[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Crossbred X Angus; TISSUE=Ileum; NIH - Mammalian Gene Collection (MGC) project; Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Functions as 15-oxo-prostaglandin 13-reductase and acts on 15-oxo-PGE1, 15-oxo-PGE2 and 15-oxo-PGE2-alpha. Has no activity towards PGE1, PGE2 and PGE2-alpha. Catalyzes the conversion of leukotriene B4 into its biologically less active metabolite, 12-oxo-leukotriene B4. This is an initial and key step of metabolic inactivation of leukotriene B4 (By similarity).
CATALYTIC ACTIVITY: n-alkanal + NAD(P)⁺ = alk-2-enal + NAD(P)H.
CATALYTIC ACTIVITY: 11-alpha-hydroxy-9,15-dioxoprost-5-enoate + NAD(P)⁺ = (5Z)-(13E)-11-alpha-hydroxy-9,15-dioxoprosta-5,13-dienoate + NAD(P)H.
SUBUNIT: Monomer or homodimer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the NADP-dependent oxidoreductase L4BD 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

BC102822; AAI02823.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001030358.1; -.

UniGene

Bt.51592

3D structure databases

SMR

Q3SZJ4; 1-329.

ModBase

Q3SZJ4.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0047522;	Molecular function: 15-oxoprostaglandin 13-oxidase activity (inferred from electronic annotation from EC).
GO:0032440;	Molecular function: 2-alkenal reductase activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR002085; AlcDHase_SF_Zn.
IPR013149; AlcDHase_Zn-bd.
IPR014190; B4_12hDHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

PANTHER

PTHR11695; ADH_Sf_Zn; 1.

Pfam

PF00107; ADH_zinc_N; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR02825; B4_12hDH; 1.

Genome annotation databases

Ensembl

ENSBTAG00000011027; Bos taurus. [Contig view]

GeneID

513177; -.

KEGG

bta:513177; -.

Phylogenomic databases

HOVERGEN

Q3SZJ4; -.

Other

UniRef

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

Keywords

Cytoplasm; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 329`	`329`	`Prostaglandin reductase 1.`	`PRO_0000285790`
`NP_BIND`	`149 166`	`18`	`NADP (Potential).`
`BINDING`	`178 178`		`NADP (By similarity).`
`BINDING`	`193 193`		`NADP (By similarity).`
`BINDING`	`217 217`		`NADP (By similarity).`
`BINDING`	`245 245`		`NADP (By similarity).`
`BINDING`	`321 321`		`NADP (By similarity).`

Sequence information

Length: 329 AA [This is the length of the unprocessed precursor]

Molecular weight: 35706 Da [This is the MW of the unprocessed precursor]

CRC64: 8CCF8128A6447C33 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVHAKSWTLK KHFVGYPTNS DFELKTVELP PLKDGEVLLE ALYLTVDPYM RIMAKSLKEG 

        70         80         90        100        110        120 
DMMMGEQVAR VVESKNSAFP TGTIVLAPSG WTTHSISNGE KLEKVLAEWP DTLPLSLALG 

       130        140        150        160        170        180 
TVGMPGLTAY FGLLDICGVK GGETVLVSAA AGAVGSIVGQ IAKLKGCKVV GTAGSDEKVA 

       190        200        210        220        230        240 
WLKKHGFDVA LNYKTVKSLE EALKEAAPEG YDCYFDNVGG EFSNVAITQM KKFGRIAICG 

       250        260        270        280        290        300 
AISVYNRTSP LSPGPSPEII IFKELHLQGF VVYRWQGEVR QKALRDLLKW VSEGKIQYHE 

       310        320 
HVTEGFENMP AAFIGLLKGE NLGKAIVKA

Q3SZJ4 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