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Reviewed, UniProtKB/Swiss-Prot Q6P3L6 (DH12A_DANRE)

Last modified November 25, 2008. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Estradiol 17-beta-dehydrogenase 12-A
    EC=1.1.1.62
Alternative name(s):
    17-beta-hydroxysteroid dehydrogenase 12-A
      Short name=17-beta-HSD 12-A
      Short name=zfHSD17B12A
      Short name=zf3.1
Gene names
Name: hsd17b12a
ORF Names: zgc:55589
OrganismDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length319 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Catalyzes the transformation of estrone (E1) into estradiol (E2), suggesting a central role in estrogen formation By similarity.

Catalytic activity

Estradiol-17-beta + NAD(P)(+) = estrone + NAD(P)H.

Pathway

Steroid biosynthesis; estrogen biosynthesis.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane proteinBy similarity.

Developmental stage

Expressed throughout development. Weakly expressed during early developmental stages from shield to tailbud. Ref.1

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family. 17-beta-HSD 3 subfamily.

Ontologies

Keywords

   Biological processLipid synthesis
Steroid biosynthesis
   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
   LigandNADP
   Molecular functionOxidoreductase

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

steroid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionbinding

Inferred from electronic annotation. Source: InterPro

estradiol 17-beta-dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 319319Estradiol 17-beta-dehydrogenase 12-A
PRO_0000248371

Regions

Transmembrane17 – 3721 Potential
Transmembrane188 – 20821 Potential
Transmembrane282 – 30221 Potential
Nucleotide binding56 – 8530NADP By similarity

Sites

Active site2081Proton acceptor By similarity
Binding site1951Substrate By similarity

Experimental info

Sequence conflict1871K → E in AAH48053. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q6P3L6-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: BA0892BF0B7A82C8

FASTA31935,551
        10         20         30         40         50         60 
MESFNVVETL QPAERALFWV GALITASLAL YVVYKTITGF RIWVLGNGDL LSPKLGKWAV 

        70         80         90        100        110        120 
VTGATDGIGK SYAEELARRG FSMMLISRSQ EKLDDVAKSL ESTYKVETKT IAVDFSQIDV 

       130        140        150        160        170        180 
YPKIEKGLAG LEIGILVNNV GISYSYPEFF LHIPDLENFI TTMINVNITS VCQMTRLVLP 

       190        200        210        220        230        240 
RMEARAKGVI LNISSASGMF PVPLLTIYSS TKAFVDFFSR GLQTEYKCKG IIIQSVLPFF 

       250        260        270        280        290        300 
VATKMTKIRK PTLDKPTPER YVAAELNTVG LQDQTNGYFP HAVMGWVTTI LAPIDLVLNL 

       310 
GLRMNKAQRG GYLRRRKLR 

« Hide

References

« Hide 'large scale' references
[1]"Identification and characterization of 17 beta-hydroxysteroid dehydrogenases in the zebrafish, Danio rerio."
Mindnich R., Deluca D., Adamski J.
Mol. Cell. Endocrinol. 215:19-30(2004) [PubMed: 15026171] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
[2]NIH - Zebrafish Gene Collection (ZGC) project
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: AB.

Cross-references

Sequence databases

AY551082 mRNA. Translation: AAS58452.1.
BC048053 mRNA. Translation: AAH48053.1.
BC063943 mRNA. Translation: AAH63943.1.
RefSeqNP_957175.1.
UniGeneDr.29406

3D structure databases

ModBaseSearch...

Genome annotation databases

EnsemblENSDARG00000015709. Danio rerio. [Contig view]
GeneID327417.
KEGGdre:327417.

Organism-specific databases

ZFINZDB-GENE-030131-5628. hsd17b12a.

Phylogenomic databases

HOVERGENQ6P3L6.

Gene expression databases

ArrayExpressQ6P3L6.

Family and domain databases

InterProIPR002198. DHase_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DHase.
IPR016040. NAD(P)-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR19410. ADH_short_C2. 1 hit.
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDH12A_DANRE
AccessionPrimary (citable) accession number: Q6P3L6
Secondary accession number(s): Q7ZUN4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: July 5, 2004
Last modified: November 25, 2008
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectZebrafish annotation project

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents