ID A0A452HDR8_9SAUR Unreviewed; 185 AA.
AC A0A452HDR8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
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};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000012955.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000012955.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A452HDR8; -.
DR STRING; 38772.ENSGAGP00000012955; -.
DR Ensembl; ENSGAGT00000014848.1; ENSGAGP00000012955.1; ENSGAGG00000009941.1.
DR Proteomes; UP000291020; 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 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:UP000291020};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..185
FT /note="Prostaglandin-H2 D-isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019387643"
FT DOMAIN 35..178
FT /note="Lipocalin/cytosolic fatty-acid binding"
FT /evidence="ECO:0000259|Pfam:PF00061"
SQ SEQUENCE 185 AA; 21034 MW; DCECC8E8A0892468 CRC64;
MQATLLSLLG LALFSVLHGQ EEVTVQPDFQ QEKFTGKWYS IGLASSSRWF MEKKQVLKMC
TTVITPTADG NLNVTSTYPK FDRCEKRNSL YIKTEQPGRF SYTSPRWGSQ HDIRVVETNY
DEYALLHAKK FKGTDTSTMV TLYGRTTELN PKLQEKFTQF SLAQGLPEDA ILLLPKTDKC
MTEAA
//
