ID   PGH1_CANLF              Reviewed;         603 AA.
AC   Q8HZR1; F1PBX3; Q8HZR0;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   14-MAY-2014, sequence version 2.
DT   27-MAR-2024, entry version 146.
DE   RecName: Full=Prostaglandin G/H synthase 1;
DE            EC=1.14.99.1 {ECO:0000250|UniProtKB:P23219};
DE   AltName: Full=Cyclooxygenase-1;
DE            Short=COX-1;
DE   AltName: Full=Prostaglandin H2 synthase 1;
DE            Short=PGH synthase 1;
DE            Short=PGHS-1;
DE            Short=PHS 1;
DE   AltName: Full=Prostaglandin-endoperoxide synthase 1;
DE   Flags: Precursor;
GN   Name=PTGS1; Synonyms=COX1;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), ALTERNATIVE SPLICING,
RP   GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Brain cortex;
RX   PubMed=12242329; DOI=10.1073/pnas.162468699;
RA   Chandrasekharan N.V., Dai H., Roos K.L., Evanson N.K., Tomsik J.,
RA   Elton T.S., Simmons D.L.;
RT   "COX-3, a cyclooxygenase-1 variant inhibited by acetaminophen and other
RT   analgesic/antipyretic drugs: cloning, structure, and expression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13926-13931(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Boxer;
RX   PubMed=16341006; DOI=10.1038/nature04338;
RA   Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA   Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA   Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA   Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA   Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA   Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA   Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA   Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA   Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA   Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA   Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA   Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA   Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA   Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA   Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA   Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA   Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA   Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA   Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA   Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA   Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA   Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA   Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA   LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA   Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA   Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA   Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA   Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA   Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA   Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA   Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA   Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA   Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA   Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA   Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA   Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA   Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA   Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA   Zembek L., Zimmer A., Lander E.S.;
RT   "Genome sequence, comparative analysis and haplotype structure of the
RT   domestic dog.";
RL   Nature 438:803-819(2005).
CC   -!- FUNCTION: Dual cyclooxygenase and peroxidase that plays an important
CC       role in the biosynthesis pathway of prostanoids, a class of C20
CC       oxylipins mainly derived from arachidonate ((5Z,8Z,11Z,14Z)-
CC       eicosatetraenoate, AA, C20:4(n-6)), with a particular role in the
CC       inflammatory response. The cyclooxygenase activity oxygenates AA to the
CC       hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase
CC       activity reduces PGG2 to the hydroxy endoperoxide prostaglandin H2
CC       (PGH2), the precursor of all 2-series prostaglandins and thromboxanes.
CC       This complex transformation is initiated by abstraction of hydrogen at
CC       carbon 13 (with S-stereochemistry), followed by insertion of molecular
CC       O2 to form the endoperoxide bridge between carbon 9 and 11 that defines
CC       prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase
CC       activity) yields a hydroperoxy group in PGG2 that is then reduced to
CC       PGH2 by two electrons. Involved in the constitutive production of
CC       prostanoids in particular in the stomach and platelets. In gastric
CC       epithelial cells, it is a key step in the generation of prostaglandins,
CC       such as prostaglandin E2 (PGE2), which plays an important role in
CC       cytoprotection. In platelets, it is involved in the generation of
CC       thromboxane A2 (TXA2), which promotes platelet activation and
CC       aggregation, vasoconstriction and proliferation of vascular smooth
CC       muscle cells. Can also use linoleate (LA, (9Z,12Z)-octadecadienoate,
CC       C18:2(n-6)) as substrate and produce hydroxyoctadecadienoates (HODEs)
CC       in a regio- and stereospecific manner, being (9R)-HODE ((9R)-hydroxy-
CC       (10E,12Z)-octadecadienoate) and (13S)-HODE ((13S)-hydroxy-(9Z,11E)-
CC       octadecadienoate) its major products. {ECO:0000250|UniProtKB:P05979}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + 2 O2 = A + H2O +
CC         prostaglandin H2; Xref=Rhea:RHEA:23728, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:57405; EC=1.14.99.1;
CC         Evidence={ECO:0000250|UniProtKB:P23219};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23729;
CC         Evidence={ECO:0000250|UniProtKB:P23219};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + 2 O2 = prostaglandin G2;
CC         Xref=Rhea:RHEA:42596, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395,
CC         ChEBI:CHEBI:82629; Evidence={ECO:0000250|UniProtKB:P23219};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42597;
CC         Evidence={ECO:0000250|UniProtKB:P23219};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + prostaglandin G2 = A + H2O + prostaglandin H2;
CC         Xref=Rhea:RHEA:42600, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:57405, ChEBI:CHEBI:82629;
CC         Evidence={ECO:0000250|UniProtKB:P23219};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42601;
CC         Evidence={ECO:0000250|UniProtKB:P23219};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (9R)-hydroxy-(10E,12Z)-
CC         octadecadienoate + A + H2O; Xref=Rhea:RHEA:75447, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:30245, ChEBI:CHEBI:77895;
CC         Evidence={ECO:0000250|UniProtKB:P05979};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75448;
CC         Evidence={ECO:0000250|UniProtKB:P05979};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (9S)-hydroxy-(10E,12Z)-
CC         octadecadienoate + A + H2O; Xref=Rhea:RHEA:75459, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:30245, ChEBI:CHEBI:77852;
CC         Evidence={ECO:0000250|UniProtKB:P05979};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75460;
CC         Evidence={ECO:0000250|UniProtKB:P05979};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (13S)-hydroxy-(9Z,11E)-
CC         octadecadienoate + A + H2O; Xref=Rhea:RHEA:75451, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:30245, ChEBI:CHEBI:90850;
CC         Evidence={ECO:0000250|UniProtKB:P05979};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75452;
CC         Evidence={ECO:0000250|UniProtKB:P05979};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (13R)-hydroxy-(9Z,11E)-
CC         octadecadienoate + A + H2O; Xref=Rhea:RHEA:75455, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:30245, ChEBI:CHEBI:136655;
CC         Evidence={ECO:0000250|UniProtKB:P05979};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75456;
CC         Evidence={ECO:0000250|UniProtKB:P05979};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC       {ECO:0000250};
CC   -!- ACTIVITY REGULATION: The cyclooxygenase activity is inhibited by
CC       nonsteroidal anti-inflammatory drugs (NSAIDs) including ibuprofen,
CC       flurbiprofen, ketoprofen, naproxen, flurbiprofen, anirolac, fenclofenac
CC       and diclofenac. {ECO:0000250|UniProtKB:P23219}.
CC   -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC       {ECO:0000250|UniProtKB:P23219}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000269|PubMed:12242329}. Endoplasmic reticulum
CC       membrane {ECO:0000269|PubMed:12242329}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:12242329}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=1; Synonyms=COX-1;
CC         IsoId=Q8HZR1-1; Sequence=Displayed;
CC       Name=2; Synonyms=COX-3;
CC         IsoId=Q8HZR1-2; Sequence=VSP_054856;
CC       Name=3; Synonyms=PCOX-1a;
CC         IsoId=Q8HZR1-3; Sequence=VSP_054856, VSP_054857;
CC       Name=4; Synonyms=PCOX-1b;
CC         IsoId=Q8HZR1-4; Sequence=VSP_054857;
CC   -!- TISSUE SPECIFICITY: Brain cortex. Isoform 2 is expressed in the
CC       cerebral cortex and heart.
CC   -!- PTM: N-glycosylated. N-linked glycosylation is necessary for enzymatic
CC       activity. {ECO:0000269|PubMed:12242329}.
CC   -!- MISCELLANEOUS: The conversion of arachidonate to prostaglandin H2 is a
CC       2 step reaction: a cyclooxygenase (COX) reaction which converts
CC       arachidonate to prostaglandin G2 (PGG2) and a peroxidase reaction in
CC       which PGG2 is reduced to prostaglandin H2 (PGH2). The cyclooxygenase
CC       reaction occurs in a hydrophobic channel in the core of the enzyme. The
CC       peroxidase reaction occurs at a heme-containing active site located
CC       near the protein surface. The nonsteroidal anti-inflammatory drugs
CC       (NSAIDs) binding site corresponds to the cyclooxygenase active site.
CC   -!- MISCELLANEOUS: Conversion of arachidonate to prostaglandin H2 is
CC       mediated by 2 different isozymes: the constitutive PTGS1 and the
CC       inducible PTGS2. PTGS1 is expressed constitutively and generally
CC       produces prostanoids acutely in response to hormonal stimuli to fine-
CC       tune physiological processes requiring instantaneous, continuous
CC       regulation (e.g. hemostasis). PTGS2 is inducible and typically produces
CC       prostanoids that mediate responses to physiological stresses such as
CC       infection and inflammation.
CC   -!- MISCELLANEOUS: PTGS1 and PTGS2 are the targets of nonsteroidal anti-
CC       inflammatory drugs (NSAIDs) including aspirin and ibuprofen. Aspirin is
CC       able to produce an irreversible inactivation of the enzyme through a
CC       serine acetylation. Inhibition of the PGHSs with NSAIDs acutely reduces
CC       inflammation, pain, and fever, and long-term use of these drugs reduces
CC       fatal thrombotic events, as well as the development of colon cancer and
CC       Alzheimer's disease. PTGS2 is the principal isozyme responsible for
CC       production of inflammatory prostaglandins. New generation PTGSs
CC       inhibitors strive to be selective for PTGS2, to avoid side effects such
CC       as gastrointestinal complications and ulceration.
CC   -!- MISCELLANEOUS: [Isoform 3]: No enzymatic activity. Membrane-bound.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the prostaglandin G/H synthase family.
CC       {ECO:0000305}.
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DR   EMBL; AF535138; AAN33049.1; -; mRNA.
DR   EMBL; AF535139; AAN38739.1; -; mRNA.
DR   EMBL; AAEX03006907; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001003023.1; NM_001003023.2.
DR   AlphaFoldDB; Q8HZR1; -.
DR   SMR; Q8HZR1; -.
DR   STRING; 9615.ENSCAFP00000044458; -.
DR   BindingDB; Q8HZR1; -.
DR   ChEMBL; CHEMBL4133; -.
DR   DrugCentral; Q8HZR1; -.
DR   PeroxiBase; 3362; CfaPGHS01.
DR   GlyCosmos; Q8HZR1; 3 sites, No reported glycans.
DR   SwissPalm; Q8HZR1; -.
DR   PaxDb; 9612-ENSCAFP00000030067; -.
DR   Ensembl; ENSCAFT00000032279.4; ENSCAFP00000030061.2; ENSCAFG00000020263.6. [Q8HZR1-3]
DR   Ensembl; ENSCAFT00000032287.6; ENSCAFP00000030067.3; ENSCAFG00000020263.6. [Q8HZR1-1]
DR   Ensembl; ENSCAFT00000062685.2; ENSCAFP00000052626.1; ENSCAFG00000020263.6. [Q8HZR1-2]
DR   Ensembl; ENSCAFT00040004500.1; ENSCAFP00040003864.1; ENSCAFG00040002347.1. [Q8HZR1-2]
DR   Ensembl; ENSCAFT00040004521.1; ENSCAFP00040003882.1; ENSCAFG00040002347.1. [Q8HZR1-1]
DR   Ensembl; ENSCAFT00040004622.1; ENSCAFP00040003972.1; ENSCAFG00040002347.1. [Q8HZR1-3]
DR   Ensembl; ENSCAFT00845024089.1; ENSCAFP00845018920.1; ENSCAFG00845013501.1. [Q8HZR1-1]
DR   GeneID; 403544; -.
DR   KEGG; cfa:403544; -.
DR   CTD; 5742; -.
DR   VEuPathDB; HostDB:ENSCAFG00845013501; -.
DR   eggNOG; KOG2408; Eukaryota.
DR   GeneTree; ENSGT00390000010743; -.
DR   HOGENOM; CLU_022428_0_0_1; -.
DR   InParanoid; Q8HZR1; -.
DR   OMA; LFGSQFQ; -.
DR   OrthoDB; 1086441at2759; -.
DR   TreeFam; TF329675; -.
DR   Reactome; R-CFA-140180; COX reactions.
DR   Reactome; R-CFA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR   UniPathway; UPA00662; -.
DR   Proteomes; UP000002254; Chromosome 9.
DR   Proteomes; UP000694429; Unplaced.
DR   Proteomes; UP000694542; Chromosome 9.
DR   Proteomes; UP000805418; Chromosome 9.
DR   Bgee; ENSCAFG00000020263; Expressed in spinal cord and 49 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IBA:GO_Central.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004666; F:prostaglandin-endoperoxide synthase activity; IBA:GO_Central.
DR   GO; GO:0019371; P:cyclooxygenase pathway; IBA:GO_Central.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd09816; prostaglandin_endoperoxide_synthase; 1.
DR   Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR   Gene3D; 2.10.25.10; Laminin; 1.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR010255; Haem_peroxidase_sf.
DR   InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR   PANTHER; PTHR11903; PROSTAGLANDIN G/H SYNTHASE; 1.
DR   PANTHER; PTHR11903:SF6; PROSTAGLANDIN G_H SYNTHASE 1; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Dioxygenase; Disulfide bond; EGF-like domain;
KW   Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Glycoprotein; Heme; Iron; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Metal-binding; Microsome; Oxidoreductase; Peroxidase;
KW   Prostaglandin biosynthesis; Prostaglandin metabolism; Reference proteome;
KW   Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..603
FT                   /note="Prostaglandin G/H synthase 1"
FT                   /id="PRO_0000429170"
FT   DOMAIN          35..73
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   ACT_SITE        210
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   ACT_SITE        388
FT                   /note="For cyclooxygenase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         391
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00298"
FT   SITE            533
FT                   /note="Aspirin-acetylated serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        71
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        107
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        147
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        39..50
FT                   /evidence="ECO:0000250"
FT   DISULFID        40..162
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..60
FT                   /evidence="ECO:0000250"
FT   DISULFID        62..72
FT                   /evidence="ECO:0000250"
FT   DISULFID        572..578
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         3
FT                   /note="R -> REFDPEAPRNPLRLPGEPRMPGPALTSRSAG (in isoform 2
FT                   and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:12242329"
FT                   /id="VSP_054856"
FT   VAR_SEQ         122..340
FT                   /note="Missing (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:12242329"
FT                   /id="VSP_054857"
FT   CONFLICT        597
FT                   /note="E -> Q (in Ref. 1; AAN33049/AAN38739)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   603 AA;  69305 MW;  435B3E3A3D5DCCA6 CRC64;
     MSRGSRLHRW PLLLLLLLLL PPPPVLPAEA RTPAPVNPCC YYPCQHQGIC VRFGLDRYQC
     DCTRTGYSGP NCTIPELWTW LRNSLRPSPS FLHFLLTHGR WFWEFINATF IRDMLMRLVL
     TARSNLIPSP PTYNIAHDYI SWESFSNVSY YTRVLPSVPQ DCPTPMGTKG KKQLPDAQLL
     GRRFLLRRKF IPDPQGTNLM FAFFAQHFTH QFFKTSGKMG PGFTKALGHG VDLGHIYGDN
     LDRQYQLRLF KDGKLKYQVL DGEMYPPSVE EAPVLMHYPR GILPQSQMAV GQEVFGLLPG
     LMLYATLWLR EHNRVCDLLK AEHPTWGDEQ LFQTARLILI GETIKIVIEE YVQQLSGYFL
     QLKFDPELLF SAQFQYRNRI AMEFNQLYHW HPLMPDSFWV GSQEYSYEQF LFNTSMLTHY
     GIEALVDAFS RQSAGRIGGG RNIDHHVLHV AVETIKESRE LRLQPFNEYR KRFGMRPYMS
     FQELTGEKEM AAELEELYGD IDALEFYPGL LLEKCHPNSI FGESMIEIGA PFSLKGLLGN
     PICSPEYWKP STFGGEMGFN MVKTATLKKL VCLNTKTCPY VSFRVPDPHQ DGGPGVERPS
     TEL
//