ID   PXL2B_SALSA             Reviewed;         200 AA.
AC   B5X9L9;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 54.
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; Synonyms=fam213b;
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA   Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA   Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA   Koop B.F.;
RT   "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT   evolutionary pressures on a post-tetraploidization genome.";
RL   BMC Genomics 11:279-279(2010).
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; BT047738; ACI67539.1; -; mRNA.
DR   RefSeq; XP_014021781.1; XM_014166306.1.
DR   AlphaFoldDB; B5X9L9; -.
DR   SMR; B5X9L9; -.
DR   STRING; 8030.ENSSSAP00000100195; -.
DR   GeneID; 106582827; -.
DR   KEGG; sasa:106582827; -.
DR   CTD; 127281; -.
DR   OrthoDB; 1255928at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa22.
DR   Bgee; ENSSSAG00000074439; Expressed in actinopterygian pyloric caecum and 14 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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:0001516; P:prostaglandin biosynthetic process; ISS:UniProtKB.
DR   InterPro; IPR032801; PXL2A/B/C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR28630; PTHR28630; 1.
DR   Pfam; PF13911; AhpC-TSA_2; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; NADP; Oxidoreductase;
KW   Prostaglandin biosynthesis; Prostaglandin metabolism; Reference proteome.
FT   CHAIN           1..200
FT                   /note="Prostamide/prostaglandin F synthase"
FT                   /id="PRO_0000406971"
SQ   SEQUENCE   200 AA;  21861 MW;  ACD0145A4A290770 CRC64;
     MAKIELKPVG TNLLKSVSGE SVELQSLWRD KPVVLFFLRR FGCQVCRWTA AEISKLEPDL
     TAHGIALVGI GPEETGLKEF KEGGFFKGDL YIDEKKQCYK DLGFKRYTAL SVVPAALGKK
     IREVTTKAKA QGIQGNFTGD LLQSGGMLIV AKGGEKVLLH FVQDSPGDYV PLEDISKALD
     ISANVQAGER PQCNDDVCTR