FUNCTION: Catalyzes the transformation of estrone (E1) into estradiol (E2), suggesting a central role in estrogen formation. Its strong expression in ovary and mammary gland suggest that it may constitute the major enzyme responsible for the conversion of E1 to E2 in females. Also has 3-ketoacyl-CoA reductase activity, reducing both long chain 3-ketoacyl-CoAs and long chain fatty acyl-CoAs, suggesting a role in long fatty acid elongation (By similarity).
CATALYTIC ACTIVITY: Estradiol-17-beta + NAD(P)⁺ = estrone + NAD(P)H.
PATHWAY: Steroid metabolism; estrogen biosynthesis .
PATHWAY: Lipid metabolism; fatty acid biosynthesis .
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein (By similarity).
DOMAIN: The di-lysine motif confers endoplasmic reticulum localization for type I membrane proteins (By similarity).
SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family. 17-beta-HSD 3 subfamily.

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

BT020943; AAX08960.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001074384.1; -.

UniGene

Bt.89260

3D structure databases

ModBase

Q5E9H7.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.

Family and domain databases

InterPro

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; ADH_short_C2; 1.

Pfam

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

PRINTS

PR00081; GDHRDH.
PR00080; SDRFAMILY.

PROSITE

PS00061; ADH_SHORT; 1.

BLOCKS

Q5E9H7.

Genome annotation databases

GeneID

616219; -.

KEGG

bta:616219; -.

Phylogenomic databases

HOVERGEN

Q5E9H7; -.

Other

ProtoNet

Q5E9H7.

UniRef

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

Keywords

Endoplasmic reticulum; Lipid synthesis; Membrane; NADP; Oxidoreductase; Steroid biosynthesis; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 312`	`312`	`Estradiol 17-beta-dehydrogenase 12.`	`PRO_0000248367`
`TRANSMEM`	`4 24`	`21`	`Potential.`
`TRANSMEM`	`182 202`	`21`	`Potential.`
`TRANSMEM`	`271 291`	`21`	`Potential.`
`NP_BIND`	`50 79`	`30`	`NADP (By similarity).`
`MOTIF`	`308 312`	`5`	`Di-lysine motif (By similarity).`
`ACT_SITE`	`202 202`		`Proton acceptor (By similarity).`
`BINDING`	`189 189`		`Substrate (By similarity).`

Sequence information

Length: 312 AA [This is the length of the unprocessed precursor]

Molecular weight: 34495 Da [This is the MW of the unprocessed precursor]

CRC64: 3A10BB92B7F6B1D1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
METALPAAGF LYWVGASTVA YLALRISCWF FTALRVWGLG HEAGVGPWLG EWAVVTGGTD 

        70         80         90        100        110        120 
GIGKSYAEEL AKRGMKIVLI SRSQDKLDQV SSEISEKFKV ETKTIAVDFT SEDIYDKIKA 

       130        140        150        160        170        180 
SLAGLNIGVL VNNVGMSYEY PEYFLDVPDL DNTIKKLITV NALSVCKMTR LVLPGMVERS 

       190        200        210        220        230        240 
KGAILNISSA SGMYPVPLLT IYSATKAFVD FFSQCLHEEY KSKGVIVQSV LPYYVATKLA 

       250        260        270        280        290        300 
KIKRPTWDKP SPETFVKSAM KTIGVQSRTN GYPIHSLVAS VSASLPSWLY FKIAMYSGNS 

       310 
IRVRYLKKMK MN

Q5E9H7 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