ID G1RBR0_NOMLE Unreviewed; 190 AA.
AC G1RBR0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Prostaglandin-H2 D-isomerase {ECO:0000256|ARBA:ARBA00023891};
DE EC=5.3.99.2 {ECO:0000256|ARBA:ARBA00023799};
DE AltName: Full=Glutathione-independent PGD synthase {ECO:0000256|ARBA:ARBA00032350};
DE AltName: Full=Lipocalin-type prostaglandin-D synthase {ECO:0000256|ARBA:ARBA00031917};
DE AltName: Full=Prostaglandin-D2 synthase {ECO:0000256|ARBA:ARBA00030654};
GN Name=PTGDS {ECO:0000313|Ensembl:ENSNLEP00000010659.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000010659.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000010659.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000010659.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00023698};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000256|ARBA:ARBA00004556}. Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus
CC {ECO:0000256|ARBA:ARBA00004555}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}. Nucleus membrane
CC {ECO:0000256|ARBA:ARBA00004126}. Rough endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004427}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000256|ARBA:ARBA00006889, ECO:0000256|RuleBase:RU003695}.
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DR EMBL; ADFV01120824; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01120825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003279846.1; XM_003279798.3.
DR RefSeq; XP_012364406.1; XM_012508952.1.
DR AlphaFoldDB; G1RBR0; -.
DR STRING; 61853.ENSNLEP00000010659; -.
DR Ensembl; ENSNLET00000011177.2; ENSNLEP00000010659.1; ENSNLEG00000008707.2.
DR GeneID; 100592404; -.
DR KEGG; nle:100592404; -.
DR CTD; 5730; -.
DR eggNOG; ENOG502S6GK; Eukaryota.
DR GeneTree; ENSGT01100000263580; -.
DR HOGENOM; CLU_094061_1_1_1; -.
DR InParanoid; G1RBR0; -.
DR OMA; LPKTDQC; -.
DR OrthoDB; 5266874at2759; -.
DR TreeFam; TF336103; -.
DR Proteomes; UP000001073; Chromosome 8.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005504; F:fatty acid binding; IEA:Ensembl.
DR GO; GO:0004667; F:prostaglandin-D synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0005501; F:retinoid binding; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
DR GO; GO:2000255; P:negative regulation of male germ cell proliferation; IEA:Ensembl.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; IEA:Ensembl.
DR CDD; cd19419; lipocalin_L-PGDS; 1.
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 PANTHER; PTHR11430; LIPOCALIN; 1.
DR PANTHER; PTHR11430:SF86; PROSTAGLANDIN-H2 D-ISOMERASE; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR00179; LIPOCALIN.
DR PRINTS; PR01254; PGNDSYNTHASE.
DR SUPFAM; SSF50814; Lipocalins; 1.
DR PROSITE; PS00213; LIPOCALIN; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Mast cell degranulation {ECO:0000256|ARBA:ARBA00022675};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Prostaglandin biosynthesis {ECO:0000256|ARBA:ARBA00022585};
KW Prostaglandin metabolism {ECO:0000256|ARBA:ARBA00022501};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..190
FT /note="Prostaglandin-H2 D-isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003420803"
FT DOMAIN 41..184
FT /note="Lipocalin/cytosolic fatty-acid binding"
FT /evidence="ECO:0000259|Pfam:PF00061"
SQ SEQUENCE 190 AA; 20971 MW; FBB3E474A1338C1C CRC64;
MATHHTLWMG LALLGVLGGL QAAPEAQVSV QPNFQQDKFL GRWFSAGLAS NSSWLREKKA
ALSMCKSVVA PAADGGLNLT STFLRKNQCE TRTMLLQPAG SLGSYSYRSP HWGSTYSVSV
VETDYDQYAL LYSQGSKGPG EDFRMATLYS RTQTPRAELK EKFTTFCKAQ GFTEDTIVFL
PQTDKCMTEQ
//
