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Prostaglandin-H2 D-isomerase (EC 5.3.99.2) (Glutathione-independent PGD synthase) (Lipocalin-type prostaglandin-D synthase) (Prostaglandin-D2 synthase) (PGD2 synthase) (PGDS) (PGDS2)

 PTGDS_RAT               Reviewed;         189 AA.
P22057;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
23-MAY-2018, entry version 154.
RecName: Full=Prostaglandin-H2 D-isomerase;
EC=5.3.99.2;
AltName: Full=Glutathione-independent PGD synthase;
AltName: Full=Lipocalin-type prostaglandin-D synthase;
AltName: Full=Prostaglandin-D2 synthase;
Short=PGD2 synthase;
Short=PGDS;
Short=PGDS2;
Flags: Precursor;
Name=Ptgds;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 39-53; 60-85; 93-108
AND 138-185, TISSUE SPECIFICITY, AND GLYCOSYLATION.
TISSUE=Brain;
PubMed=2642896;
Urade Y., Nagata A., Suzuki Y., Fujii Y., Hayaishi O.;
"Primary structure of rat brain prostaglandin D synthetase deduced
from cDNA sequence.";
J. Biol. Chem. 264:1041-1045(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Wistar;
PubMed=1608945; DOI=10.1073/pnas.89.12.5376;
Igarashi M., Nagata A., Toh H., Urade Y., Hayaihi O.;
"Structural organization of the gene for prostaglandin D synthase in
the rat brain.";
Proc. Natl. Acad. Sci. U.S.A. 89:5376-5380(1992).
[3]
PROTEIN SEQUENCE OF 26-42, PYROGLUTAMATE FORMATION AT GLN-25, TISSUE
SPECIFICITY, AND MASS SPECTROMETRY.
STRAIN=Wistar Kyoto; TISSUE=Cerebrospinal fluid;
PubMed=11565799;
DOI=10.1002/1522-2683(200108)22:14<3043::AID-ELPS3043>3.0.CO;2-M;
Wait R., Gianazza E., Eberini I., Sironi L., Dunn M.J., Gemeiner M.,
Miller I.;
"Proteins of rat serum, urine, and cerebrospinal fluid: VI. Further
protein identifications and interstrain comparison.";
Electrophoresis 22:3043-3052(2001).
[4]
PROTEIN SEQUENCE OF 27-41, AND TISSUE SPECIFICITY.
TISSUE=Cerebrospinal fluid;
PubMed=8599604; DOI=10.1016/0167-4889(95)00182-4;
Giacomelli S., Leone M.-G., Grima J., Silvestrini B., Cheng C.Y.;
"Astrocytes synthesize and secrete prostaglandin D synthetase in
vitro.";
Biochim. Biophys. Acta 1310:269-276(1996).
[5]
PROTEIN SEQUENCE OF 26-32, ACTIVE SITE, DISULFIDE BOND, AND
MUTAGENESIS OF CYS-65; CYS-89 AND CYS-186.
TISSUE=Brain;
PubMed=7836410; DOI=10.1074/jbc.270.3.1422;
Urade Y., Tanaka T., Eguchi N., Kikuchi M., Kimura H., Toh H.,
Hayaishi O.;
"Structural and functional significance of cysteine residues of
glutathione-independent prostaglandin D synthase. Identification of
Cys65 as an essential thiol.";
J. Biol. Chem. 270:1422-1428(1995).
[6]
NUCLEOTIDE SEQUENCE OF 124-189.
PubMed=8216319; DOI=10.1006/bbrc.1993.2262;
Garcia-Fernandez L.F., Iniguez M.A., Rodriguez-Pena A., Munoz A.,
Bernal J.;
"Brain-specific prostaglandin D2 synthetase mRNA is dependent on
thyroid hormone during rat brain development.";
Biochem. Biophys. Res. Commun. 196:396-401(1993).
[7]
PROTEIN SEQUENCE OF 169-185, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain;
Lubec G., Kang S.U., Lubec S.;
Submitted (SEP-2007) to UniProtKB.
[8]
FUNCTION, AND ENZYME REGULATION BY RETINOIDS.
PubMed=9188476; DOI=10.1074/jbc.272.25.15789;
Tanaka T., Urade Y., Kimura H., Eguchi N., Nishikawa A., Hayaishi O.;
"Lipocalin-type prostaglandin D synthase (beta-trace) is a newly
recognized type of retinoid transporter.";
J. Biol. Chem. 272:15789-15795(1997).
[9]
FUNCTION, AND ENZYME REGULATION.
PubMed=10387044; DOI=10.1021/bi990261p;
Beuckmann C.T., Aoyagi M., Okazaki I., Hiroike T., Toh H.,
Hayaishi O., Urade Y.;
"Binding of biliverdin, bilirubin, and thyroid hormones to lipocalin-
type prostaglandin D synthase.";
Biochemistry 38:8006-8013(1999).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=11058225;
DOI=10.1002/1096-9861(20001204)428:1<62::AID-CNE6>3.0.CO;2-E;
Beuckmann C.T., Lazarus M., Gerashchenko D., Mizoguchi A., Nomura S.,
Mohri I., Uesugi A., Kaneko T., Mizuno N., Hayaishi O., Urade Y.;
"Cellular localization of lipocalin-type prostaglandin D synthase
(beta-trace) in the central nervous system of the adult rat.";
J. Comp. Neurol. 428:62-78(2000).
[11]
FUNCTION, TISSUE SPECIFICITY, INDUCTION BY PROGESTERONE, AND RETINOIDS
AND THYROID HORMONE.
PubMed=10650953; DOI=10.1210/endo.141.2.7329;
Samy E.T., Li J.C.H., Grima J., Lee W.M., Silvestrini B., Cheng C.Y.;
"Sertoli cell prostaglandin D2 synthetase is a multifunctional
molecule: its expression and regulation.";
Endocrinology 141:710-721(2000).
[12]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=8815894;
Beuckmann C.T., Gordon W.C., Kanaoka Y., Eguchi N., Marcheselli V.L.,
Gerashchenko D.Y., Urade Y., Hayaishi O., Bazan N.G.;
"Lipocalin-type prostaglandin D synthase (beta-trace) is located in
pigment epithelial cells of rat retina and accumulates within
interphotoreceptor matrix.";
J. Neurosci. 16:6119-6124(1996).
[13]
TISSUE SPECIFICITY.
PubMed=8415655; DOI=10.1073/pnas.90.19.9070;
Urade Y., Kitahama K., Ohishi H., Kaneko T., Mizuno N., Hayaishi O.;
"Dominant expression of mRNA for prostaglandin D synthase in
leptomeninges, choroid plexus, and oligodendrocytes of the adult rat
brain.";
Proc. Natl. Acad. Sci. U.S.A. 90:9070-9074(1993).
[14]
TISSUE SPECIFICITY.
PubMed=9430563;
Gerashchenko D.Y., Beuckmann C.T., Marcheselli V.L., Gordon W.C.,
Kanaoka Y., Eguchi N., Urade Y., Hayaishi O., Bazan N.G.;
"Localization of lipocalin-type prostaglandin D synthase (beta-trace)
in iris, ciliary body, and eye fluids.";
Invest. Ophthalmol. Vis. Sci. 39:198-203(1998).
[15]
TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION BY
DIHYDROTESTOSTERONE.
PubMed=9746734; DOI=10.1095/biolreprod59.4.843;
Sorrentino C., Silvestrini B., Braghiroli L., Chung S.S.W.,
Giacomelli S., Leone M.-G., Xie Y.-B., Sui Y.-P., Mo M.-Y.,
Cheng C.Y.;
"Rat prostaglandin D2 synthetase: its tissue distribution, changes
during maturation, and regulation in the testis and epididymis.";
Biol. Reprod. 59:843-853(1998).
[16]
INDUCTION BY THYROID HORMONE AND RETINOIDS.
PubMed=9582446; DOI=10.1016/S0169-328X(98)00015-1;
Garcia-Fernandez L.F., Urade Y., Hayaishi O., Bernal J., Munoz A.;
"Identification of a thyroid hormone response element in the promoter
region of the rat lipocalin-type prostaglandin D synthase (beta-trace)
gene.";
Brain Res. Mol. Brain Res. 55:321-330(1998).
[17]
INDUCTION BY IL-1 BETA, AND REPRESSION BY NOTCH-HES.
PubMed=12488457; DOI=10.1074/jbc.M208288200;
Fujimori K., Fujitani Y., Kadoyama K., Kumanogoh H., Ishikawa K.,
Urade Y.;
"Regulation of lipocalin-type prostaglandin D synthase gene expression
by Hes-1 through E-box and interleukin-1 beta via two NF-kappaB
elements in rat leptomeningeal cells.";
J. Biol. Chem. 278:6018-6026(2003).
[18]
SIMILARITY TO THE LIPOCALIN FAMILY.
PubMed=1723819; DOI=10.1016/0968-0004(91)90149-P;
Peitsch M.C., Boguski M.S.;
"The first lipocalin with enzymatic activity.";
Trends Biochem. Sci. 16:363-363(1991).
-!- FUNCTION: Catalyzes the conversion of PGH2 to PGD2, a
prostaglandin involved in smooth muscle contraction/relaxation and
a potent inhibitor of platelet aggregation. Involved in a variety
of CNS functions, such as sedation, NREM sleep and PGE2-induced
allodynia, and may have an anti-apoptotic role in
oligodendrocytes. Binds small non-substrate lipophilic molecules,
including biliverdin, bilirubin, retinal, retinoic acid and
thyroid hormone, and may act as a scavenger for harmful
hydrophopic molecules and as a secretory retinoid and thyroid
hormone transporter. Possibly involved in development and
maintenance of the blood-brain, blood-retina, blood-aqueous humor
and blood-testis barrier. It is likely to play important roles in
both maturation and maintenance of the central nervous system and
male reproductive system. {ECO:0000269|PubMed:10387044,
ECO:0000269|PubMed:10650953, ECO:0000269|PubMed:11058225,
ECO:0000269|PubMed:9188476}.
-!- CATALYTIC ACTIVITY: (5Z,13E,15S)-9-alpha,11-alpha-epidioxy-15-
hydroxyprosta-5,13-dienoate = (5Z,13E,15S)-9-alpha,15-dihydroxy-
11-oxoprosta-5,13-dienoate.
-!- SUBUNIT: Monomer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum. Nucleus
membrane. Golgi apparatus. Cytoplasm, perinuclear region.
Secreted. Note=Detected on rough endoplasmic reticulum of
arachnoid and menigioma cells. Localized to the nuclear envelope,
Golgi apparatus, secretory vesicles and spherical cytoplasmic
structures in arachnoid trabecular cells, and to circular
cytoplasmic structures in meningeal macrophages and perivascular
microglial cells. In oligodendrocytes, localized to the rough
endoplasmic reticulum and nuclear envelope. In retinal pigment
epithelial cells, localized to distinct cytoplasmic domains
including the perinuclear region. Also secreted.
-!- TISSUE SPECIFICITY: Abundant in the brain and CNS, where it is
expressed in tissues of the blood-brain barrier and secreted into
the cerebro-spinal fluid. In the eye, it is expressed in the
pigmented epithelium of the retina and the nonpigmented epithelium
of the iris and ciliary body, and accumulates within the
interphotoreceptor matrix, photoreceptors, and aqueous and
vitreous humors. In the male reproductive system, it is expressed
in the testis and epididymis, and is secreted into the seminal
fluid. It has also been detected in the cochlea.
{ECO:0000269|PubMed:10650953, ECO:0000269|PubMed:11058225,
ECO:0000269|PubMed:11565799, ECO:0000269|PubMed:2642896,
ECO:0000269|PubMed:8415655, ECO:0000269|PubMed:8599604,
ECO:0000269|PubMed:8815894, ECO:0000269|PubMed:9430563,
ECO:0000269|PubMed:9746734}.
-!- DEVELOPMENTAL STAGE: In the brain it is localized in many neurons
at 1-2 weeks after birth, whereas in mature animals it is
localized to tissues of the blood-brain barrier.
{ECO:0000269|PubMed:9746734}.
-!- INDUCTION: By IL-1 beta and thyroid hormone. Probably induced by
dexamethasone, dihydrotestosterone, progesterone, retinoic acid
and retinal. Repressed by the Notch-Hes signaling pathway.
{ECO:0000269|PubMed:10650953, ECO:0000269|PubMed:12488457,
ECO:0000269|PubMed:9582446, ECO:0000269|PubMed:9746734}.
-!- DOMAIN: Forms a beta-barrel structure that accommodates
hydrophobic ligands in its interior. {ECO:0000250}.
-!- MASS SPECTROMETRY: Mass=18808; Method=MALDI; Range=25-189;
Evidence={ECO:0000269|PubMed:11565799};
-!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; J04488; AAA41839.1; -; mRNA.
EMBL; M94134; AAA41840.1; -; Genomic_DNA.
EMBL; S66190; -; NOT_ANNOTATED_CDS; mRNA.
PIR; A32202; A32202.
PIR; S65717; S65717.
RefSeq; NP_037147.1; NM_013015.2.
UniGene; Rn.11400; -.
ProteinModelPortal; P22057; -.
SMR; P22057; -.
BioGrid; 247558; 2.
STRING; 10116.ENSRNOP00000020926; -.
iPTMnet; P22057; -.
PaxDb; P22057; -.
PRIDE; P22057; -.
Ensembl; ENSRNOT00000020926; ENSRNOP00000020926; ENSRNOG00000015550.
GeneID; 25526; -.
KEGG; rno:25526; -.
UCSC; RGD:3433; rat.
CTD; 5730; -.
RGD; 3433; Ptgds.
eggNOG; ENOG410II11; Eukaryota.
eggNOG; ENOG4111YRI; LUCA.
GeneTree; ENSGT00620000088005; -.
HOGENOM; HOG000231660; -.
HOVERGEN; HBG106490; -.
InParanoid; P22057; -.
KO; K01830; -.
OMA; KGPGQDF; -.
OrthoDB; EOG091G0NAJ; -.
PhylomeDB; P22057; -.
TreeFam; TF336103; -.
BRENDA; 5.3.99.2; 5301.
Reactome; R-RNO-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
PRO; PR:P22057; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000015550; -.
Genevisible; P22057; RN.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; NAS:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005791; C:rough endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0004667; F:prostaglandin-D synthase activity; IDA:UniProtKB.
GO; GO:0005501; F:retinoid binding; IDA:UniProtKB.
GO; GO:0036094; F:small molecule binding; IEA:InterPro.
GO; GO:2000255; P:negative regulation of male germ cell proliferation; IEA:Ensembl.
GO; GO:0001516; P:prostaglandin biosynthetic process; IDA:UniProtKB.
GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; ISS:UniProtKB.
GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
Gene3D; 2.40.128.20; -; 1.
InterPro; IPR012674; Calycin.
InterPro; IPR002345; Lipocalin.
InterPro; IPR022272; Lipocalin_CS.
InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
InterPro; IPR002972; PstgldnD_synth.
PANTHER; PTHR11430; PTHR11430; 1.
PANTHER; PTHR11430:SF86; PTHR11430:SF86; 1.
Pfam; PF00061; Lipocalin; 1.
SUPFAM; SSF50814; SSF50814; 1.
PROSITE; PS00213; LIPOCALIN; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Direct protein sequencing;
Disulfide bond; Endoplasmic reticulum; Fatty acid biosynthesis;
Fatty acid metabolism; Glycoprotein; Golgi apparatus; Isomerase;
Lipid biosynthesis; Lipid metabolism; Membrane; Nucleus;
Prostaglandin biosynthesis; Prostaglandin metabolism;
Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal;
Transport.
SIGNAL 1 24
CHAIN 25 189 Prostaglandin-H2 D-isomerase.
/FTId=PRO_0000017950.
ACT_SITE 65 65 Nucleophile.
{ECO:0000269|PubMed:7836410}.
MOD_RES 25 25 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:11565799}.
CARBOHYD 51 51 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:2642896}.
CARBOHYD 78 78 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:2642896}.
DISULFID 89 186 {ECO:0000269|PubMed:7836410}.
MUTAGEN 65 65 C->A,S: Loss of enzymatic activity.
{ECO:0000269|PubMed:7836410}.
MUTAGEN 89 89 C->A,S: Disrupts disulfide bond.
{ECO:0000269|PubMed:7836410}.
MUTAGEN 186 186 C->A,S: Disrupts disulfide bond.
{ECO:0000269|PubMed:7836410}.
CONFLICT 138 138 G -> A (in Ref. 6; S66190).
{ECO:0000305}.
CONFLICT 144 144 R -> G (in Ref. 6; S66190).
{ECO:0000305}.
SEQUENCE 189 AA; 21301 MW; 866E4CFE0F814FDC CRC64;
MAALPMLWTG LVLLGLLGFP QTPAQGHDTV QPNFQQDKFL GRWYSAGLAS NSSWFREKKE
LLFMCQTVVA PSTEGGLNLT STFLRKNQCE TKVMVLQPAG VPGQYTYNSP HWGSFHSLSV
VETDYDEYAF LFSKGTKGPG QDFRMATLYS RAQLLKEELK EKFITFSKDQ GLTEEDIVFL
PQPDKCIQE


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6017 Snell Ave, Ste 357
San Jose, CA 95123




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