17-beta-hydroxysteroid dehydrogenase type 6 precursor

Contribute

Send feedback

Read comments (?) or add your own

O14756 (H17B6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 110. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	317 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. K_M=0.19 µM for NAD Ref.2 Ref.4 K_M=0.18 µM for NADH K_M=54 µM for NADPH K_M=940 µM for NADP K_M=3.2 µM for all-trans-retinol K_M=0.24 µM for allopregnanolone K_M=0.13 µM for 3-alpha-androstanediol K_M=0.23 µM for androsterone K_M=0.13 µM for dehydroepiandrosterone V_max=1.2 nmol/min/mg enzyme with all-trans-retinol V_max=14.7 nmol/min/mg enzyme with allopregnanolone V_max=16.5 nmol/min/mg enzyme with 3-alpha-androstanediol V_max=35 nmol/min/mg enzyme with androsterone V_max=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.

Ontologies

Keywords
Biological process	Lipid metabolism Steroid metabolism
Cellular component	Endoplasmic reticulum Endosome Membrane Microsome
Domain	Signal
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	androgen biosynthetic process Non-traceable author statement Ref.1. Source: UniProtKB androgen catabolic process Traceable author statement Ref.1. Source: UniProtKB
Cellular_component	early endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW intracellular Non-traceable author statement Ref.5. Source: UniProtKB
Molecular_function	electron carrier activity Traceable author statement Ref.1. Source: UniProtKB estradiol 17-beta-dehydrogenase activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity Non-traceable author statement Ref.1. Source: UniProtKB retinol dehydrogenase activity Inferred from electronic annotation. Source: EC testosterone dehydrogenase (NAD+) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 17

Potential

Chain

18 – 317

300

17-beta-hydroxysteroid dehydrogenase type 6

PRO_0000303211

Regions

Nucleotide binding

33 – 57

NAD By similarity

Sites

Active site

176

Proton acceptor By similarity

Binding site

164

Substrate Potential

Amino acid modifications

Glycosylation

161

N-linked (GlcNAc...) Potential

Glycosylation

215

N-linked (GlcNAc...) Potential

Glycosylation

256

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

E → D in AAB88252. Ref.1

Sequence conflict

105

G → R in AAB88252. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

O14756 [UniParc].

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

FASTA

317

35,966

        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' referencesShow '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.
IPI	IPI00099595.
RefSeq	NP_003716.2. NM_003725.2.
UniGene	Hs.524513.
3D structure databases
HSSP	HSSP built from PDB template 1FDS based on UniProtKB P14061.
ProteinModelPortal	O14756.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000318631.
PTM databases
PhosphoSite	O14756.
Proteomic databases
PaxDb	O14756.
PRIDE	O14756.
Protocols and materials databases
DNASU	8630.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000322165; ENSP00000318631; ENSG00000025423. ENST00000554150; ENSP00000452273; ENSG00000025423. ENST00000554643; ENSP00000451406; ENSG00000025423. ENST00000555159; ENSP00000450698; ENSG00000025423. ENST00000555805; ENSP00000451753; ENSG00000025423.
GeneID	8630.
KEGG	hsa:8630.
UCSC	uc001smg.1. human.
Organism-specific databases
CTD	8630.
GeneCards	GC12P057157.
HGNC	HGNC:23316. HSD17B6.
MIM	606623. gene.
neXtProt	NX_O14756.
PharmGKB	PA142671671.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1028.
HOVERGEN	HBG005482.
InParanoid	O14756.
KO	K13369.
OMA	PITLCEW.
OrthoDB	EOG4STS56.
PhylomeDB	O14756.
Gene expression databases
ArrayExpress	O14756.
Bgee	O14756.
CleanEx	HS_HSD17B6.
Genevestigator	O14756.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR002198. DH_sc/Rdtase_SDR. IPR002347. Glc/ribitol_DH. IPR016040. NAD(P)-bd_dom. IPR020904. Sc_DH/Rdtase_CS. [Graphical view]
Pfam	PF00106. adh_short. 1 hit. [Graphical view]
PRINTS	PR00081. GDHRDH. PR00080. SDRFAMILY.
PROSITE	PS00061. ADH_SHORT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00139. Succinic acid.
GenomeRNAi	8630.
NextBio	32349.
SOURCE	Search...

Entry information

Entry name

H17B6_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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

Human chromosome 12

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

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents