ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P51975

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name DHI1_SHEEP
Primary accession number P51975
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 59)
Name and origin of the protein
Protein name Corticosteroid 11-beta-dehydrogenase isozyme 1
Synonyms EC 1.1.1.146
11-beta-hydroxysteroid dehydrogenase 1
11-beta-HSD1
11-DH
Gene name
Name: HSD11B1
From
Ovis aries (Sheep) [TaxID: 9940] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Caprinae; Ovis.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
DOI=10.1210/en.131.5.2120; PubMed=1425412 [NCBI, ExPASy, EBI, Israel, Japan]
Yang K., Smith C.L., Dales D., Hammond G.L., Challis J.R.;
"Cloning of an ovine 11 beta-hydroxysteroid dehydrogenase complementary deoxyribonucleic acid: tissue and temporal distribution of its messenger ribonucleic acid during fetal and neonatal development.";
Endocrinology 131:2120-2126(1992).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X69561; CAA49290.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S33117; S33117.
RefSeq NP_001009395.1; -.
UniGene Oar.418
3D structure databases
SMR P51975; 23-288, 24-289.
ModBase P51975.
Ontologies
GO
GO:0005789; Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005488; Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0016491; Molecular function: oxidoreductase activity (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0008202; Biological process: steroid metabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR002198; DHase_sc/Rdtase_SDR.
IPR002347; Glc/ribitol_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
PANTHER PTHR19410; ADH_short_C2; 1.
Pfam PF00106; adh_short; 1.
Pfam graphical view of domain structure.
PRINTS PR00081; GDHRDH.
PROSITE PS00061; ADH_SHORT; 1.
Genome annotation databases
GeneID 443409; -.
Phylogenomic databases
HOVERGEN P51975; -.
Other
ProtoNet P51975.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Endoplasmic reticulum; Glycoprotein; Lipid metabolism; Membrane; NADP; Oxidoreductase; Signal-anchor; Steroid metabolism; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   292  291     Corticosteroid 11-beta-dehydrogenase isozyme 1. PRO_0000054625
TOPO_DOM   2     7  6     Cytoplasmic (Potential). 
TRANSMEM   8    24  17     Signal-anchor for type II membrane protein (Potential). 
TOPO_DOM   25   292  268     Lumenal (Potential). 
NP_BIND   34    63  30     NADP (By similarity). 
ACT_SITE   183   183        Proton acceptor (By similarity). 
BINDING   170   170        Substrate (By similarity). 
CARBOHYD   95    95        N-linked (GlcNAc...) (Potential). 
CARBOHYD   207   207        N-linked (GlcNAc...) (Potential). 
Sequence information
Length: 292 AA [This is the length of the unprocessed precursor] Molecular weight: 32154 Da [This is the MW of the unprocessed precursor] CRC64: ADBD024E73EB95E3 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MAFMKKYLLP ILGIFLAYYY YSANEEFRPE MLRGKRVIVT GASKGIGREM AYHLARMGAH 

        70         80         90        100        110        120 
VVVTARSEES LKKVVSRCLE LGAASAHYVA GTMENMTFAE QFVAKAGELV GGLDMLILNH 

       130        140        150        160        170        180 
INYTPLRVFS NDIHLLRRSL EVNLLSYVVL STAALPMLKQ TSGSIVVVSS VAGKIACPLA 

       190        200        210        220        230        240 
AAYSASKFAL DGFFSSLRTE YEATKVNVSI TLCILGLIDT DTAMKAVAGI YNAEASPKEE 

       250        260        270        280        290 
CALEIIKGGA LRQDEVYYDN SILTSLLLKN PGRKIMEFLS LKKYNMERFI NN
P51975 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by au flag APAF Australia Mirror sites: Brazil Canada China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!