[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 257-269 AND 315-323. STRAIN=Sprague-Dawley; TISSUE=Corpus luteum; DOI=10.1006/bbrc.1994.1844; PubMed=8024573 [NCBI, ExPASy, EBI, Israel, Japan] Mao J., Duan W.R., Albarracin C.T., Parmer T.G., Gibori G.; "Isolation and characterization of a rat luteal cDNA encoding 20 alpha-hydroxysteroid dehydrogenase."; Biochem. Biophys. Res. Commun. 201:1289-1295(1994).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Wistar Imamichi; TISSUE=Ovary; PubMed=8172618 [NCBI, ExPASy, EBI, Israel, Japan] Miura R., Shiota K., Noda K., Yagi S., Ogawa T., Takahashi M.; "Molecular cloning of cDNA for rat ovarian 20 alpha-hydroxysteroid dehydrogenase (HSD1)."; Biochem. J. 299:561-567(1994).
[3]	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).
[4]	PROTEIN SEQUENCE OF 233-243; 252-269 AND 315-323. STRAIN=Sprague-Dawley; TISSUE=Corpus luteum; DOI=10.1210/en.134.6.2453; PubMed=8194472 [NCBI, ExPASy, EBI, Israel, Japan] Albarracin C.T., Parmer T.G., Duan W.R., Nelson S.E., Gibori G.; "Identification of a major prolactin-regulated protein as 20 alpha-hydroxysteroid dehydrogenase: coordinate regulation of its activity, protein content, and messenger ribonucleic acid expression."; Endocrinology 134:2453-2460(1994).
[5]	PROTEIN SEQUENCE OF 3-21. Noda K., Shiota K., Ogawa T., Yagi S., Takahashi M.; J. Reprod. Dev. 39:169-173(1993).

Comments

FUNCTION: Catalyzes the conversion of progesterone into 20-alpha-dihydroprogesterone (20 alpha-OHP).
CATALYTIC ACTIVITY: 17-alpha,20-alpha-dihydroxypregn-4-en-3-one + NAD(P)⁺ = 17-alpha-hydroxyprogesterone + NAD(P)H.
SUBUNIT: Monomer.
SUBCELLULAR LOCATION: Cytoplasm.
TISSUE SPECIFICITY: Corpus luteum (large luteal cells).
DEVELOPMENTAL STAGE: Remains repressed throughout pregnancy and becomes highly and rapidly expressed before parturition.
INDUCTION: Repressed by prolactin.
PTM: The N-terminus is blocked.
SIMILARITY: Belongs to the aldo/keto reductase 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

L32601; AAA40601.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D14424; BAA03317.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC100248; AAI00249.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

JC2330; JC2330.

NP_612519.1; -.

3D structure databases

HSSP

P23457; 1LWI. [HSSP ENTRY / PDB]

SMR

P51652; 6-323.

ModBase

P51652.

Organism-specific databases

RGD

708428; LOC171516.

Gene expression databases

ArrayExpress

P51652; -.

GermOnline

ENSRNOG00000017531; Rattus norvegicus.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from direct assay from MGI).
GO:0005625;	Cellular component: soluble fraction (inferred from direct assay from MGI).
GO:0047006;	Molecular function: 20-alpha-hydroxysteroid dehydrogenase activity (inferred from direct assay from MGI).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0042448;	Biological process: progesterone metabolic process (inferred from direct assay from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR001395; Aldo/ket_red.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.100; Aldo/ket_red; 1.

PANTHER

PTHR11732; Aldo/ket_red; 1.

Pfam

PF00248; Aldo_ket_red; 1.
Pfam graphical view of domain structure.

PRINTS

PR00069; ALDKETRDTASE.

ProDom

PD000288; Aldo/ket_red; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00798; ALDOKETO_REDUCTASE_1; 1.
PS00062; ALDOKETO_REDUCTASE_2; 1.
PS00063; ALDOKETO_REDUCTASE_3; 1.

Proteomics databases

PRIDE

P51652; -.

Genome annotation databases

Ensembl

ENSRNOG00000017531; Rattus norvegicus. [Contig view]

GeneID

171516; -.

KEGG

rno:171516; -.

Phylogenomic databases

HOVERGEN

P51652; -.

Other

622481; -.

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

Keywords

Cytoplasm; Direct protein sequencing; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 323`	`323`	`Aldo-keto reductase family 1 member C18.`	`PRO_0000124650`
`NP_BIND`	`13 22`	`10`	`NADP (Potential).`
`NP_BIND`	`217 280`	`64`	`NADP (By similarity).`
`ACT_SITE`	`55 55`		`Proton donor (By similarity).`
`BINDING`	`117 117`		`Substrate (By similarity).`
`SITE`	`54 54`	`1`	`Important for substrate specificity (By similarity).`
`SITE`	`84 84`	`1`	`Lowers pKa of active site Tyr (By similarity).`
`CONFLICT`	`242 242`		`C -> L (in Ref. 4; AA sequence).`

Sequence information

Length: 323 AA [This is the length of the unprocessed precursor]

Molecular weight: 37300 Da [This is the MW of the unprocessed precursor]

CRC64: D14270961515195E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNSKIQKMEL NDGHSIPVLG FGTYATEENL RKKSMESTKI AIDVGFRHID CSHLYQNEEE 

        70         80         90        100        110        120 
IGQAIVSKIE DGTVKREDIF YTSKLWSTSH RPELVRPSLE NSLRKLNLDY VDLYLIHFPV 

       130        140        150        160        170        180 
SLKPGDELLP QDEHGNLILD TVDLCDTWEA MEKCKDAGLA KSIGVSNFNR RQLEKILNKP 

       190        200        210        220        230        240 
GLKHRPVCNQ VECHLYLNQS KLLAYCKMND IVLVAYGALG TQRYKYCINE DTPVLLDDPI 

       250        260        270        280        290        300 
LCTMAKKYKR TPALIALRYQ LERGIVTLVK SFNEERIREN LQVFDFQLAS DDMEILDNLD 

       310        320 
RNLRYFPANM FKAHPNFPFS DEY

P51652 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