GenomeNet

Database: RefSeq
Entry: NP_001076150
LinkDB: NP_001076150
Original site: NP_001076150 
LOCUS       NP_001076150             606 aa            linear   MAM 02-DEC-2024
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              :: single sample supports all introns
                                           SAMEA5760392, SAMEA5760441
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..606
                     /organism="Oryctolagus cuniculus"
                     /db_xref="taxon:9986"
                     /chromosome="1"
                     /map="1"
     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:6.0"
                     /calculated_mol_wt=3256
     mat_peptide     31..606
                     /product="Prostaglandin G/H synthase 1.
                     /id=PRO_0000041818"
                     /note="propagated from UniProtKB/Swiss-Prot (O97554.1)"
                     /calculated_mol_wt=65838
     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
//
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