[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). STRAIN=ICR; TISSUE=Ovary; Ishida M., Chang K., Hirabayashi K., Nishihara M., Takahashi M.; "Cloning of mouse 20alpha-hydroxysteroid dehydrogenase cDNA and its mRNA localization during pregnancy."; J. Reprod. Dev. 45:321-329(1999).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). STRAIN=FVB/N; TISSUE=Kidney; 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 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 (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	Q8K023-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	Q8K023-2
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_014039.

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

AB059565; BAB40958.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC034259; AAH34259.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_598827.1; -.

UniGene

Mm.41337

3D structure databases

HSSP

P23457; 1LWI. [HSSP ENTRY / PDB]

Q8K023; 6-323.

PTM databases

Q8K023; -.

Organism-specific databases

MGI

MGI:2145420; Akr1c18.

Gene expression databases

ArrayExpress

Q8K023; -.

CleanEx

MM_AKR1C18; -.

GermOnline

ENSMUSG00000021214; Mus musculus.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
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:0007567;	Biological process: parturition (inferred from mutant phenotype from MGI).
GO:0006709;	Biological process: progesterone catabolic 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

PS00062; ALDOKETO_REDUCTASE_2; 1.
PS00063; ALDOKETO_REDUCTASE_3; 1.

ProtoNet

Q8K023.

Genome annotation databases

Ensembl

ENSMUSG00000021214; Mus musculus. [Contig view]

GeneID

105349; -.

KEGG

mmu:105349; -.

Phylogenomic databases

HOGENOM

Q8K023; -.

HOVERGEN

Q8K023; -.

Other

NextBio

357616; -.

SOURCE

Akr1c18; Mus musculus.

UniRef

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

Keywords

Alternative splicing; Cytoplasm; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 323`	`323`	`Aldo-keto reductase family 1 member C18.`	`PRO_0000124649`
`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).`
`VAR_SEQ`	`124 149`		`Missing (in isoform 2).`	`VSP_014039`

Sequence information

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

Molecular weight: 37177 Da [This is the MW of the unprocessed precursor]

CRC64: F2732C09C60B4544 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNSKIQKIEL NDGHSIPVLG FGTYATEEHL KKKSMESTKI AIDVGFCHID CSHLYQNEEE 

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

       130        140        150        160        170        180 
SLKPGNELLP KDEHGNLIFD TVDLCDTWEA MEKCKDAGLA KSIGVSNFNR RQLEMILNKP 

       190        200        210        220        230        240 
GLKYKPVCNQ VECHLYLNQS KLLAYCKMND IVLVAYGALG TQRYKYCINE DTPVLLDDPV 

       250        260        270        280        290        300 
LCAMAKKYKR TPALIALRYQ LDRGIVALAK SFNEERIREN MQVFDFQLAS DDMKILDGLD 

       310        320 
RNLRYFPADM FKAHPNFPFF DEY

Q8K023 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