[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Lung; NIH - Xenopus Gene Collection (XGC) project; Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Catalyzes the transformation of estrone (E1) into estradiol (E2), suggesting a central role in estrogen formation (By similarity).
CATALYTIC ACTIVITY: Estradiol-17-beta + NAD(P)⁺ = estrone + NAD(P)H.
PATHWAY: Steroid metabolism; estrogen biosynthesis .
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein (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

BC084629; AAH84629.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001088370.1; -.

UniGene

Xl.19362

3D structure databases

ModBase

Q5XG41.

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

Q5XG41.

Genome annotation databases

GeneID

495218; -.

KEGG

xla:495218; -.

Phylogenomic databases

HOVERGEN

Q5XG41; -.

Other

ProtoNet

Q5XG41.

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`	`1 318`	`318`	`Estradiol 17-beta-dehydrogenase 12-A.`	`PRO_0000248373`
`TRANSMEM`	`15 35`	`21`	`Potential.`
`TRANSMEM`	`187 207`	`21`	`Potential.`
`TRANSMEM`	`281 301`	`21`	`Potential.`
`NP_BIND`	`54 83`	`30`	`NADP (By similarity).`
`ACT_SITE`	`207 207`		`Proton acceptor (By similarity).`
`BINDING`	`194 194`		`Substrate (By similarity).`

Sequence information

Length: 318 AA [This is the length of the unprocessed precursor]

Molecular weight: 34994 Da [This is the MW of the unprocessed precursor]

CRC64: 87D46FD9D88A2F6A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAPESLVEVP GCNCFWYLGV LAAAWWGLRA ACCLLNGARA WVLGSGAQVG PRIGKWAVVT 

        70         80         90        100        110        120 
GATDGIGKAY AEELARRGMS IVLISRSPEK LDEAAKHIKE TFKVETKIIA ADFGKPTEIY 

       130        140        150        160        170        180 
ERIEAGLRDL EIGVLVNNVG VSYEYPEYFL EIPDLENTLD KMININIMSV CQMTRLVLPG 

       190        200        210        220        230        240 
MLGRGKGVIL NISSASGMYP VPLLTVYSAT KAFVDFFSRG LHAEYRNKGI NVQSVLPFYV 

       250        260        270        280        290        300 
ATKLAKIRKP TWDKPSPETY VRSAVNTVGL QTQTNGYLPH AIMGWISTSL VPVSVAISMG 

       310 
MKMNKGLRSR FLKRKKQK

Q5XG41 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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