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O14756 (H17B6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
17-beta-hydroxysteroid dehydrogenase type 6

Short name=17-beta-HSD 6
Short name=17-beta-HSD6
EC=1.1.1.105
EC=1.1.1.239
EC=1.1.1.62
Alternative name(s):
3-alpha->beta-hydroxysteroid epimerase
Short name=3-alpha->beta-HSE
Oxidative 3-alpha hydroxysteroid dehydrogenase
Gene names
Name:HSD17B6
Synonyms:RODH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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 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). Has retinol dehydrogenase activity towards all-trans-retinol (in vitro). Can convert androsterone to epi-androsterone. Androsterone is first oxidized to 5-alpha-androstane-3,17-dione and then reduced to epi-andosterone. Can act on both C-19 and C-21 3-alpha-hydroxysteroids. Ref.2 Ref.4 Ref.5

Catalytic activity

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

Testosterone + NAD+ = androstenedione + NADH.

All-trans-retinol-[cellular-retinol-binding-protein] + NAD+ = all-trans-retinal-[cellular-retinol-binding-protein] + NADH.

Subcellular location

Microsome membrane; Peripheral membrane protein; Lumenal side. Early endosome membrane; Peripheral membrane protein; Lumenal side Potential Ref.4.

Tissue specificity

Detected in liver and prostate (at protein level). Detected in adult liver, lung, brain, placenta, prostate, adrenal gland, testis, mammary gland, spleen, spinal cord and uterus. Detected in caudate nucleus, and at lower levels in amygdala, corpus callosum, hippocampus, substantia nigra and thalamus. Detected in fetal lung, liver and brain. Ref.1 Ref.2

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

The kinetic parameters were determined using microsomes from transfected cells.

KM=0.19 µM for NAD Ref.2 Ref.4

KM=0.18 µM for NADH

KM=54 µM for NADPH

KM=940 µM for NADP

KM=3.2 µM for all-trans-retinol

KM=0.24 µM for allopregnanolone

KM=0.13 µM for 3-alpha-androstanediol

KM=0.23 µM for androsterone

KM=0.13 µM for dehydroepiandrosterone

Vmax=1.2 nmol/min/mg enzyme with all-trans-retinol

Vmax=14.7 nmol/min/mg enzyme with allopregnanolone

Vmax=16.5 nmol/min/mg enzyme with 3-alpha-androstanediol

Vmax=35 nmol/min/mg enzyme with androsterone

Vmax=0.90 nmol/min/mg enzyme with dehydroepiandrosterone

Sequence caution

The sequence AAB88252.1 differs from that shown. Reason: Frameshift at positions 158 and 174.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 31730017-beta-hydroxysteroid dehydrogenase type 6
PRO_0000303211

Regions

Nucleotide binding33 – 5725NAD By similarity

Sites

Active site1761Proton acceptor By similarity
Binding site1641Substrate Potential

Amino acid modifications

Glycosylation1611N-linked (GlcNAc...) Potential
Glycosylation2151N-linked (GlcNAc...) Potential
Glycosylation2561N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict631E → D in AAB88252. Ref.1
Sequence conflict1051G → R in AAB88252. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O14756 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 46F1E940605CBEE9

FASTA31735,966
        10         20         30         40         50         60 
MWLYLAAFVG LYYLLHWYRE RQVVSHLQDK YVFITGCDSG FGNLLARQLD ARGLRVLAAC 

        70         80         90        100        110        120 
LTEKGAEQLR GQTSDRLETV TLDVTKMESI AAATQWVKEH VGDRGLWGLV NNAGILTPIT 

       130        140        150        160        170        180 
LCEWLNTEDS MNMLKVNLIG VIQVTLSMLP LVRRARGRIV NVSSILGRVA FFVGGYCVSK 

       190        200        210        220        230        240 
YGVEAFSDIL RREIQHFGVK ISIVEPGYFR TGMTNMTQSL ERMKQSWKEA PKHIKETYGQ 

       250        260        270        280        290        300 
QYFDALYNIM KEGLLNCSTN LNLVTDCMEH ALTSVHPRTR YSAGWDAKFF FIPLSYLPTS 

       310 
LADYILTRSW PKPAQAV 

« 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Prostate.
[2]"Molecular characterization of a first human 3(alpha-->beta)-hydroxysteroid epimerase."
Huang X.-F., Luu-The V.
J. Biol. Chem. 275:29452-29457(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
Tissue: Liver.
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[4]"Further characterization of human microsomal 3alpha-hydroxysteroid dehydrogenase."
Chetyrkin S.V., Hu J., Gough W.H., Dumaual N., Kedishvili N.Y.
Arch. Biochem. Biophys. 386:1-10(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
[5]"Gene structure, chromosomal localization and analysis of 3-ketosteroid reductase activity of the human 3(alpha-->beta)-hydroxysteroid epimerase."
Huang X.-F., Luu-The V.
Biochim. Biophys. Acta 1520:124-130(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U89281 mRNA. Translation: AAB88252.1. Frameshift.
AF016509 mRNA. Translation: AAB67236.1.
AF223225 mRNA. Translation: AAF81017.1.
BC020710 mRNA. Translation: AAH20710.1.
CCDSCCDS8925.1.
RefSeqNP_003716.2. NM_003725.3.
XP_005269264.1. XM_005269207.1.
XP_005269265.1. XM_005269208.1.
XP_005269266.1. XM_005269209.1.
XP_006719735.1. XM_006719672.1.
UniGeneHs.524513.

3D structure databases

ProteinModelPortalO14756.
SMRO14756. Positions 27-281.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000318631.

Chemistry

DrugBankDB00139. Succinic acid.

PTM databases

PhosphoSiteO14756.

Proteomic databases

PaxDbO14756.
PRIDEO14756.

Protocols and materials databases

DNASU8630.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000322165; ENSP00000318631; ENSG00000025423.
ENST00000554150; ENSP00000452273; ENSG00000025423.
ENST00000554643; ENSP00000451406; ENSG00000025423.
ENST00000555159; ENSP00000450698; ENSG00000025423.
ENST00000555805; ENSP00000451753; ENSG00000025423.
GeneID8630.
KEGGhsa:8630.
UCSCuc001smg.1. human.

Organism-specific databases

CTD8630.
GeneCardsGC12P057157.
HGNCHGNC:23316. HSD17B6.
HPAHPA059141.
MIM606623. gene.
neXtProtNX_O14756.
PharmGKBPA142671671.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1028.
HOVERGENHBG005482.
InParanoidO14756.
KOK13369.
OMAPITLCEW.
OrthoDBEOG7FXZZX.
PhylomeDBO14756.
TreeFamTF325617.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.

Gene expression databases

ArrayExpressO14756.
BgeeO14756.
CleanExHS_HSD17B6.
GenevestigatorO14756.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiHSD17B6.
GenomeRNAi8630.
NextBio32349.
PROO14756.
SOURCESearch...

Entry information

Entry nameH17B6_HUMAN
AccessionPrimary (citable) accession number: O14756
Secondary accession number(s): O43275
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM