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Protein

Corticosteroid 11-beta-dehydrogenase isozyme 1

Gene

Hsd11b1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes reversibly the conversion of corticosterone to 11-dehydrocorticosterone.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei166 – 1661SubstrateBy similarity
Active sitei179 – 1791Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi37 – 6327NADPBy similarityAdd
BLAST
Nucleotide bindingi88 – 892NADPBy similarity
Nucleotide bindingi115 – 1173NADPBy similarity
Nucleotide bindingi179 – 1835NADPBy similarity
Nucleotide bindingi212 – 2187NADPBy similarity

GO - Molecular functioni

  • 11-beta-hydroxysteroid dehydrogenase (NADP+) activity Source: UniProtKB-EC
  • 11-beta-hydroxysteroid dehydrogenase [NAD(P)] activity Source: RGD
  • NADP binding Source: RGD
  • steroid binding Source: RGD

GO - Biological processi

  • cellular response to estradiol stimulus Source: RGD
  • glucocorticoid biosynthetic process Source: RGD
  • glucocorticoid catabolic process Source: RGD
  • phthalate metabolic process Source: RGD
  • regulation of pentose-phosphate shunt Source: RGD
  • response to nutrient levels Source: RGD
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. 5301.
SABIO-RKP16232.

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
Gene namesi
Name:Hsd11b1
Synonyms:Hsd11
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 13

Organism-specific databases

RGDi2834. Hsd11b1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44CytoplasmicSequence analysis
Transmembranei5 – 2016Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini21 – 288268LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

  • apical part of cell Source: RGD
  • cytoplasm Source: RGD
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • intracellular membrane-bounded organelle Source: RGD
  • nuclear membrane Source: RGD
  • rough endoplasmic reticulum Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi110 – 1101D → N: Slight loss of activity.
Mutagenesisi179 – 1791Y → F or S: Complete loss of activity. 1 Publication
Mutagenesisi183 – 1831K → R: Complete loss of activity. 1 Publication

Chemistry

ChEMBLiCHEMBL2391.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 288288Corticosteroid 11-beta-dehydrogenase isozyme 1PRO_0000054623Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi158 – 1581N-linked (GlcNAc...)Sequence analysis
Glycosylationi203 – 2031N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Glycosylated.

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiP16232.

PTM databases

iPTMnetiP16232.

Expressioni

Tissue specificityi

Liver, kidney, testis and placenta.

Developmental stagei

Expression of both isoforms is found in 1 week-old rats. Expression increases exponentially up to 4 weeks but after this time there is no further increase up to 16 weeks.

Gene expression databases

ExpressionAtlasiP16232. baseline and differential.
GenevisibleiP16232. RN.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

MINTiMINT-4580128.

Chemistry

BindingDBiP16232.

Structurei

3D structure databases

ProteinModelPortaliP16232.
SMRiP16232. Positions 21-285.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00780000121888.
HOGENOMiHOG000010276.
HOVERGENiHBG005481.
InParanoidiP16232.
KOiK15680.
OMAiFIDTESA.
PhylomeDBiP16232.

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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative promoter usage. AlignAdd to basket

Isoform 11-HSD1A (identifier: P16232-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKKYLLPVLV LCLGYYYSTN EEFRPEMLQG KKVIVTGASK GIGREMAYHL
60 70 80 90 100
SKMGAHVVLT ARSEEGLQKV VSRCLELGAA SAHYIAGTME DMAFAERFVV
110 120 130 140 150
EAGKLLGGLD MLILNHITQT TMSLFHDDIH SVRRSMEVNF LSYVVLSTAA
160 170 180 190 200
LPMLKQSNGS IAIISSMAGK MTQPLIASYS ASKFALDGFF STIRKEHLMT
210 220 230 240 250
KVNVSITLCV LGFIDTETAL KETSGIILSQ AAPKEECALE IIKGTVLRKD
260 270 280
EVYYDKSSWT PLLLGNPGRR IMEFLSLRSY NRDLFVSN
Length:288
Mass (Da):31,883
Last modified:October 10, 2002 - v2
Checksum:iAC445C0D92004808
GO
Isoform 11-HSD1B (identifier: P16232-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: Missing.

Note: Kidney-specific.
Show »
Length:262
Mass (Da):28,732
Checksum:i22616268BA4DF8C9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311K → N in CAA71447 (PubMed:10906322).Curated
Sequence conflicti235 – 2351E → Q in AAA40886 (PubMed:2808402).Curated
Sequence conflicti241 – 2411Missing in AAA40886 (PubMed:2808402).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2626Missing in isoform 11-HSD1B. CuratedVSP_012616Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05107 mRNA. Translation: AAA40886.1.
BC078865 mRNA. Translation: AAH78865.1.
S43333 Genomic DNA. Translation: AAB22993.1.
Y10420 Genomic DNA. Translation: CAA71447.1.
M77835 mRNA. Translation: AAA40600.1.
PIRiA34430. DXRTBH.
RefSeqiNP_058776.2. NM_017080.2. [P16232-1]
XP_006250535.1. XM_006250473.2. [P16232-1]
UniGeneiRn.231830.
Rn.888.

Genome annotation databases

EnsembliENSRNOT00000007870; ENSRNOP00000007870; ENSRNOG00000005861. [P16232-1]
GeneIDi25116.
KEGGirno:25116.

Keywords - Coding sequence diversityi

Alternative promoter usage

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05107 mRNA. Translation: AAA40886.1.
BC078865 mRNA. Translation: AAH78865.1.
S43333 Genomic DNA. Translation: AAB22993.1.
Y10420 Genomic DNA. Translation: CAA71447.1.
M77835 mRNA. Translation: AAA40600.1.
PIRiA34430. DXRTBH.
RefSeqiNP_058776.2. NM_017080.2. [P16232-1]
XP_006250535.1. XM_006250473.2. [P16232-1]
UniGeneiRn.231830.
Rn.888.

3D structure databases

ProteinModelPortaliP16232.
SMRiP16232. Positions 21-285.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4580128.

Chemistry

BindingDBiP16232.
ChEMBLiCHEMBL2391.

PTM databases

iPTMnetiP16232.

Proteomic databases

PRIDEiP16232.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000007870; ENSRNOP00000007870; ENSRNOG00000005861. [P16232-1]
GeneIDi25116.
KEGGirno:25116.

Organism-specific databases

CTDi3290.
RGDi2834. Hsd11b1.

Phylogenomic databases

GeneTreeiENSGT00780000121888.
HOGENOMiHOG000010276.
HOVERGENiHBG005481.
InParanoidiP16232.
KOiK15680.
OMAiFIDTESA.
PhylomeDBiP16232.

Enzyme and pathway databases

BRENDAi1.1.1.146. 5301.
SABIO-RKP16232.

Miscellaneous databases

NextBioi605481.
PROiP16232.

Gene expression databases

ExpressionAtlasiP16232. baseline and differential.
GenevisibleiP16232. RN.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of rat cDNA encoding corticosteroid 11 beta-dehydrogenase."
    Agarwal A.K., Monder C., Eckstein B., White P.C.
    J. Biol. Chem. 264:18939-18943(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 11-HSD1A).
    Tissue: Liver.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  3. "Differential promoter usage by the rat 11 beta-hydroxysteroid dehydrogenase gene."
    Moisan M.P., Edwards C.R., Seckl J.R.
    Mol. Endocrinol. 6:1082-1087(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 1-69 (ISOFORMS 11-HSD1A AND 11-HSD1B), ALTERNATIVE PROMOTER USAGE.
  4. "C/EBP regulates hepatic transcription of 11beta-hydroxysteroid dehydrogenase type 1. A novel mechanism for cross-talk between the C/EBP and glucocorticoid signaling pathways."
    Williams L.J.S., Lyons V., MacLeod I., Rajan V., Darlington G.J., Poli V., Seckl J.R., Chapman K.E.
    J. Biol. Chem. 275:30232-30239(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69 (ISOFORM 11-HSD1A).
    Strain: Sprague-Dawley.
  5. "Purification of full-length recombinant human and rat type 1 11beta-hydroxysteroid dehydrogenases with retained oxidoreductase activities."
    Nobel C.S.I., Dunas F., Abrahmsen L.B.
    Protein Expr. Purif. 26:349-356(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 21-273.
  6. "Tissue-specific expression of an 11 beta-hydroxysteroid dehydrogenase with a truncated N-terminal domain. A potential mechanism for differential intracellular localization within mineralocorticoid target cells."
    Krozowski Z., Obeyesekere V., Smith R., Mercer W.
    J. Biol. Chem. 267:2569-2574(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 11-HSD1A AND 11-HSD1B), ALTERNATIVE PROMOTER USAGE.
    Strain: Sprague-Dawley.
    Tissue: Kidney.
  7. "The syndrome of apparent mineralocorticoid excess: its association with 11 beta-dehydrogenase and 5 beta-reductase deficiency and some consequences for corticosteroid metabolism."
    Monder C., Shackleton C.H.L., Bradlow H.L., New M.I., Stoner E., Iohan F., Lakshmi V.
    J. Clin. Endocrinol. Metab. 63:550-557(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-40.
  8. "Tyr-179 and Lys-183 are essential for enzymatic activity of 11 beta-hydroxysteroid dehydrogenase."
    Obeid J., White P.C.
    Biochem. Biophys. Res. Commun. 188:222-227(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-179 AND LYS-183.

Entry informationi

Entry nameiDHI1_RAT
AccessioniPrimary (citable) accession number: P16232
Secondary accession number(s): O09170, Q6LDH6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: October 10, 2002
Last modified: April 13, 2016
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.