ID G3W418_SARHA Unreviewed; 201 AA.
AC G3W418;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 2.
DT 27-MAR-2024, entry version 66.
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:ENSSHAP00000010173.2};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000010173.2, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000010173.2, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000010173.2}
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}.
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DR AlphaFoldDB; G3W418; -.
DR Ensembl; ENSSHAT00000010262.2; ENSSHAP00000010173.2; ENSSHAG00000008790.2.
DR GeneTree; ENSGT01100000263580; -.
DR HOGENOM; CLU_094061_3_1_1; -.
DR OrthoDB; 5266874at2759; -.
DR Proteomes; UP000007648; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0004667; F:prostaglandin-D synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0036094; F:small molecule binding; IEA:InterPro.
DR GO; GO:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR002345; Lipocalin.
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.
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 Milk protein {ECO:0000256|ARBA:ARBA00022743};
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:UP000007648};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..201
FT /note="Prostaglandin-H2 D-isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5029715504"
FT DOMAIN 42..184
FT /note="Lipocalin/cytosolic fatty-acid binding"
FT /evidence="ECO:0000259|Pfam:PF00061"
SQ SEQUENCE 201 AA; 22837 MW; 8F2CBFCEEF966A40 CRC64;
MMAMGLLWMG LALLQALETQ GQSQESPQEI PVQPDFLEDK FVGTWYSVGL ASTFPWFLKK
KAELMMCKTV LTPEADGTVN FTATFVSNNQ CETRTSLLRK TQQPGHYVYK SIKWGSEHNI
FVVETNYEEY SLLYTTKTKG NSNFNMATLY SRTKDVRPEL KERFISFAKS HGFTEDTIVI
LPKTVRSCTC LDHPLGPQAL L
//
