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O09114

- PTGDS_MOUSE

UniProt

O09114 - PTGDS_MOUSE

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Protein
Prostaglandin-H2 D-isomerase
Gene
Ptgds
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.8 Publications

Catalytic activityi

(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.2 Publications

Kineticsi

  1. KM=0.8 µM for prostaglandin H21 Publication

Vmax=5.9 µmol/min/mg enzyme

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei65 – 651Nucleophile

GO - Molecular functioni

  1. fatty acid binding Source: Ensembl
  2. prostaglandin-D synthase activity Source: UniProtKB
  3. retinoid binding Source: UniProtKB
  4. transporter activity Source: UniProtKB

GO - Biological processi

  1. prostaglandin biosynthetic process Source: UniProtKB
  2. regulation of circadian sleep/wake cycle, sleep Source: UniProtKB
  3. response to glucocorticoid Source: Ensembl
  4. transport Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Prostaglandin biosynthesis, Prostaglandin metabolism, Transport

Enzyme and pathway databases

BRENDAi5.3.99.2. 3474.
ReactomeiREACT_188623. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).

Names & Taxonomyi

Protein namesi
Recommended name:
Prostaglandin-H2 D-isomerase (EC:5.3.99.2)
Alternative name(s):
Glutathione-independent PGD synthase
Lipocalin-type prostaglandin-D synthase
Prostaglandin-D2 synthase
Short name:
L-PGDS
Short name:
PGD2 synthase
Short name:
PGDS2
Gene namesi
Name:Ptgds
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:99261. Ptgds.

Subcellular locationi

Rough endoplasmic reticulum By similarity. Nucleus membrane By similarity. Golgi apparatus By similarity. Cytoplasmperinuclear region By similarity. Secreted By similarity
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 By similarity.

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB
  2. extracellular region Source: UniProtKB
  3. extracellular space Source: Ensembl
  4. nuclear membrane Source: UniProtKB-SubCell
  5. perinuclear region of cytoplasm Source: UniProtKB-SubCell
  6. rough endoplasmic reticulum Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Membrane, Nucleus, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi45 – 451S → A: Reduces enzyme activity by about half. Reduces enzyme activity tenfold; when associated with A-67 and A-81. 1 Publication
Mutagenesisi65 – 651C → A: Loss of enzyme activity. No effect on ligand binding. 1 Publication
Mutagenesisi67 – 671T → A: Reduces enzyme activity by about half. Reduces enzyme activity tenfold; when associated with A-45 and A-81. 1 Publication
Mutagenesisi81 – 811S → A: Slightly reduced enzyme activity. half. Reduces enzyme activity tenfold; when associated with A-45 and A-67. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424 By similarity
Add
BLAST
Chaini25 – 189165Prostaglandin-H2 D-isomerase
PRO_0000017947Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251Pyrrolidone carboxylic acid By similarity
Glycosylationi51 – 511N-linked (GlcNAc...) By similarity
Glycosylationi78 – 781N-linked (GlcNAc...) By similarity
Disulfide bondi89 ↔ 1861 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

MaxQBiO09114.
PaxDbiO09114.
PRIDEiO09114.

PTM databases

PhosphoSiteiO09114.

Expressioni

Tissue specificityi

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 male reproductive system, it is expressed in the testis, efferent ducts and epididymis, and is secreted into the seminal fluid. In the eye, it is expressed in the pigmented epithelium of the retina and the nonpigmented epithelium of the ciliary body, and secreted into the aqueous humor. Low levels detected in various tissue fluids such as serum, normal urine, ascitic fluid and tear fluid. Also found in a number of other organs including the ear, heart and lung.4 Publications

Developmental stagei

Initially detected at 14.5 dpc in the mesenchymal cells of the brain. Later in development, observed in the choroid plexus and within single cells in the brain.

Inductioni

By IL-1 beta and thyroid hormone. Probably induced by dexamethasone, dihydrotestosterone, progesterone, retinoic acid and retinal. Repressed by the Notch-Hes signaling pathway.1 Publication

Gene expression databases

BgeeiO09114.
CleanExiMM_PTGDS.
GenevestigatoriO09114.

Interactioni

Subunit structurei

Monomer By similarity.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 293
Helixi36 – 394
Beta strandi41 – 5010
Helixi55 – 584
Turni59 – 613
Beta strandi66 – 716
Beta strandi75 – 8511
Beta strandi89 – 9810
Beta strandi104 – 1074
Beta strandi110 – 1134
Beta strandi116 – 1249
Turni125 – 1273
Beta strandi128 – 1347
Turni137 – 1404
Beta strandi144 – 15411
Helixi157 – 16913
Helixi174 – 1763
Beta strandi177 – 1793
Beta strandi184 – 1874

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CZTX-ray2.00A25-189[»]
2CZUX-ray2.10A/B25-189[»]
2E4JNMR-A25-189[»]
2KTDNMR-A25-189[»]
2RQ0NMR-A25-189[»]
ProteinModelPortaliO09114.
SMRiO09114. Positions 35-189.

Miscellaneous databases

EvolutionaryTraceiO09114.

Family & Domainsi

Domaini

Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.3 Publications

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG45731.
GeneTreeiENSGT00620000088005.
HOGENOMiHOG000231660.
HOVERGENiHBG106490.
InParanoidiO09114.
KOiK01830.
OMAiPGQDFRM.
OrthoDBiEOG78PVBH.
PhylomeDBiO09114.
TreeFamiTF336103.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002972. PstgldnD_synth.
[Graphical view]
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00179. LIPOCALIN.
PR01254. PGNDSYNTHASE.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00213. LIPOCALIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O09114-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MAALRMLWMG LVLLGLLGFP QTPAQGHDTV QPNFQQDKFL GRWYSAGLAS    50
NSSWFREKKA VLYMCKTVVA PSTEGGLNLT STFLRKNQCE TKIMVLQPAG 100
APGHYTYSSP HSGSIHSVSV VEANYDEYAL LFSRGTKGPG QDFRMATLYS 150
RTQTLKDELK EKFTTFSKAQ GLTEEDIVFL PQPDKCIQE 189
Length:189
Mass (Da):21,066
Last modified:July 1, 1997 - v1
Checksum:iC2C0B3E3B5928643
GO
Isoform 2 (identifier: O09114-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-63: Missing.

Note: No experimental confirmation available.

Show »
Length:126
Mass (Da):13,941
Checksum:i7F9FEDCFBEFF99A6
GO

Sequence cautioni

The sequence BAA21769.1 differs from that shown. Reason: Frameshift at position 47.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6363Missing in isoform 2.
VSP_041029Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X89222 mRNA. Translation: CAA61506.1.
Y10138 Genomic DNA. Translation: CAA71226.1.
AB006361 mRNA. Translation: BAA21769.1. Frameshift.
D83329 Genomic DNA. Translation: BAA74461.1.
AK131859 mRNA. Translation: BAE20833.1.
CH466542 Genomic DNA. Translation: EDL08250.1.
CH466542 Genomic DNA. Translation: EDL08251.1.
BC038083 mRNA. Translation: AAH38083.1.
BC043015 mRNA. Translation: AAH43015.1.
CCDSiCCDS38074.1. [O09114-1]
PIRiS57748.
RefSeqiNP_032989.2. NM_008963.2. [O09114-1]
XP_006497849.1. XM_006497786.1. [O09114-1]
XP_006497850.1. XM_006497787.1. [O09114-1]
UniGeneiMm.1008.

Genome annotation databases

EnsembliENSMUST00000015234; ENSMUSP00000015234; ENSMUSG00000015090. [O09114-1]
ENSMUST00000114251; ENSMUSP00000109889; ENSMUSG00000015090. [O09114-1]
ENSMUST00000114259; ENSMUSP00000109897; ENSMUSG00000015090. [O09114-1]
GeneIDi19215.
KEGGimmu:19215.
UCSCiuc008isf.1. mouse. [O09114-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X89222 mRNA. Translation: CAA61506.1 .
Y10138 Genomic DNA. Translation: CAA71226.1 .
AB006361 mRNA. Translation: BAA21769.1 . Frameshift.
D83329 Genomic DNA. Translation: BAA74461.1 .
AK131859 mRNA. Translation: BAE20833.1 .
CH466542 Genomic DNA. Translation: EDL08250.1 .
CH466542 Genomic DNA. Translation: EDL08251.1 .
BC038083 mRNA. Translation: AAH38083.1 .
BC043015 mRNA. Translation: AAH43015.1 .
CCDSi CCDS38074.1. [O09114-1 ]
PIRi S57748.
RefSeqi NP_032989.2. NM_008963.2. [O09114-1 ]
XP_006497849.1. XM_006497786.1. [O09114-1 ]
XP_006497850.1. XM_006497787.1. [O09114-1 ]
UniGenei Mm.1008.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CZT X-ray 2.00 A 25-189 [» ]
2CZU X-ray 2.10 A/B 25-189 [» ]
2E4J NMR - A 25-189 [» ]
2KTD NMR - A 25-189 [» ]
2RQ0 NMR - A 25-189 [» ]
ProteinModelPortali O09114.
SMRi O09114. Positions 35-189.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi O09114.
ChEMBLi CHEMBL4334.

PTM databases

PhosphoSitei O09114.

Proteomic databases

MaxQBi O09114.
PaxDbi O09114.
PRIDEi O09114.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000015234 ; ENSMUSP00000015234 ; ENSMUSG00000015090 . [O09114-1 ]
ENSMUST00000114251 ; ENSMUSP00000109889 ; ENSMUSG00000015090 . [O09114-1 ]
ENSMUST00000114259 ; ENSMUSP00000109897 ; ENSMUSG00000015090 . [O09114-1 ]
GeneIDi 19215.
KEGGi mmu:19215.
UCSCi uc008isf.1. mouse. [O09114-1 ]

Organism-specific databases

CTDi 5730.
MGIi MGI:99261. Ptgds.

Phylogenomic databases

eggNOGi NOG45731.
GeneTreei ENSGT00620000088005.
HOGENOMi HOG000231660.
HOVERGENi HBG106490.
InParanoidi O09114.
KOi K01830.
OMAi PGQDFRM.
OrthoDBi EOG78PVBH.
PhylomeDBi O09114.
TreeFami TF336103.

Enzyme and pathway databases

BRENDAi 5.3.99.2. 3474.
Reactomei REACT_188623. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).

Miscellaneous databases

ChiTaRSi PTGDS. mouse.
EvolutionaryTracei O09114.
NextBioi 295972.
PROi O09114.
SOURCEi Search...

Gene expression databases

Bgeei O09114.
CleanExi MM_PTGDS.
Genevestigatori O09114.

Family and domain databases

Gene3Di 2.40.128.20. 1 hit.
InterProi IPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002972. PstgldnD_synth.
[Graphical view ]
Pfami PF00061. Lipocalin. 1 hit.
[Graphical view ]
PRINTSi PR00179. LIPOCALIN.
PR01254. PGNDSYNTHASE.
SUPFAMi SSF50814. SSF50814. 1 hit.
PROSITEi PS00213. LIPOCALIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Developmental expression of murine Beta-trace in embryos and adult animals suggests a function in maturation and maintenance of blood-tissue barriers."
    Hoffmann A., Baechner D., Betat N., Lauber J., Gross G.
    Dev. Dyn. 207:332-343(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    Strain: NMRI.
    Tissue: Brain.
  2. Hoffmann A., Steinert P., Lauber J., Gross G.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
  3. "Isolation of putative prostaglandin D synthetase from mouse choroid plexus."
    Kita H., Kawamoto S., Okubo K., Matsubara K.
    Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C57BL/6.
    Tissue: Brain.
  4. "Lack of tactile pain (allodynia) in lipocalin-type prostaglandin D synthase-deficient mice."
    Eguchi N., Minami T., Shirafuji N., Kanaoka Y., Tanaka T., Nagata A., Yoshida N., Urade Y., Ito S., Hayaishi O.
    Proc. Natl. Acad. Sci. U.S.A. 96:726-730(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    Strain: 129/Sv.
    Tissue: Liver.
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Small intestine.
  6. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Eye.
  8. "Prostaglandin D synthase gene is involved in the regulation of non-rapid eye movement sleep."
    Pinzar E., Kanaoka Y., Inui T., Eguchi N., Urade Y., Hayaishi O.
    Proc. Natl. Acad. Sci. U.S.A. 97:4903-4907(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Pronounced eosinophilic lung inflammation and Th2 cytokine release in human lipocalin-type prostaglandin D synthase transgenic mice."
    Fujitani Y., Kanaoka Y., Aritake K., Uodome N., Okazaki-Hatake K., Urade Y.
    J. Immunol. 168:443-449(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  10. "Perineuronal oligodendrocytes protect against neuronal apoptosis through the production of lipocalin-type prostaglandin D synthase in a genetic demyelinating model."
    Taniike M., Mohri I., Eguchi N., Beuckmann C.T., Suzuki K., Urade Y.
    J. Neurosci. 22:4885-4896(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Stage and region-specific localization of lipocalin-type prostaglandin D synthase in the adult murine testis and epididymis."
    Gerena R.L., Eguchi N., Urade Y., Killian G.J.
    J. Androl. 21:848-854(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  12. "Dexamethasone induces lipocalin-type prostaglandin D synthase gene expression in mouse neuronal cells."
    Garcia-Fernandez L.F., Iniguez M.A., Eguchi N., Fresno M., Urade Y., Munoz A.
    J. Neurochem. 75:460-470(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY DEXAMETHASONE.
  13. "Structural basis of multi-functional lipocalin-type prostaglandin D synthase."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 24-189.
  14. "NMR solution structure of lipocalin-type prostaglandin D synthase: evidence for partial overlapping of catalytic pocket and retinoic acid-binding pocket within the central cavity."
    Shimamoto S., Yoshida T., Inui T., Gohda K., Kobayashi Y., Fujimori K., Tsurumura T., Aritake K., Urade Y., Ohkubo T.
    J. Biol. Chem. 282:31373-31379(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 25-189, FUNCTION, CATALYTIC ACTIVITY, DOMAIN.
  15. "Structural basis of the catalytic mechanism operating in open-closed conformers of lipocalin type prostaglandin D synthase."
    Kumasaka T., Aritake K., Ago H., Irikura D., Tsurumura T., Yamamoto M., Miyano M., Urade Y., Hayaishi O.
    J. Biol. Chem. 284:22344-22352(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 25-189 OF MUTANT ALA-65 IN COMPLEX WITH RETINOIC ACID, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF SER-45; CYS-65; THR-67 AND SER-81, BIOPHYSICOCHEMICAL PROPERTIES, DISULFIDE BOND, DOMAIN.
  16. "Structural analysis of lipocalin-type prostaglandin D synthase complexed with biliverdin by small-angle X-ray scattering and multi-dimensional NMR."
    Miyamoto Y., Nishimura S., Inoue K., Shimamoto S., Yoshida T., Fukuhara A., Yamada M., Urade Y., Yagi N., Ohkubo T., Inui T.
    J. Struct. Biol. 169:209-218(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 25-189 IN COMPLEX WITH BILIVERDIN, FUNCTION, DOMAIN.

Entry informationi

Entry nameiPTGDS_MOUSE
AccessioniPrimary (citable) accession number: O09114
Secondary accession number(s): O09157
, O35091, Q3V2G5, Q62169
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: September 3, 2014
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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