PTGDS_MOUSE
ID PTGDS_MOUSE Reviewed; 189 AA.
AC O09114; O09157; O35091; Q3V2G5; Q62169;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Prostaglandin-H2 D-isomerase;
DE EC=5.3.99.2 {ECO:0000269|PubMed:17715133, ECO:0000269|PubMed:19546224};
DE AltName: Full=Glutathione-independent PGD synthase;
DE AltName: Full=Lipocalin-type prostaglandin-D synthase;
DE AltName: Full=Prostaglandin-D2 synthase;
DE Short=L-PGDS;
DE Short=PGD2 synthase;
DE Short=PGDS2;
DE Flags: Precursor;
GN Name=Ptgds;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=NMRI; TISSUE=Brain;
RX PubMed=8922532;
RX DOI=10.1002/(sici)1097-0177(199611)207:3<332::aid-aja10>3.0.co;2-6;
RA Hoffmann A., Baechner D., Betat N., Lauber J., Gross G.;
RT "Developmental expression of murine Beta-trace in embryos and adult animals
RT suggests a function in maturation and maintenance of blood-tissue
RT barriers.";
RL Dev. Dyn. 207:332-343(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RA Hoffmann A., Steinert P., Lauber J., Gross G.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Kita H., Kawamoto S., Okubo K., Matsubara K.;
RT "Isolation of putative prostaglandin D synthetase from mouse choroid
RT plexus.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), FUNCTION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=129/Sv; TISSUE=Liver;
RX PubMed=9892701; DOI=10.1073/pnas.96.2.726;
RA Eguchi N., Minami T., Shirafuji N., Kanaoka Y., Tanaka T., Nagata A.,
RA Yoshida N., Urade Y., Ito S., Hayaishi O.;
RT "Lack of tactile pain (allodynia) in lipocalin-type prostaglandin D
RT synthase-deficient mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:726-730(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Small intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP FUNCTION.
RX PubMed=10781097; DOI=10.1073/pnas.090093997;
RA Pinzar E., Kanaoka Y., Inui T., Eguchi N., Urade Y., Hayaishi O.;
RT "Prostaglandin D synthase gene is involved in the regulation of non-rapid
RT eye movement sleep.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:4903-4907(2000).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11751991; DOI=10.4049/jimmunol.168.1.443;
RA Fujitani Y., Kanaoka Y., Aritake K., Uodome N., Okazaki-Hatake K.,
RA Urade Y.;
RT "Pronounced eosinophilic lung inflammation and Th2 cytokine release in
RT human lipocalin-type prostaglandin D synthase transgenic mice.";
RL J. Immunol. 168:443-449(2002).
RN [10]
RP FUNCTION.
RX PubMed=12077186; DOI=10.1523/jneurosci.22-12-04885.2002;
RA Taniike M., Mohri I., Eguchi N., Beuckmann C.T., Suzuki K., Urade Y.;
RT "Perineuronal oligodendrocytes protect against neuronal apoptosis through
RT the production of lipocalin-type prostaglandin D synthase in a genetic
RT demyelinating model.";
RL J. Neurosci. 22:4885-4896(2002).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=11105911;
RA Gerena R.L., Eguchi N., Urade Y., Killian G.J.;
RT "Stage and region-specific localization of lipocalin-type prostaglandin D
RT synthase in the adult murine testis and epididymis.";
RL J. Androl. 21:848-854(2000).
RN [12]
RP INDUCTION BY DEXAMETHASONE.
RX PubMed=10899920; DOI=10.1046/j.1471-4159.2000.0750460.x;
RA Garcia-Fernandez L.F., Iniguez M.A., Eguchi N., Fresno M., Urade Y.,
RA Munoz A.;
RT "Dexamethasone induces lipocalin-type prostaglandin D synthase gene
RT expression in mouse neuronal cells.";
RL J. Neurochem. 75:460-470(2000).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23624557; DOI=10.1038/ni.2586;
RA Taketomi Y., Ueno N., Kojima T., Sato H., Murase R., Yamamoto K.,
RA Tanaka S., Sakanaka M., Nakamura M., Nishito Y., Kawana M., Kambe N.,
RA Ikeda K., Taguchi R., Nakamizo S., Kabashima K., Gelb M.H., Arita M.,
RA Yokomizo T., Nakamura M., Watanabe K., Hirai H., Nakamura M., Okayama Y.,
RA Ra C., Aritake K., Urade Y., Morimoto K., Sugimoto Y., Shimizu T.,
RA Narumiya S., Hara S., Murakami M.;
RT "Mast cell maturation is driven via a group III phospholipase A2-
RT prostaglandin D2-DP1 receptor paracrine axis.";
RL Nat. Immunol. 14:554-563(2013).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 24-189.
RG RIKEN structural genomics initiative (RSGI);
RT "Structural basis of multi-functional lipocalin-type prostaglandin D
RT synthase.";
RL Submitted (OCT-2006) to the PDB data bank.
RN [16]
RP STRUCTURE BY NMR OF 25-189, FUNCTION, CATALYTIC ACTIVITY, AND DOMAIN.
RX PubMed=17715133; DOI=10.1074/jbc.m700123200;
RA Shimamoto S., Yoshida T., Inui T., Gohda K., Kobayashi Y., Fujimori K.,
RA Tsurumura T., Aritake K., Urade Y., Ohkubo T.;
RT "NMR solution structure of lipocalin-type prostaglandin D synthase:
RT evidence for partial overlapping of catalytic pocket and retinoic acid-
RT binding pocket within the central cavity.";
RL J. Biol. Chem. 282:31373-31379(2007).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 25-189 OF MUTANT ALA-65 IN COMPLEX
RP WITH RETINOIC ACID, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF SER-45;
RP CYS-65; THR-67 AND SER-81, BIOPHYSICOCHEMICAL PROPERTIES, DISULFIDE BOND,
RP AND DOMAIN.
RX PubMed=19546224; DOI=10.1074/jbc.m109.018341;
RA Kumasaka T., Aritake K., Ago H., Irikura D., Tsurumura T., Yamamoto M.,
RA Miyano M., Urade Y., Hayaishi O.;
RT "Structural basis of the catalytic mechanism operating in open-closed
RT conformers of lipocalin type prostaglandin D synthase.";
RL J. Biol. Chem. 284:22344-22352(2009).
RN [18]
RP STRUCTURE BY NMR OF 25-189 IN COMPLEX WITH BILIVERDIN, FUNCTION, AND
RP DOMAIN.
RX PubMed=19833210; DOI=10.1016/j.jsb.2009.10.005;
RA Miyamoto Y., Nishimura S., Inoue K., Shimamoto S., Yoshida T., Fukuhara A.,
RA Yamada M., Urade Y., Yagi N., Ohkubo T., Inui T.;
RT "Structural analysis of lipocalin-type prostaglandin D synthase complexed
RT with biliverdin by small-angle X-ray scattering and multi-dimensional
RT NMR.";
RL J. Struct. Biol. 169:209-218(2010).
CC -!- FUNCTION: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin
CC involved in smooth muscle contraction/relaxation and a potent inhibitor
CC of platelet aggregation. Involved in a variety of CNS functions, such
CC as sedation, NREM sleep and PGE2-induced allodynia, and may have an
CC anti-apoptotic role in oligodendrocytes. Binds small non-substrate
CC lipophilic molecules, including biliverdin, bilirubin, retinal,
CC retinoic acid and thyroid hormone, and may act as a scavenger for
CC harmful hydrophobic molecules and as a secretory retinoid and thyroid
CC hormone transporter. Possibly involved in development and maintenance
CC of the blood-brain, blood-retina, blood-aqueous humor and blood-testis
CC barrier. It is likely to play important roles in both maturation and
CC maintenance of the central nervous system and male reproductive system
CC (PubMed:10781097, PubMed:11751991, PubMed:12077186, PubMed:17715133,
CC PubMed:19546224, PubMed:19833210, PubMed:8922532, PubMed:9892701).
CC Involved in PLA2G3-dependent maturation of mast cells. PLA2G3 is
CC secreted by immature mast cells and acts on nearby fibroblasts upstream
CC to PTDGS to synthesize PGD2, which in turn promotes mast cell
CC maturation and degranulation via PTGDR (PubMed:23624557).
CC {ECO:0000269|PubMed:10781097, ECO:0000269|PubMed:11751991,
CC ECO:0000269|PubMed:12077186, ECO:0000269|PubMed:17715133,
CC ECO:0000269|PubMed:19546224, ECO:0000269|PubMed:19833210,
CC ECO:0000269|PubMed:23624557, ECO:0000269|PubMed:8922532,
CC ECO:0000269|PubMed:9892701}.
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:17715133, ECO:0000269|PubMed:19546224};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.8 uM for prostaglandin H2 {ECO:0000269|PubMed:19546224};
CC Vmax=5.9 umol/min/mg enzyme {ECO:0000269|PubMed:19546224};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P41222}.
CC -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P41222}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P41222}. Golgi apparatus
CC {ECO:0000250|UniProtKB:P41222}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P41222}. Secreted
CC {ECO:0000250|UniProtKB:P41222}. Note=Detected on rough endoplasmic
CC reticulum of arachnoid and menigioma cells. Localized to the nuclear
CC envelope, Golgi apparatus, secretory vesicles and spherical cytoplasmic
CC structures in arachnoid trabecular cells, and to circular cytoplasmic
CC structures in meningeal macrophages and perivascular microglial cells.
CC In oligodendrocytes, localized to the rough endoplasmic reticulum and
CC nuclear envelope. In retinal pigment epithelial cells, localized to
CC distinct cytoplasmic domains including the perinuclear region. Also
CC secreted. {ECO:0000250|UniProtKB:P41222}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O09114-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O09114-2; Sequence=VSP_041029;
CC -!- TISSUE SPECIFICITY: Abundant in the brain and CNS, where it is
CC expressed in tissues of the blood-brain barrier and secreted into the
CC cerebro-spinal fluid. In the male reproductive system, it is expressed
CC in the testis, efferent ducts and epididymis, and is secreted into the
CC seminal fluid. In the eye, it is expressed in the pigmented epithelium
CC of the retina and the nonpigmented epithelium of the ciliary body, and
CC secreted into the aqueous humor. Low levels detected in various tissue
CC fluids such as serum, normal urine, ascitic fluid and tear fluid. Also
CC found in a number of other organs including the ear, heart and lung.
CC {ECO:0000269|PubMed:11105911, ECO:0000269|PubMed:11751991,
CC ECO:0000269|PubMed:8922532, ECO:0000269|PubMed:9892701}.
CC -!- DEVELOPMENTAL STAGE: Initially detected at 14.5 dpc in the mesenchymal
CC cells of the brain. Later in development, observed in the choroid
CC plexus and within single cells in the brain.
CC -!- INDUCTION: By IL-1 beta and thyroid hormone. Probably induced by
CC dexamethasone, dihydrotestosterone, progesterone, retinoic acid and
CC retinal. Repressed by the Notch-Hes signaling pathway.
CC {ECO:0000269|PubMed:10899920}.
CC -!- DOMAIN: Forms a beta-barrel structure that accommodates hydrophobic
CC ligands in its interior. {ECO:0000269|PubMed:17715133,
CC ECO:0000269|PubMed:19546224, ECO:0000269|PubMed:19833210}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice show decreased susceptibility to
CC passive cutaneous anaphylaxis associated with decreased mast cell
CC degranulation. {ECO:0000269|PubMed:23624557}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA21769.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X89222; CAA61506.1; -; mRNA.
DR EMBL; Y10138; CAA71226.1; -; Genomic_DNA.
DR EMBL; AB006361; BAA21769.1; ALT_FRAME; mRNA.
DR EMBL; D83329; BAA74461.1; -; Genomic_DNA.
DR EMBL; AK131859; BAE20833.1; -; mRNA.
DR EMBL; CH466542; EDL08250.1; -; Genomic_DNA.
DR EMBL; CH466542; EDL08251.1; -; Genomic_DNA.
DR EMBL; BC038083; AAH38083.1; -; mRNA.
DR EMBL; BC043015; AAH43015.1; -; mRNA.
DR CCDS; CCDS38074.1; -. [O09114-1]
DR PIR; S57748; S57748.
DR RefSeq; NP_032989.2; NM_008963.2. [O09114-1]
DR RefSeq; XP_006497849.1; XM_006497786.3. [O09114-1]
DR RefSeq; XP_006497850.1; XM_006497787.3. [O09114-1]
DR PDB; 2CZT; X-ray; 2.00 A; A=25-189.
DR PDB; 2CZU; X-ray; 2.10 A; A/B=25-189.
DR PDB; 2E4J; NMR; -; A=25-189.
DR PDB; 2KTD; NMR; -; A=25-189.
DR PDB; 2RQ0; NMR; -; A=25-189.
DR PDBsum; 2CZT; -.
DR PDBsum; 2CZU; -.
DR PDBsum; 2E4J; -.
DR PDBsum; 2KTD; -.
DR PDBsum; 2RQ0; -.
DR AlphaFoldDB; O09114; -.
DR BMRB; O09114; -.
DR SMR; O09114; -.
DR BioGRID; 202453; 14.
DR STRING; 10090.ENSMUSP00000015234; -.
DR BindingDB; O09114; -.
DR ChEMBL; CHEMBL4334; -.
DR DrugCentral; O09114; -.
DR GlyConnect; 2617; 11 N-Linked glycans (2 sites).
DR GlyGen; O09114; 2 sites, 11 N-linked glycans (2 sites).
DR PhosphoSitePlus; O09114; -.
DR MaxQB; O09114; -.
DR PaxDb; O09114; -.
DR PeptideAtlas; O09114; -.
DR PRIDE; O09114; -.
DR ProteomicsDB; 301897; -. [O09114-1]
DR ProteomicsDB; 301898; -. [O09114-2]
DR DNASU; 19215; -.
DR Ensembl; ENSMUST00000015234; ENSMUSP00000015234; ENSMUSG00000015090. [O09114-1]
DR Ensembl; ENSMUST00000114251; ENSMUSP00000109889; ENSMUSG00000015090. [O09114-1]
DR Ensembl; ENSMUST00000114259; ENSMUSP00000109897; ENSMUSG00000015090. [O09114-1]
DR GeneID; 19215; -.
DR KEGG; mmu:19215; -.
DR UCSC; uc008isf.1; mouse. [O09114-1]
DR CTD; 5730; -.
DR MGI; MGI:99261; Ptgds.
DR VEuPathDB; HostDB:ENSMUSG00000015090; -.
DR eggNOG; ENOG502S6GK; Eukaryota.
DR GeneTree; ENSGT01050000244979; -.
DR HOGENOM; CLU_094061_1_1_1; -.
DR InParanoid; O09114; -.
DR OMA; WFREKKS; -.
DR OrthoDB; 1341030at2759; -.
DR PhylomeDB; O09114; -.
DR TreeFam; TF336103; -.
DR BRENDA; 5.3.99.2; 3474.
DR Reactome; R-MMU-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR SABIO-RK; O09114; -.
DR BioGRID-ORCS; 19215; 1 hit in 59 CRISPR screens.
DR ChiTaRS; Ptgds; mouse.
DR EvolutionaryTrace; O09114; -.
DR PRO; PR:O09114; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O09114; protein.
DR Bgee; ENSMUSG00000015090; Expressed in vestibular membrane of cochlear duct and 218 other tissues.
DR Genevisible; O09114; MM.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005504; F:fatty acid binding; ISO:MGI.
DR GO; GO:0004667; F:prostaglandin-D synthase activity; IDA:UniProtKB.
DR GO; GO:0005501; F:retinoid binding; IDA:UniProtKB.
DR GO; GO:0036094; F:small molecule binding; IEA:InterPro.
DR GO; GO:0010467; P:gene expression; IDA:MGI.
DR GO; GO:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
DR GO; GO:2000255; P:negative regulation of male germ cell proliferation; IGI:MGI.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IDA:UniProtKB.
DR GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; IDA:UniProtKB.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR002345; Lipocalin.
DR InterPro; IPR022272; Lipocalin_CS.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR InterPro; IPR002972; PstgldnD_synth.
DR PANTHER; PTHR11430; PTHR11430; 1.
DR PANTHER; PTHR11430:SF86; PTHR11430:SF86; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00213; LIPOCALIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Disulfide bond;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Glycoprotein; Golgi apparatus; Isomerase; Lipid biosynthesis;
KW Lipid metabolism; Mast cell degranulation; Membrane; Nucleus;
KW Prostaglandin biosynthesis; Prostaglandin metabolism;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal;
KW Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000250|UniProtKB:P41222"
FT CHAIN 25..189
FT /note="Prostaglandin-H2 D-isomerase"
FT /id="PRO_0000017947"
FT ACT_SITE 65
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:19546224"
FT MOD_RES 25
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P22057"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 89..186
FT /evidence="ECO:0000269|PubMed:19546224"
FT VAR_SEQ 1..63
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_041029"
FT MUTAGEN 45
FT /note="S->A: Reduces enzyme activity by about half. Reduces
FT enzyme activity tenfold; when associated with A-67 and A-
FT 81."
FT /evidence="ECO:0000269|PubMed:19546224"
FT MUTAGEN 65
FT /note="C->A: Loss of enzyme activity. No effect on ligand
FT binding."
FT /evidence="ECO:0000269|PubMed:19546224"
FT MUTAGEN 67
FT /note="T->A: Reduces enzyme activity by about half. Reduces
FT enzyme activity tenfold; when associated with A-45 and A-
FT 81."
FT /evidence="ECO:0000269|PubMed:19546224"
FT MUTAGEN 81
FT /note="S->A: Slightly reduced enzyme activity. half.
FT Reduces enzyme activity tenfold; when associated with A-45
FT and A-67."
FT /evidence="ECO:0000269|PubMed:19546224"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:2E4J"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:2CZT"
FT STRAND 41..50
FT /evidence="ECO:0007829|PDB:2CZT"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:2CZT"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:2CZT"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:2CZT"
FT STRAND 75..85
FT /evidence="ECO:0007829|PDB:2CZT"
FT STRAND 89..98
FT /evidence="ECO:0007829|PDB:2CZT"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:2CZT"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:2CZT"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:2CZT"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:2CZT"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:2CZT"
FT TURN 137..140
FT /evidence="ECO:0007829|PDB:2RQ0"
FT STRAND 144..154
FT /evidence="ECO:0007829|PDB:2CZT"
FT HELIX 157..169
FT /evidence="ECO:0007829|PDB:2CZT"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:2CZT"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:2CZT"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:2CZU"
SQ SEQUENCE 189 AA; 21066 MW; C2C0B3E3B5928643 CRC64;
MAALRMLWMG LVLLGLLGFP QTPAQGHDTV QPNFQQDKFL GRWYSAGLAS NSSWFREKKA
VLYMCKTVVA PSTEGGLNLT STFLRKNQCE TKIMVLQPAG APGHYTYSSP HSGSIHSVSV
VEANYDEYAL LFSRGTKGPG QDFRMATLYS RTQTLKDELK EKFTTFSKAQ GLTEEDIVFL
PQPDKCIQE
