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Protein

Corticosteroid 11-beta-dehydrogenase isozyme 1

Gene

HSD11B1

Organism
Cavia porcellus (Guinea pig)
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. Catalyzes reversibly the conversion of 7-ketocholesterol to 7-beta-hydroxycholesterol. In intact cells, the reaction runs only in one direction, from 7-ketocholesterol to 7-beta-hydroxycholesterol (By similarity).By similarity1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei170 – 1701SubstrateBy similarity
Active sitei183 – 1831Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi41 – 6727NADP3 PublicationsAdd
BLAST
Nucleotide bindingi92 – 932NADP3 Publications
Nucleotide bindingi119 – 1235NADP3 Publications
Nucleotide bindingi183 – 1875NADP3 Publications
Nucleotide bindingi218 – 2225NADP3 Publications

GO - Molecular functioni

GO - Biological processi

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. 1225.
1.1.1.B40. 1225.
SABIO-RKQ6QLL4.

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
OrganismiCavia porcellus (Guinea pig)
Taxonomic identifieri10141 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia
Proteomesi
  • UP000005447 Componenti: Unassembled WGS sequence

Subcellular locationi

  • Endoplasmic reticulum membrane 1 Publication; Single-pass type II membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 76CytoplasmicSequence analysis
Transmembranei8 – 2417Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini25 – 300276LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 300299Corticosteroid 11-beta-dehydrogenase isozyme 1PRO_0000054618Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Glycoprotein

Expressioni

Tissue specificityi

Widely expressed at low levels. Highest expression in liver.1 Publication

Interactioni

Subunit structurei

Homodimer.3 Publications

Protein-protein interaction databases

STRINGi10141.ENSCPOP00000005042.

Structurei

Secondary structure

1
300
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi29 – 324Combined sources
Beta strandi36 – 416Combined sources
Helixi45 – 5612Combined sources
Beta strandi60 – 667Combined sources
Helixi68 – 8114Combined sources
Beta strandi84 – 907Combined 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 – 2607Combined sources
Helixi264 – 2685Combined sources
Helixi271 – 28111Combined sources
Helixi286 – 2905Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XSEX-ray2.50A/B24-297[»]
3DWFX-ray2.20A/B/C/D24-299[»]
3G49X-ray2.50A/B/C/D24-300[»]
3LZ6X-ray1.84A/B/C/D26-288[»]
ProteinModelPortaliQ6QLL4.
SMRiQ6QLL4. Positions 24-297.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6QLL4.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1205. Eukaryota.
COG1028. LUCA.
GeneTreeiENSGT00840000129712.
HOGENOMiHOG000010276.
HOVERGENiHBG005481.
InParanoidiQ6QLL4.
OMAiGLFMAYY.
OrthoDBiEOG7353X9.
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.

Q6QLL4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFLKKYLLT ILMVFLAYYY YSANEKFRPE MLQGKKVIVT GASKGIGREI
60 70 80 90 100
AYHLAKMGAH VVVTARSKEA LQKVVARCLE LGAASAHYIA GSMEDMTFAE
110 120 130 140 150
EFVAEAGNLM GGLDMLILNH VLYNRLTFFH GEIDNVRKSM EVNFHSFVVL
160 170 180 190 200
SVAAMPMLMQ SQGSIAVVSS VAGKITYPLI APYSASKFAL DGFFSTLRSE
210 220 230 240 250
FLVNKVNVSI TLCILGLIDT ETAIKATSGI YLGPASPKEE CALEIIKGTA
260 270 280 290 300
LRQDEMYYVG SRWVPYLLGN PGRKIMEFLS AAEYNWDNVL SNEKLYGRWA
Length:300
Mass (Da):33,226
Last modified:January 23, 2007 - v3
Checksum:i8D8A9725F7A6D912
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221S → P in AAF01249 (PubMed:10699594).Curated
Sequence conflicti103 – 1031V → A in AAF01249 (PubMed:10699594).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF188005 mRNA. Translation: AAF01249.1.
AY535424 mRNA. Translation: AAS47491.1.
RefSeqiNP_001166328.1. NM_001172857.1.
XP_013012714.1. XM_013157260.1.

Genome annotation databases

EnsembliENSCPOT00000005656; ENSCPOP00000005042; ENSCPOG00000005596.
GeneIDi100135542.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF188005 mRNA. Translation: AAF01249.1.
AY535424 mRNA. Translation: AAS47491.1.
RefSeqiNP_001166328.1. NM_001172857.1.
XP_013012714.1. XM_013157260.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XSEX-ray2.50A/B24-297[»]
3DWFX-ray2.20A/B/C/D24-299[»]
3G49X-ray2.50A/B/C/D24-300[»]
3LZ6X-ray1.84A/B/C/D26-288[»]
ProteinModelPortaliQ6QLL4.
SMRiQ6QLL4. Positions 24-297.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10141.ENSCPOP00000005042.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSCPOT00000005656; ENSCPOP00000005042; ENSCPOG00000005596.
GeneIDi100135542.

Organism-specific databases

CTDi3290.

Phylogenomic databases

eggNOGiKOG1205. Eukaryota.
COG1028. LUCA.
GeneTreeiENSGT00840000129712.
HOGENOMiHOG000010276.
HOVERGENiHBG005481.
InParanoidiQ6QLL4.
OMAiGLFMAYY.
OrthoDBiEOG7353X9.
TreeFamiTF329114.

Enzyme and pathway databases

BRENDAi1.1.1.146. 1225.
1.1.1.B40. 1225.
SABIO-RKQ6QLL4.

Miscellaneous databases

EvolutionaryTraceiQ6QLL4.

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

  1. "Guinea pig 11beta-hydroxysteroid dehydrogenase type 1: primary structure and catalytic properties."
    Pu X., Yang K.
    Steroids 65:148-156(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: Hartley.
    Tissue: Liver.
  2. "Guinea pig 11-beta-hydroxysteroid dehydrogenase type 1: species specific properties."
    Odermatt A., Kadereit B.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The crystal structure of guinea pig 11beta-hydroxysteroid dehydrogenase type 1 provides a model for enzyme-lipid bilayer interactions."
    Ogg D., Elleby B., Norstroem C., Stefansson K., Abrahmsen L., Oppermann U., Svensson S.
    J. Biol. Chem. 280:3789-3794(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 25-297 IN COMPLEX WITH NADP, HOMODIMERIZATION.
  4. "N-(Pyridin-2-yl) arylsulfonamide inhibitors of 11beta-hydroxysteroid dehydrogenase type 1: Discovery of PF-915275."
    Siu M., Johnson T.O., Wang Y., Nair S.K., Taylor W.D., Cripps S.J., Matthews J.J., Edwards M.P., Pauly T.A., Ermolieff J., Castro A., Hosea N.A., LaPaglia A., Fanjul A.N., Vogel J.E.
    Bioorg. Med. Chem. Lett. 19:3493-3497(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 24-300 IN COMPLEX WITH NADP AND SYNTHETIC INHIBITOR.
  5. "Mutations of key hydrophobic surface residues of 11 beta-hydroxysteroid dehydrogenase type 1 increase solubility and monodispersity in a bacterial expression system."
    Lawson A.J., Walker E.A., White S.A., Dafforn T.R., Stewart P.M., Ride J.P.
    Protein Sci. 18:1552-1563(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 24-299 IN COMPLEX WITH NADP.

Entry informationi

Entry nameiDHI1_CAVPO
AccessioniPrimary (citable) accession number: Q6QLL4
Secondary accession number(s): Q9QZE1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 92 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.