[1]	NUCLEOTIDE SEQUENCE [MRNA]. Trzyna W.C., Gabbeta V., McHugh K.M.; Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Pituitary anterior lobe; 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: 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.
SEQUENCE CAUTION:
- Sequence=AAD00504.1; Type=Frameshift; Positions=272;

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

U81186; AAD00504.1; ALT_FRAME; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC061543; AAH61543.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_114455.1; -.

UniGene

Rn.203283

3D structure databases

ModBase

Q6P7R8.

PTM databases

PhosphoSite

Q6P7R8; -.

Organism-specific databases

RGD

708367; Hsd17b12.

Gene expression databases

ArrayExpress

Q6P7R8; -.

GermOnline

ENSRNOG00000009630; Rattus norvegicus.

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

Q6P7R8.

Genome annotation databases

Ensembl

ENSRNOG00000009630; Rattus norvegicus. [Contig view]

GeneID

84013; -.

KEGG

rno:84013; -.

NMPDR

fig|10116.3.peg.19242; -.

Phylogenomic databases

HOVERGEN

Q6P7R8; -.

Other

ProtoNet

Q6P7R8.

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_0000248370`
`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).`
`CONFLICT`	`236 236`		`A -> S (in Ref. 1; AAD00504).`

Sequence information

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

Molecular weight: 34841 Da [This is the MW of the unprocessed precursor]

CRC64: 8531943458EFC711 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MERALPAAGF LYWVGASTIA YLTLRASYSL FRAFQVWCVG NQAFVGPRLG EWAVVTGGTD 

        70         80         90        100        110        120 
GIGKSYAEEL AKRGMKIVLI SRSQDKLKEV SNNIKEKFNV ETRTIAVDFS LDDIYDKIKT 

       130        140        150        160        170        180 
GLSGLEIGVL VNNVGMSYEY PEYFLEIPDL DNTIKKLINI NVLSICKVTR LVLPGMVERS 

       190        200        210        220        230        240 
KGVILNISSA SGMLPVPLLT VYSATKAFVD FFSQCLHEEY KSKGIFVQSV LPFFVATKLA 

       250        260        270        280        290        300 
KIRKPTLDKP SAETFVKSAI KTVGLQTRTT GYVIHAIMGS INSILPRWIY FKTIMGFNKS 

       310 
LRNRYLKKTK KN

Q6P7R8 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