[1]	NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY. STRAIN=Sprague-Dawley; TISSUE=Ovary; DOI=10.1210/en.135.4.1477; PubMed=7925110 [NCBI, ExPASy, EBI, Israel, Japan] Ghersevich S., Nokelainen P., Poutanen M., Orava M., Autio-Harmainen H., Rajaniemi H., Vihko R.; "Rat 17 beta-hydroxysteroid dehydrogenase type 1: primary structure and regulation of enzyme expression in rat ovary by diethylstilbestrol and gonadotropins in vivo."; Endocrinology 135:1477-1487(1994).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Sprague-Dawley; TISSUE=Kidney; DOI=10.1210/en.137.5.1572; PubMed=8612487 [NCBI, ExPASy, EBI, Israel, Japan] Akinola L.A., Poutanen M., Vihko R.; "Cloning of rat 17 beta-hydroxysteroid dehydrogenase type 2 and characterization of tissue distribution and catalytic activity of rat type 1 and type 2 enzymes."; Endocrinology 137:1572-1579(1996).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=Sprague-Dawley; TISSUE=Testis; DOI=10.1016/S0378-1119(97)00669-0; PubMed=9524272 [NCBI, ExPASy, EBI, Israel, Japan] Akinola L.A., Poutanen M., Peltoketo H., Vihko R., Vihko P.; "Characterization of rat 17 beta-hydroxysteroid dehydrogenase type 1 gene and mRNA transcripts."; Gene 208:229-238(1998).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Ovary; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

Comments

FUNCTION: Favors the reduction of estrogens and androgens. Uses preferentially NADH.
CATALYTIC ACTIVITY: Estradiol-17-beta + NAD(P)⁺ = estrone + NAD(P)H.
PATHWAY: Steroid biosynthesis; estrogen biosynthesis .
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X78811; CAA55389.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X97754; CAA66349.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X98038; CAA66657.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC086365; AAH86365.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S57901; S57901.

NP_036983.1; -.

3D structure databases

HSSP

P14061; 1FDW. [HSSP ENTRY / PDB]

SMR

P51657; 4-284.

ModBase

P51657.

Organism-specific databases

RGD

2836; Hsd17b1.

Gene expression databases

ArrayExpress

P51657; -.

GermOnline

ENSRNOG00000019830; Rattus norvegicus.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0004303;	Molecular function: estradiol 17-beta-dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0006703;	Biological process: estrogen biosynthetic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR011348; 17beta_DHase.
IPR002198; DHase_sc/Rdtase_SDR.
IPR002347; Glc/ribitol_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

PANTHER

PTHR19410:SF47; 17beta_DH; 1.
PTHR19410; ADH_short_C2; 1.

Pfam

PF00106; adh_short; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000095; 17beta-HSD; 1.

PRINTS

PR00081; GDHRDH.
PR00080; SDRFAMILY.

PROSITE

PS00061; ADH_SHORT; 1.

Proteomics databases

PRIDE

P51657; -.

Genome annotation databases

Ensembl

ENSRNOG00000019830; Rattus norvegicus. [Contig view]

GeneID

25322; -.

KEGG

rno:25322; -.

Phylogenomic databases

HOVERGEN

P51657; -.

Other

606169; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; Lipid synthesis; NAD; Oxidoreductase; Steroid biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 344`	`344`	`Estradiol 17-beta-dehydrogenase 1.`	`PRO_0000054569`
`NP_BIND`	`3 32`	`30`	`NAD (By similarity).`
`ACT_SITE`	`156 156`		`Proton acceptor (By similarity).`
`BINDING`	`143 143`		`Substrate (By similarity).`

Sequence information

Length: 344 AA [This is the length of the unprocessed precursor]

Molecular weight: 36967 Da [This is the MW of the unprocessed precursor]

CRC64: CB5FC139FBB3995E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDSTVVLITG CSSGIGLHLA VRLASDRSQS FKVYATLRDL KSQGPLLEAA RAQGCPPGSL 

        70         80         90        100        110        120 
EILELDVRDS ESVAAARACV TEGRVDVLVC NAGRGLFGPL EAHELNAVGA VLDVNVLGTI 

       130        140        150        160        170        180 
RMLQAFLPDM KRRHSGRVLV TASVGGLMGL PFHEVYCASK FALEGLCESL AILLPLFGVH 

       190        200        210        220        230        240 
VSLIECGAVH TAFHEKLEGG PGGALERADA QTRHLFAHYQ RGYEQALSEA QDPEEVTELF 

       250        260        270        280        290        300 
LTAMRAPQPA LRYFSTNRFL PLARMRTEDP SGSSYVEAMH REAFSDLQVQ EGAKAGAQVS 

       310        320        330        340 
GDPDTPPRAL ICLPECAIPR VTAELGWSAS DKPGQNKSCY QQKI

P51657 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools