards C.R., Seckl J.R.
    J. Steroid Biochem. Mol. Biol. 52:141-147(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6 X CBA.
    Tissue: Liver.
  2. "Cloning and primary structure of murine 11 beta-hydroxysteroid dehydrogenase/microsomal carbonyl reductase."
    Oppermann U.C.T., Netter K.J., Maser E.
    Eur. J. Biochem. 227:202-208(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Liver.
  3. "The sequence of 5' flanking DNA from the mouse 11 beta-hydroxysteroid dehydrogenase type 1 gene and analysis of putative transcription factor binding sites."
    Voice M.W., Seckl J.R., Chapman K.E.
    Gene 181:233-235(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
  4. "Crystal structure of murine 11 beta-hydroxysteroid dehydrogenase 1: an important therapeutic target for diabetes."
    Zhang J., Osslund T.D., Plant M.H., Clogston C.L., Nybo R.E., Xiong F., Delaney J.M., Jordan S.R.
    Biochemistry 44:6948-6957(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 24-291 IN COMPLEXES WITH NADP AND CORTICOSTERONE, SUBUNIT.

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: April 1, 2015
This is version 131 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

External Data

Dasty 3

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 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.