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 Q8AVY8


[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 DH12B_XENLA
Primary accession number Q8AVY8
Secondary accession numbers None
Integrated into Swiss-Prot on September 5, 2006
Sequence was last modified on March 1, 2003 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 35)
Name and origin of the protein
Protein name Estradiol 17-beta-dehydrogenase 12-B
Synonyms EC 1.1.1.62
17-beta-hydroxysteroid dehydrogenase 12-B
17-beta-HSD 12-B
Gene name
Name: hsd17b12-B
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=Embryo;
NIH - Xenopus Gene Collection (XGC) project;
Submitted (DEC-2002) 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
BC041194; AAH41194.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001080055.1; -.
UniGene Xl.21849
3D structure databases
ModBase Q8AVY8.
Organism-specific databases
Xenbase XB-FEAT-945228; hsd17b12.
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.
Genome annotation databases
GeneID 379747; -.
KEGG xla:379747; -.
Phylogenomic databases
HOVERGEN Q8AVY8; -.
Other
ProtoNet Q8AVY8.
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-B. PRO_0000248374
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: 34861 Da [This is the MW of the unprocessed precursor] CRC64: A5D8971F8AE72AD0 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAPESLAEVP GCNCFWYLGV VAATWWGLRA AWCLLNGARV WVLGSGAQVG PTIGKWAVVT 

        70         80         90        100        110        120 
GATDGIGKAY AEELARRGMN IVLISRSPEK LEEAAIHIKQ KFKVETKIIA ADFGKPTEIY 

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

       190        200        210        220        230        240 
MLGRGKGVVL NISSASGMYP VPLLTVYSAT KAFVDFFSRG LHAEYRSKGV TVQSVLPFFV 

       250        260        270        280        290        300 
ATKLAKIRKP TWDKPSPETY VRSALNTVGL QTQTNGYLPH AITGWISTSL VPVSAAISMG 

       310 
MKMNKGLRAR FLKKAKQN 

Q8AVY8 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 ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!