HPGDS_CHICK
ID HPGDS_CHICK Reviewed; 199 AA.
AC O73888;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Hematopoietic prostaglandin D synthase {ECO:0000305};
DE Short=H-PGDS;
DE EC=5.3.99.2 {ECO:0000269|PubMed:9657971};
DE AltName: Full=GST class-sigma;
DE AltName: Full=Glutathione S-transferase;
DE EC=2.5.1.18 {ECO:0000269|PubMed:9657971};
DE AltName: Full=Glutathione-dependent PGD synthase;
DE AltName: Full=Glutathione-requiring prostaglandin D synthase;
DE AltName: Full=Prostaglandin-H2 D-isomerase;
GN Name=HPGDS; Synonyms=GSTS, PGDS, PTGDS2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC TISSUE=Spleen;
RX PubMed=9657971; DOI=10.1042/bj3330317;
RA Thomson A.M., Meyer D.J., Hayes J.D.;
RT "Sequence, catalytic properties and expression of chicken glutathione-
RT dependent prostaglandin D2 synthase, a novel class Sigma glutathione S-
RT transferase.";
RL Biochem. J. 333:317-325(1998).
RN [2]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11572089; DOI=10.1007/s004410100414;
RA Zhu Y., Wang M., Lin H., Li Z., Luo J.;
RT "Identification of estrogen-responsive genes in chick liver.";
RL Cell Tissue Res. 305:357-363(2001).
CC -!- FUNCTION: Bifunctional enzyme which catalyzes both the conversion of
CC PGH2 to PGD2, a prostaglandin involved in smooth muscle
CC contraction/relaxation and a potent inhibitor of platelet aggregation,
CC and the conjugation of glutathione with a wide range of aryl halides,
CC organic isothiocyanates and alpha,beta-unsaturated carbonyls. Also
CC exhibits low glutathione-peroxidase activity towards cumene
CC hydroperoxide and t-butyl hydroperoxide. {ECO:0000269|PubMed:9657971}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=prostaglandin H2 = prostaglandin D2; Xref=Rhea:RHEA:10600,
CC ChEBI:CHEBI:57405, ChEBI:CHEBI:57406; EC=5.3.99.2;
CC Evidence={ECO:0000269|PubMed:9657971};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10601;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC Evidence={ECO:0000269|PubMed:9657971};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-glyceryl-prostaglandin H2 = 2-glyceryl-prostaglandin D2;
CC Xref=Rhea:RHEA:51232, ChEBI:CHEBI:85166, ChEBI:CHEBI:133979;
CC Evidence={ECO:0000250|UniProtKB:O60760};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51233;
CC Evidence={ECO:0000250|UniProtKB:O60760};
CC -!- COFACTOR:
CC Name=glutathione; Xref=ChEBI:CHEBI:57925;
CC Evidence={ECO:0000269|PubMed:9657971};
CC Note=Glutathione is required for the prostaglandin D synthase activity.
CC {ECO:0000269|PubMed:9657971};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=128 umol/min/mg enzyme with 1-bromo-2,4-dinitrobenzene as
CC substrate {ECO:0000269|PubMed:9657971};
CC Vmax=97 umol/min/mg enzyme with 1-chloro-2,4-dinitrobenzene as
CC substrate {ECO:0000269|PubMed:9657971};
CC Vmax=410 umol/min/mg enzyme with 1-fluoro-2,4-dinitrobenzene as
CC substrate {ECO:0000269|PubMed:9657971};
CC Vmax=116 umol/min/mg enzyme with 1-iodo-2,4-dinitrobenzene as
CC substrate {ECO:0000269|PubMed:9657971};
CC Vmax=67 umol/min/mg enzyme with 7-chloro-4-nitrobenz-2-oxa-1,3-
CC diazole as substrate {ECO:0000269|PubMed:9657971};
CC Vmax=1.4 umol/min/mg enzyme with 4-nitrobenzyl chloride as substrate
CC {ECO:0000269|PubMed:9657971};
CC Vmax=0.05 umol/min/mg enzyme with 1,2-dichloro-4-nitrobenzene as
CC substrate {ECO:0000269|PubMed:9657971};
CC Vmax=0.04 umol/min/mg enzyme with ethacrynic acid as substrate
CC {ECO:0000269|PubMed:9657971};
CC Vmax=2.8 umol/min/mg enzyme with 4-hydroxynon-2-enal as substrate
CC {ECO:0000269|PubMed:9657971};
CC Vmax=0.06 umol/min/mg enzyme with trans,trans-deca-2,4-dienal as
CC substrate {ECO:0000269|PubMed:9657971};
CC Vmax=0.02 umol/min/mg enzyme with trans-non-2-enal as substrate
CC {ECO:0000269|PubMed:9657971};
CC Vmax=0.5 umol/min/mg enzyme with cumene hydroperoxide as substrate
CC {ECO:0000269|PubMed:9657971};
CC Vmax=0.06 umol/min/mg enzyme with t-butyl hydroperoxide as substrate
CC {ECO:0000269|PubMed:9657971};
CC Vmax=12.6 umol/min/mg enzyme with allyl isothiocyanate as substrate
CC {ECO:0000269|PubMed:9657971};
CC Vmax=17.6 umol/min/mg enzyme with benzyl isothiocyanate as substrate
CC {ECO:0000269|PubMed:9657971};
CC Vmax=0.02 umol/min/mg enzyme with Delta5-androstene-3,17-dione as
CC substrate {ECO:0000269|PubMed:9657971};
CC Vmax=0.11 umol/min/mg enzyme with 4-nitrophenyl acetate as substrate
CC {ECO:0000269|PubMed:9657971};
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver, kidney, small intestine
CC and colon, moderately in pancreas, bone marrow, lung and ovary, and
CC expressed at low levels in spleen, thymus, heart and brain. Not
CC detected in oviduct or skin (at protein level) (PubMed:9657971).
CC Expressed in liver (PubMed:11572089). {ECO:0000269|PubMed:11572089,
CC ECO:0000269|PubMed:9657971}.
CC -!- INDUCTION: Significantly increased expression by estrogen. Up-regulated
CC after 1 hour of exposure to estrogen. Expression persists through 72
CC hours. {ECO:0000269|PubMed:11572089}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Sigma family.
CC {ECO:0000305}.
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DR EMBL; AJ006405; CAA07005.1; -; mRNA.
DR RefSeq; NP_990342.1; NM_205011.1.
DR AlphaFoldDB; O73888; -.
DR SMR; O73888; -.
DR STRING; 9031.ENSGALP00000016919; -.
DR PaxDb; O73888; -.
DR Ensembl; ENSGALT00000016938; ENSGALP00000016919; ENSGALG00000010402.
DR Ensembl; ENSGALT00000089249; ENSGALP00000062839; ENSGALG00000010402.
DR GeneID; 395863; -.
DR KEGG; gga:395863; -.
DR CTD; 27306; -.
DR VEuPathDB; HostDB:geneid_395863; -.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00940000160278; -.
DR HOGENOM; CLU_039475_1_0_1; -.
DR InParanoid; O73888; -.
DR OMA; KEMELMW; -.
DR OrthoDB; 1162336at2759; -.
DR PhylomeDB; O73888; -.
DR TreeFam; TF105321; -.
DR BRENDA; 5.3.99.2; 1306.
DR PRO; PR:O73888; -.
DR Proteomes; UP000000539; Chromosome 4.
DR Bgee; ENSGALG00000010402; Expressed in kidney and 10 other tissues.
DR ExpressionAtlas; O73888; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0004667; F:prostaglandin-D synthase activity; ISS:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006693; P:prostaglandin metabolic process; ISS:UniProtKB.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF14497; GST_C_3; 1.
DR Pfam; PF02798; GST_N; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism; Isomerase;
KW Lipid biosynthesis; Lipid metabolism; Prostaglandin biosynthesis;
KW Prostaglandin metabolism; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..199
FT /note="Hematopoietic prostaglandin D synthase"
FT /id="PRO_0000185937"
FT DOMAIN 2..79
FT /note="GST N-terminal"
FT DOMAIN 81..199
FT /note="GST C-terminal"
FT BINDING 8
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O60760"
FT BINDING 14
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O60760"
FT BINDING 39
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O60760"
FT BINDING 49..51
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O60760"
FT BINDING 63..64
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O60760"
SQ SEQUENCE 199 AA; 22730 MW; 335A884D93009069 CRC64;
MPNYKLTYFN LRGRAEICRY LFAYAGIKYE DHRLEGADWP KIKPTIPFGK VPILEVDGVI
IHQSLAIARY LARESGLAGQ TPVEQALADA IVDTIDDFMM LFPWAEKNQD VKEKAFNDIL
TNKAPELLKD LDTFLGDKKW FVGKSVTWAD FYWDVCSTTL LSYKADLADK YPRLLALRDR
VEALPAIAAW IQKRPKTAI
