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UniProtKB/Swiss-Prot entry Q5XG41


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

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Entry information
Entry name DH12A_XENLA
Primary accession number Q5XG41
Secondary accession numbers None
Integrated into Swiss-Prot on September 5, 2006
Sequence was last modified on November 23, 2004 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 31)
Name and origin of the protein
Protein name Estradiol 17-beta-dehydrogenase 12-A
Synonyms EC 1.1.1.62
17-beta-hydroxysteroid dehydrogenase 12-A
17-beta-HSD 12-A
Gene name
Name: hsd17b12-A
From
Xenopus laevis (African clawed frog) [TaxID: 8355] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
NIH - Xenopus Gene Collection (XGC) project;
Submitted (OCT-2004) 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
BC084629; AAH84629.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001088370.1; -.
UniGene Xl.19362
3D structure databases
ModBase Q5XG41.
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.
ProtoNet Q5XG41.
Genome annotation databases
GeneID 495218; -.
KEGG xla:495218; -.
Phylogenomic databases
HOVERGEN Q5XG41; -.
Other
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   318  318     Estradiol 17-beta-dehydrogenase 12-A. PRO_0000248373
TRANSMEM   15    35  21     Potential. 
TRANSMEM   187   207  21     Potential. 
TRANSMEM   281   301  21     Potential. 
NP_BIND   54    83  30     NADP (By similarity). 
ACT_SITE   207   207        Proton acceptor (By similarity). 
BINDING   194   194        Substrate (By similarity). 
Sequence information
Length: 318 AA [This is the length of the unprocessed precursor] Molecular weight: 34994 Da [This is the MW of the unprocessed precursor] CRC64: 87D46FD9D88A2F6A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAPESLVEVP GCNCFWYLGV LAAAWWGLRA ACCLLNGARA WVLGSGAQVG PRIGKWAVVT 

        70         80         90        100        110        120 
GATDGIGKAY AEELARRGMS IVLISRSPEK LDEAAKHIKE TFKVETKIIA ADFGKPTEIY 

       130        140        150        160        170        180 
ERIEAGLRDL EIGVLVNNVG VSYEYPEYFL EIPDLENTLD KMININIMSV CQMTRLVLPG 

       190        200        210        220        230        240 
MLGRGKGVIL NISSASGMYP VPLLTVYSAT KAFVDFFSRG LHAEYRNKGI NVQSVLPFYV 

       250        260        270        280        290        300 
ATKLAKIRKP TWDKPSPETY VRSAVNTVGL QTQTNGYLPH AIMGWISTSL VPVSVAISMG 

       310 
MKMNKGLRSR FLKRKKQK 

Q5XG41 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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