PXL2B_RAT
ID PXL2B_RAT Reviewed; 201 AA.
AC D3ZVR7;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Prostamide/prostaglandin F synthase;
DE Short=Prostamide/PG F synthase;
DE Short=Prostamide/PGF synthase;
DE EC=1.11.1.20 {ECO:0000250|UniProtKB:Q9DB60};
DE AltName: Full=Peroxiredoxin-like 2B;
GN Name=Prxl2b {ECO:0000312|RGD:1308251}; Synonyms=Fam213b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reduction of prostaglandin-ethanolamide H(2)
CC (prostamide H(2)) to prostamide F(2alpha) with NADPH as proton donor.
CC Also able to reduce prostaglandin H(2) to prostaglandin F(2alpha) (By
CC similarity). {ECO:0000250|UniProtKB:Q9DB60}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + prostaglandin H2 = [thioredoxin]-
CC disulfide + prostaglandin F2alpha; Xref=Rhea:RHEA:28214, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:50058, ChEBI:CHEBI:57404, ChEBI:CHEBI:57405;
CC EC=1.11.1.20; Evidence={ECO:0000250|UniProtKB:Q9DB60};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + prostamide F2alpha = [thioredoxin]-
CC dithiol + prostamide H2; Xref=Rhea:RHEA:26373, Rhea:RHEA-COMP:10698,
CC Rhea:RHEA-COMP:10700, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:53081, ChEBI:CHEBI:53082; EC=1.11.1.20;
CC Evidence={ECO:0000250|UniProtKB:Q9DB60};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9DB60}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin-like PRXL2 family.
CC Prostamide/prostaglandin F synthase subfamily. {ECO:0000305}.
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DR EMBL; CH473968; EDL81278.1; -; Genomic_DNA.
DR RefSeq; NP_001102167.1; NM_001108697.1.
DR AlphaFoldDB; D3ZVR7; -.
DR SMR; D3ZVR7; -.
DR STRING; 10116.ENSRNOP00000018453; -.
DR iPTMnet; D3ZVR7; -.
DR PhosphoSitePlus; D3ZVR7; -.
DR PaxDb; D3ZVR7; -.
DR PeptideAtlas; D3ZVR7; -.
DR PRIDE; D3ZVR7; -.
DR GeneID; 362676; -.
DR KEGG; rno:362676; -.
DR CTD; 127281; -.
DR RGD; 1308251; Prxl2b.
DR eggNOG; KOG4498; Eukaryota.
DR HOGENOM; CLU_094994_0_0_1; -.
DR InParanoid; D3ZVR7; -.
DR OMA; QRPVCND; -.
DR OrthoDB; 1255928at2759; -.
DR PhylomeDB; D3ZVR7; -.
DR TreeFam; TF313804; -.
DR PRO; PR:D3ZVR7; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Proteomes; UP000234681; Chromosome 5.
DR Bgee; ENSRNOG00000013468; Expressed in duodenum and 18 other tissues.
DR Genevisible; D3ZVR7; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:CAFA.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:CAFA.
DR GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
DR GO; GO:0016209; F:antioxidant activity; IBA:GO_Central.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; ISS:UniProtKB.
DR GO; GO:0047017; F:prostaglandin-F synthase activity; ISS:CAFA.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; ISS:UniProtKB.
DR InterPro; IPR032801; PXL2A/B/C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR28630; PTHR28630; 1.
DR Pfam; PF13911; AhpC-TSA_2; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; NADP; Oxidoreductase; Phosphoprotein;
KW Prostaglandin biosynthesis; Prostaglandin metabolism; Reference proteome.
FT CHAIN 1..201
FT /note="Prostamide/prostaglandin F synthase"
FT /id="PRO_0000406969"
FT MOD_RES 108
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8TBF2"
SQ SEQUENCE 201 AA; 21607 MW; D8FC444C21207494 CRC64;
MSTLDLGRVG ACVLKHAVTG EAVELRSLWQ EKACVVAGLR RFGCMVCRWI AQDLSNLRGI
LDQNDVRLVG IGPEALGLQE FLDGGYFSGE LYLDESKQIY KELGFKRYNS LSILPAALGK
PVRDVASKAK AVGIQGNLSG DLLQSGGLLV VSKGGDRVLL HFIQSSPGDY VPQENILQAL
GISAEVCSSK PPQCDEEVCG R