O54753 (H17B6_RAT) Reviewed, UniProtKB/Swiss-Prot

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:	Hsd17b9

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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 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). Ref.1
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.
Enzyme regulation	Competitively inhibited by 9-cis-retinoic ancid and 13-cis-retinoic acid. Ref.1
Subcellular location	Microsome membrane; Peripheral membrane protein; Lumenal side By similarity. Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side By similarity.
Tissue specificity	Detected in prostate, liver and kidney. Ref.1
Induction	Up-regulated by testosterone. Levels are very low in castrated male rats. Ref.1
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 Ref.1 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 caution	The sequence AAB88253.1 differs from that shown. Reason: Erroneous initiation. The sequence AAH88104.1 differs from that shown. Reason: Erroneous initiation. The sequence AAH91114.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 17	17	Potential
	Chain	18 – 317	300	17-beta-hydroxysteroid dehydrogenase type 6		PRO_0000303213
Regions
	Nucleotide binding	33 – 57	25	NAD By similarity
Sites
	Active site	176	1	Proton acceptor By similarity
	Binding site	164	1	Substrate Potential
Amino acid modifications
	Glycosylation	161	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	219	1	I → S in AAB88253. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O54753 [UniParc]. Last modified September 11, 2007. Version 2. Checksum: 4AB3F3160C6675A9	FASTA	317	36,145
	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

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], 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U89280 mRNA. Translation: AAB88253.1. Different initiation. BC088104 mRNA. Translation: AAH88104.1. Different initiation. BC091114 mRNA. Translation: AAH91114.1. Different initiation.
IPI	IPI00197982.
RefSeq	NP_775427.1. NM_173305.1.
UniGene	Rn.10857.
3D structure databases
HSSP	HSSP built from PDB template 1FDS based on UniProtKB P14061.
ProteinModelPortal	O54753.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000031599.
Proteomic databases
PaxDb	O54753.
PRIDE	O54753.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	286964.
KEGG	rno:286964.
UCSC	RGD:708343. rat.
Organism-specific databases
CTD	8630.
RGD	708343. Hsd17b6.
Phylogenomic databases
eggNOG	COG1028.
HOVERGEN	HBG005482.
InParanoid	O54753.
KO	K13369.
OrthoDB	EOG4STS56.
Gene expression databases
ArrayExpress	O54753.
Genevestigator	O54753.
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
NextBio	625175.

Entry information

Entry name

H17B6_RAT

Accession

Primary (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:	April 3, 2013
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program