PXL2B_PONAB
ID PXL2B_PONAB Reviewed; 198 AA.
AC Q5R7S9;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 64.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR860030; CAH92181.1; -; mRNA.
DR RefSeq; NP_001128963.1; NM_001135491.1.
DR AlphaFoldDB; Q5R7S9; -.
DR STRING; 9601.ENSPPYP00000002288; -.
DR GeneID; 100190803; -.
DR KEGG; pon:100190803; -.
DR CTD; 127281; -.
DR eggNOG; KOG4498; Eukaryota.
DR InParanoid; Q5R7S9; -.
DR OrthoDB; 1255928at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:CAFA.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:CAFA.
DR GO; GO:0043209; C:myelin sheath; ISS:CAFA.
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 2: Evidence at transcript level;
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..198
FT /note="Prostamide/prostaglandin F synthase"
FT /id="PRO_0000284639"
FT MOD_RES 108
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8TBF2"
SQ SEQUENCE 198 AA; 21182 MW; F1BE39D6F3DB2ABA CRC64;
MSTVDLARVG ACILKHAVTG EAVELRSLWR ERACVVAGLR RFGCVVCRWI AQDLSSLAGL
LDQHGVRLVG VGPEALGLQE FLDGDYFAGE LYLDESKQLY NELGFKRYNS PSILPAALGK
PVRDVAAKAK AVGIQGNLSG DLLQSGGLLV VSKGGDKVLL HFVQKSPGDY VPKEHILQVL
GISAEVCASN PPQCDREA
