Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot O54753 (H17B6_RAT)

Last modified November 25, 2008. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
    Hydroxysteroid 17-beta dehydrogenase 6
    EC=1.1.1.62
    EC=1.1.1.63
    EC=1.1.1.105
Alternative name(s):
    17-beta-HSD6
    Oxidative 3-alpha hydroxysteroid dehydrogenase
    3-alpha->beta-hydroxysteroid epimerase
      Short name=3-alpha->beta-HSE
Gene names
Name: Hsd17b6
Synonyms: Hsd17b9
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

NAD-dependent oxidoreductase with broad substrate specificity that shows both oxidative and reductive activity (in vitro). Has retinol dehydrogenase activity towards all-trans-retinol (in vitro) By similarity. Has 17-beta-hydroxysteroid dehydrogenase activity towards various steroids (in vitro). Converts 5-alpha-androstan-3-alpha,17-beta-diol to androsterone and estradiol to estrone (in vitro). Has 3-alpha-hydroxysteroid dehydrogenase activity towards androsterone (in vitro).

Catalytic activity

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

Testosterone + NAD(+) = androst-4-ene-3,17-dione + NADH.

Retinol + NAD(+) = retinal + NADH.

Enzyme regulation

Competitively inhibited by 9-cis-retinoic ancid and 13-cis-retinoic acid.

Subcellular location

Microsome membrane; Peripheral membrane protein; Lumenal sideBy similarity. Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal sideBy similarity.

Tissue specificity

Detected in prostate, liver and kidney.

Induction

Up-regulated by testosterone. Levels are very low in castrated male rats.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Biophysicochemical properties

Kinetic parameters:

Vmax was measured using transfected cell lysates.

KM=0.1 µM for 5-alpha-androstan-3-alpha,17-beta-diol

KM=0.2 µM for androsterone

KM=0.5 µM for dihydrotestosterone

KM=1.1 µM for testosterone

KM=0.8 µM for estradiol

KM=3 µM for NAD

KM=1 mM for NADP

Vmax=2.5 nmol/min/mg enzyme for 5-alpha-androstan-3-alpha,17-beta-diol

Vmax=0.1 nmol/min/mg enzyme for androsterone

Vmax=0.5 nmol/min/mg enzyme for dihydrotestosterone

Vmax=1.1 nmol/min/mg enzyme for testosterone

Vmax=2.1 nmol/min/mg enzyme for estradiol

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 317300Hydroxysteroid 17-beta dehydrogenase 6
PRO_0000303213

Regions

Nucleotide binding33 – 5725NAD By similarity

Sites

Active site1761Proton acceptor By similarity
Binding site1641Substrate Potential

Amino acid modifications

Glycosylation1611N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2191I → S in AAB88253. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O54753-1 [UniParc].

Last modified September 11, 2007. Version 2.
Checksum: 4AB3F3160C6675A9

FASTA31736,145
        10         20         30         40         50         60 
MWFYLVTLVG LYYLLRWYRE RQVVSHLHDK YVFITGCDSG FGNLLARQLD RRGMRVLAAC 

        70         80         90        100        110        120 
LTEKGAEELK SKTSDRLETV ILDVTNTDSI SAATQWVKEH VGDKGLWGLV NNAGVFQAFA 

       130        140        150        160        170        180 
YIEWCRPEDC MSIFQVNLIG LAQVTLSMLF LVKKARGRIV NVSSVLGRVA LFGGFYSCSK 

       190        200        210        220        230        240 
YGVEAFSDVL RREIRDFGVK VSIIEPGSFK TRMTDAELII EKTKKTWEAT PEHIRESYGQ 

       250        260        270        280        290        300 
QFFDDFCNTT RRELKKCSTN LSLVTDCMEH ALTSKYPRTR YSAGWDARLF FIPLSYLPTS 

       310 
LVDCLLAISR RKPAQAV 

« Hide

References

« Hide 'large scale' references
[1]"Expression cloning and characterization of oxidative 17beta- and 3alpha-hydroxysteroid dehydrogenases from rat and human prostate."
Biswas M.G., Russell D.W.
J. Biol. Chem. 272:15959-15966(1997) [PubMed: 9188497] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, INDUCTION, TISSUE SPECIFICITY.
Tissue: Prostate.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.

Cross-references

Sequence databases

U89280 mRNA. Translation: AAB88253.1. Different initiation.
BC088104 mRNA. Translation: AAH88104.1. Different initiation.
BC091114 mRNA. Translation: AAH91114.1. Different initiation.
RefSeqNP_775427.1.
UniGeneRn.10857

3D structure databases

HSSPHSSP built from PDB template 1FDS based on UniProtKB P14061.
ModBaseSearch...

Genome annotation databases

EnsemblENSRNOG00000007758. Rattus norvegicus. [Contig view]
GeneID286964.
KEGGrno:286964.

Organism-specific databases

RGD708343. Hsd17b6.

Phylogenomic databases

HOVERGENO54753.

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...

Other Resources

NextBio625175.

Entry information

Entry nameH17B6_RAT
AccessionPrimary (citable) accession number: O54753
Secondary accession number(s): Q5M8C8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: November 25, 2008
This is version 50 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

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