LOCUS NP_001076150 606 aa linear MAM 28-APR-2020
DEFINITION prostaglandin G/H synthase 1 precursor [Oryctolagus cuniculus].
ACCESSION NP_001076150
VERSION NP_001076150.1
DBSOURCE REFSEQ: accession NM_001082681.1
KEYWORDS RefSeq.
SOURCE Oryctolagus cuniculus (rabbit)
ORGANISM Oryctolagus cuniculus
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha;
Leporidae; Oryctolagus.
REFERENCE 1 (residues 1 to 606)
AUTHORS Okuda-Tanino A, Sugawara D, Tashiro T, Iwashita M, Obara Y, Moriya
T, Tsushima C, Saigusa D, Tomioka Y, Ishii K and Nakahata N.
TITLE Licochalcones extracted from Glycyrrhiza inflata inhibit platelet
aggregation accompanied by inhibition of COX-1 activity
JOURNAL PLoS ONE 12 (3), e0173628 (2017)
PUBMED 28282426
REMARK GeneRIF: These results suggest that licochalcones inhibit
collagen-induced platelet aggregation accompanied by inhibition of
COX-1 activity.
Publication Status: Online-Only
COMMENT PROVISIONAL REFSEQ: This record has not yet been subject to final
NCBI review. The reference sequence was derived from AF026008.1.
##Evidence-Data-START##
Transcript exon combination :: AF026008.1 [ECO:0000332]
RNAseq introns :: mixed/partial sample support
SAMEA1876818, SAMEA1876819
[ECO:0000350]
##Evidence-Data-END##
FEATURES Location/Qualifiers
source 1..606
/organism="Oryctolagus cuniculus"
/db_xref="taxon:9986"
Protein 1..606
/product="prostaglandin G/H synthase 1 precursor"
/EC_number="1.14.99.1"
/note="prostaglandin G/H synthase 1; PHS 1; PGHS-1; PGH
synthase 1; prostaglandin H2 synthase 1; cyclooxygenase-1;
prostaglandin-endoperoxide synthase 1 (prostaglandin G/H
synthase and cyclooxygenase)"
/calculated_mol_wt=65838
sig_peptide 1..30
/inference="COORDINATES: ab initio prediction:SignalP:4.0"
/calculated_mol_wt=3256
Region 39..76
/region_name="EGF_CA"
/note="Calcium-binding EGF-like domain, present in a large
number of membrane-bound and extracellular (mostly animal)
proteins. Many of these proteins require calcium for their
biological function and calcium-binding sites have been
found to be located at the...; cd00054"
/db_xref="CDD:238011"
Site 74
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (O97554.1)"
Region 96..582
/region_name="prostaglandin_endoperoxide_synthase"
/note="Animal prostaglandin endoperoxide synthase and
related bacterial proteins; cd09816"
/db_xref="CDD:188648"
Site 110
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (O97554.1)"
Site order(123,211,351,354..355,359,361,387,391,393,524,528,
532..533,536..537,540)
/site_type="other"
/note="substrate binding site [chemical binding]"
/db_xref="CDD:188648"
Site order(131,133..135,142..146,148,235,325..329,332..333,336,
339..340,343,373..380,543..544,547..551,553..555,557..558)
/site_type="other"
/note="homodimer interface [polypeptide binding]"
/db_xref="CDD:188648"
Site 150
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (O97554.1)"
Site order(154,205,209,213,216..218,301,388,391..394,397,414,
450,452..453,456)
/site_type="other"
/note="heme binding site [chemical binding]"
/db_xref="CDD:188648"
Site 416
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (O97554.1)"
Site 536
/site_type="other"
/note="Aspirin-acetylated serine. /evidence=ECO:0000250;
propagated from UniProtKB/Swiss-Prot (O97554.1)"
CDS 1..606
/gene="PTGS1"
/gene_synonym="COX-1"
/coded_by="NM_001082681.1:26..1846"
/db_xref="GeneID:100009407"
ORIGIN
1 msrsspslrl pvllllllll llpppppvlp adpgapapvn pccyfpcqhq gvcvrvaldr
61 yqcdctrtgy sgpnctvpdl wtwlrsslrp sptfvhyllt hvrwfwefvn atfirdtlmr
121 lvltvrsnli pspptynldy dyisweafsn vsyytrvlps vpkdcptpmg tkgkkqlpda
181 qvlahrfllr rtfipdpqgt nlmfaffaqh fthqffktsg kmgpgftkal ghgvdlghiy
241 gdslerqyhl rlfkdgklky qvldgevypp sveeapvlmh yprgvpprsq mavgqevfgl
301 lpglmlyatl wlrehnrvcd llkaehptwd deqlfqttrl iligetikiv ieeyvqqlsg
361 yflqlkfdpe mlfsvqfqyr nriamefnhl yhwhplmpds fqvgsqeysy eqflfntsml
421 vdygvealvd afsrqsagri gggrnidhhv lhvavevike sremrlqpfn eyrkrfglkp
481 yasfqeltge temaaeleel ygdidalefy pglllekcqp nsifgesmie igapfslkgl
541 lgnpicspey wkpstfggev gsnliktatl kklvclntkt cpyvsfrvpr ssgddgpaae
601 rrstel
//
