Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P05980 (PGFS1_BOVIN)

Last modified July 28, 2009. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Prostaglandin F synthase 1
      Short name=PGF synthase 1
      Short name=PGFS1
      Short name=PGF 1
    EC=1.1.1.188
Alternative name(s):
    Prostaglandin F synthase I
      Short name=PGFSI
    Prostaglandin-D2 11 reductase 1
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Hide | Top

Protein attributes

Sequence length323 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

Catalyzes the reduction of PGD2 and PGH2 to PGF(2 alpha) and a stereoisomer, respectively. It has a broad substrate specificity and reduces also other carbonyl compounds.

Catalytic activity

(5Z,13E)-(15S)-9-alpha,11-alpha,15-trihydroxyprosta-5,13-dienoate + NADP+ = (5Z,13E)-(15S)-9-alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADPH.

Pathway

Lipid metabolism; prostaglandin biosynthesis.

Subunit structure

Monomer.

Subcellular location

Cytoplasm.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the aldo/keto reductase family.

Hide | Top

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Lipid synthesis
Prostaglandin biosynthesis
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

prostaglandin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprostaglandin-F synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 323323Prostaglandin F synthase 1
PRO_0000124646

Regions

Nucleotide binding13 – 2210NADP Potential
Nucleotide binding217 – 28064NADP By similarity

Sites

Active site551Proton donor By similarity
Binding site1171Substrate By similarity
Site841Lowers pKa of active site Tyr By similarity

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P05980-1 [UniParc].

Last modified October 1, 1996. Version 3.
Checksum: 27E35CA47FB2FECC

FASTA32336,720
        10         20         30         40         50         60 
MDPKSQRVKL NDGHFIPVLG FGTYAPEEVP KSEALEATKF AIEVGFRHVD SAHLYQNEEQ 

        70         80         90        100        110        120 
VGQAIRSKIA DGTVKREDIF YTSKLWCNSL QPELVRPALE KSLQNLQLDY VDLYIIHSPV 

       130        140        150        160        170        180 
SLKPGNKFVP KDESGKLIFD SVDLCHTWEA LEKCKDAGLT KSIGVSNFNH KQLEKILNKP 

       190        200        210        220        230        240 
GLKYKPVCNQ VECHPYLNQS KLLEFCKSHD IVLVAYAALG AQLLSEWVNS NNPVLLEDPV 

       250        260        270        280        290        300 
LCAIAKKHKQ TPALVALRYQ VQRGVVVLAK SFNKKRIKEN MQVFDFELTP EDMKAIDGLN 

       310        320 
RNIRYYDFQK GIGHPEYPFS EEY

« Hide

Hide | Top

References

[1]"Structural similarity of bovine lung prostaglandin F synthase to lens epsilon-crystallin of the European common frog."
Watanabe K., Fujii Y., Nakayama K., Ohkubo H., Kuramitsu S., Kagamiyama H., Nakanishi S., Hayaishi O.
Proc. Natl. Acad. Sci. U.S.A. 85:11-15(1988) [PubMed: 2829166] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Lung.

Hide | Top

Cross-references

Sequence databases

J03570 mRNA. Translation: AAA30694.1.
IPIIPI00690622.
PIRA28396.
UniGeneBt.64820
Bt.66508
Bt.67184
Bt.91770

3D structure databases

HSSPHSSP built from PDB template 1J96 based on UniProtKB P52895.
SMRP05980. Positions 2-323.
ModBaseSearch...

Genome annotation databases

EnsemblENSBTAT00000024086; ENSBTAP00000024086; ENSBTAG00000022570; Bos taurus. [Genome view]

Phylogenomic databases

HOVERGENP05980.

Enzyme and pathway databases

BRENDA1.1.1.188. 251.

Family and domain databases

InterProIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_sg.
[Graphical view]
Gene3DG3DSA:3.20.20.100. Aldo/ket_red. 1 hit.
PANTHERPTHR11732. Aldo/ket_red. 1 hit.
PfamPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PRINTSPR00069. ALDKETRDTASE.
ProDomPD000288. Aldo/ket_red. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry namePGFS1_BOVIN
AccessionPrimary (citable) accession number: P05980
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 1, 1996
Last modified: July 28, 2009
This is version 80 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Hide | Top

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents