ID A0A3L8SEL4_CHLGU Unreviewed; 242 AA.
AC A0A3L8SEL4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
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 ORFNames=DV515_00008976 {ECO:0000313|EMBL:RLW00549.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW00549.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLW00549.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLW00549.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLW00549.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLW00549.1}.
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DR EMBL; QUSF01000027; RLW00549.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8SEL4; -.
DR STRING; 44316.ENSEGOP00005011543; -.
DR Proteomes; UP000276834; 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:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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; 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; 2.
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:UP000276834};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..242
FT /note="Prostaglandin-H2 D-isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018018157"
FT DOMAIN 47..118
FT /note="Lipocalin/cytosolic fatty-acid binding"
FT /evidence="ECO:0000259|Pfam:PF00061"
FT DOMAIN 154..228
FT /note="Lipocalin/cytosolic fatty-acid binding"
FT /evidence="ECO:0000259|Pfam:PF00061"
SQ SEQUENCE 242 AA; 26755 MW; A7FB5EA19933EF6A CRC64;
MGFVTLQMNF SSSMATLLGI LGLALLGTLH AQDSIPVQAD FQQDKLTGRW YSIGLASNSN
WFKEKRHLMK MCTTIISTTP EGNLEVTSTY PKGDQCVTRN SLYTKTEQPG QFSYTNPREC
PASVGQLRTC LQSCCPCFCL VADLELRAEL CPMFPTGWGS KHNMHVVETN YEEYALVATQ
ISKGTGSSTM VLLYSRTKEL SPRRLEMFTQ FSREQGLTDN EILILPQTGE TGSTGMVSGS
RG
//
