[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Neurula; Sanger Xenopus tropicalis EST/cDNA project; Submitted (JUN-2006) 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

CR760225; CAJ83357.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001017234.1; -.

UniGene

Str.10270

3D structure databases

ModBase

Q28IU1.

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

Q28IU1.

Genome annotation databases

GeneID

549988; -.

KEGG

xtr:549988; -.

Phylogenomic databases

HOVERGEN

Q28IU1; -.

Other

ProtoNet

Q28IU1.

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`	`1 320`	`320`	`Estradiol 17-beta-dehydrogenase 12.`	`PRO_0000248375`
`TRANSMEM`	`17 37`	`21`	`Potential.`
`TRANSMEM`	`189 209`	`21`	`Potential.`
`TRANSMEM`	`283 303`	`21`	`Potential.`
`NP_BIND`	`56 85`	`30`	`NADP (By similarity).`
`ACT_SITE`	`209 209`		`Proton acceptor (By similarity).`
`BINDING`	`196 196`		`Substrate (By similarity).`

Sequence information

Length: 320 AA [This is the length of the unprocessed precursor]

Molecular weight: 35101 Da [This is the MW of the unprocessed precursor]

CRC64: C216ECF085D4AF14 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATESLAEVP VPGCNCFWYL GVVAAVWWGL RAAWCLLDGA RVWVLGSGAQ VGPRIGKWAV 

        70         80         90        100        110        120 
VTGATDGIGK AYAEELAKRG MNIVLISRSP EKLEEVAKQI KEKFKVETKI IAADFGKPTE 

       130        140        150        160        170        180 
IYGRIESGLR DLEIGVLVNN VGVSYEHPEY FLEIPDLENT LDKMININIT SVCQMTRLVL 

       190        200        210        220        230        240 
PGMLGRGRGV ILNISSASGM YPVPLLTVYS ATKAFVDFFS RGLQAEYRSK GVTVQSVLPF 

       250        260        270        280        290        300 
YVATKLAKIR KPTWDKPSPE TYVQSALNTV GLQTQTNGYL PHAIMGWIST SLVPVSTAIS 

       310        320 
LGMKMNKGLR ARFLKRAKQK

Q28IU1 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