ID   PXL2B_PIG               Reviewed;         202 AA.
AC   A9CQL8;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 60.
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:0000269|PubMed:18006499};
DE   AltName: Full=Peroxiredoxin-like 2B;
GN   Name=PRXL2B; Synonyms=FAM213B;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=18006499; DOI=10.1074/jbc.m705638200;
RA   Moriuchi H., Koda N., Okuda-Ashitaka E., Daiyasu H., Ogasawara K., Toh H.,
RA   Ito S., Woodward D.F., Watanabe K.;
RT   "Molecular characterization of a novel type of prostamide/prostaglandin F
RT   synthase, belonging to the thioredoxin-like superfamily.";
RL   J. Biol. Chem. 283:792-801(2008).
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).
CC       {ECO:0000269|PubMed:18006499}.
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:0000269|PubMed:18006499};
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:0000269|PubMed:18006499};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.0076 mM for prostamide H(2) {ECO:0000269|PubMed:18006499};
CC         KM=0.0069 mM for prostaglandin H(2) {ECO:0000269|PubMed:18006499};
CC         Vmax=0.25 umol/min/mg enzyme with prostamide H(2) as substrate
CC         {ECO:0000269|PubMed:18006499};
CC         Vmax=0.685 umol/min/mg enzyme with prostaglandin H(2) as substrate
CC         {ECO:0000269|PubMed:18006499};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin-like PRXL2 family.
CC       Prostamide/prostaglandin F synthase subfamily. {ECO:0000305}.
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DR   EMBL; AB329665; BAF96021.1; -; mRNA.
DR   RefSeq; NP_001106912.1; NM_001113441.1.
DR   AlphaFoldDB; A9CQL8; -.
DR   STRING; 9823.ENSSSCP00000023293; -.
DR   SwissLipids; SLP:000001102; -.
DR   PaxDb; A9CQL8; -.
DR   PeptideAtlas; A9CQL8; -.
DR   Ensembl; ENSSSCT00000028536; ENSSSCP00000023293; ENSSSCG00000026554.
DR   GeneID; 100134955; -.
DR   KEGG; ssc:100134955; -.
DR   CTD; 127281; -.
DR   VGNC; VGNC:98543; PRXL2B.
DR   eggNOG; KOG4498; Eukaryota.
DR   GeneTree; ENSGT00940000162566; -.
DR   InParanoid; A9CQL8; -.
DR   OMA; QRPVCND; -.
DR   OrthoDB; 1255928at2759; -.
DR   BRENDA; 1.1.1.188; 6170.
DR   BRENDA; 1.11.1.20; 6170.
DR   SABIO-RK; A9CQL8; -.
DR   Proteomes; UP000008227; Chromosome 6.
DR   Proteomes; UP000314985; Unplaced.
DR   Bgee; ENSSSCG00000026554; Expressed in longissimus lumborum muscle and 43 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:CAFA.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:CAFA.
DR   GO; GO:0043209; C:myelin sheath; ISS:CAFA.
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; IDA:UniProtKB.
DR   GO; GO:0047017; F:prostaglandin-F synthase activity; IDA:UniProtKB.
DR   GO; GO:0001516; P:prostaglandin biosynthetic process; IDA: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   1: Evidence at protein 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..202
FT                   /note="Prostamide/prostaglandin F synthase"
FT                   /id="PRO_0000406970"
FT   MOD_RES         108
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TBF2"
SQ   SEQUENCE   202 AA;  21547 MW;  4B1EFE9D50839698 CRC64;
     MSTVDLARVG ACVLKHAVTG EAVELRSLWQ EQACVVAGLR RFGCMVCRWI ARDLSSLKGL
     LDQHGVRLVG VGPEALGLQE FLDGGYFAGD LYLDESKQFY KELGFKRYSS LSILPAALGK
     PVRDVAAKAK AAGIQGNLSG DLLQSGGLLV VAKGGDKVLL HFVQKSPGDY APQESILQAL
     CISAEAACTH QPPQCDEEAC SR