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UniProtKB/Swiss-Prot entry O57314

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

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Entry information
Entry name DHB12_ANAPL
Primary accession number O57314
Secondary accession numbers None
Integrated into Swiss-Prot on December 15, 1998
Sequence was last modified on June 1, 1998 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 40)
Name and origin of the protein
Protein name Estradiol 17-beta-dehydrogenase 12
Synonyms EC 1.1.1.62
17-beta-hydroxysteroid dehydrogenase 12
17-beta-HSD 12
Gene name
Name: HSD17B12
Synonyms: SPM2
From
Anas platyrhynchos (Domestic duck) (Anas boschas) [TaxID: 8839] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; Neognathae; Anseriformes; Anatidae; Anas.
Protein existence 2: Evidence at transcript level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Forebrain;
Kimura N., Kurosawa N., Kondo K., Tsukada Y.;
"Molecular cloning of SPM2 from duckling brain: a putative brain specific steroid dehydrogenase and its induction by imprinting stimuli.";
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
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
AB009304; BAA23765.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
ModBase O57314.
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:0004303; Molecular function: estradiol 17-beta-dehydrogenase activity (inferred from electronic annotation from EC).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006694; Biological process: steroid biosynthetic 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.
PR00080; SDRFAMILY.
PROSITE PS00061; ADH_SHORT; 1.
Phylogenomic databases
HOVERGEN O57314; -.
Other
ProtoNet O57314.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Endoplasmic reticulum; Lipid synthesis; Membrane; NADP; Oxidoreductase; Steroid biosynthesis; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   312  312     Estradiol 17-beta-dehydrogenase 12. PRO_0000054577
TRANSMEM   33    53  21     Potential. 
TRANSMEM   181   201  21     Potential. 
TRANSMEM   274   294  21     Potential. 
NP_BIND   48    77  30     NADP (By similarity). 
ACT_SITE   201   201        Proton acceptor (By similarity). 
BINDING   188   188        Substrate (By similarity). 
Sequence information
Length: 312 AA [This is the length of the unprocessed precursor] Molecular weight: 33896 Da [This is the MW of the unprocessed precursor] CRC64: 744D8F44491A9262 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MLPAAGLLWW VGALGALYAA VRGALGLLGA LRVWGIGAGR AALGPGLGAW AVVTGATDGI 

        70         80         90        100        110        120 
GKAYAKELAK RGMKVALISR SKEKLDQVAG EITEQYGVET KVIVADFGER EDIYDRIRAG 

       130        140        150        160        170        180 
LEGLEIGVLV NNVGISYSYP EYFIDVPDLD KTIDKMININ IMSVCKMTRL VLPGMLERSK 

       190        200        210        220        230        240 
GVILNISSAA GMYPTPLLTL YSASKAFVDY FSRGLHAEYK SKGIIVQSVM PYYVATKMSK 

       250        260        270        280        290        300 
ISKPSFDKPT PETYVRAAIG TVGLQSQTNG CLPHAFMGWV FSILPTSTVM NLLMKTNKQI 

       310 
RARFLKKKMK EK
O57314 in FASTA format

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