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Database: UniProt/SWISS-PROT
Entry: PGH2_MOUSE
LinkDB: PGH2_MOUSE
Original site: PGH2_MOUSE 
ID   PGH2_MOUSE              Reviewed;         604 AA.
AC   Q05769; Q543K3;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   05-DEC-2018, entry version 196.
DE   RecName: Full=Prostaglandin G/H synthase 2;
DE            EC=1.14.99.1;
DE   AltName: Full=Cyclooxygenase-2;
DE            Short=COX-2;
DE   AltName: Full=Glucocorticoid-regulated inflammatory cyclooxygenase;
DE   AltName: Full=Gripghs;
DE   AltName: Full=Macrophage activation-associated marker protein P71/73;
DE   AltName: Full=PES-2;
DE   AltName: Full=PHS II;
DE   AltName: Full=Prostaglandin H2 synthase 2;
DE            Short=PGH synthase 2;
DE            Short=PGHS-2;
DE   AltName: Full=Prostaglandin-endoperoxide synthase 2;
DE   AltName: Full=TIS10 protein;
DE   Flags: Precursor;
GN   Name=Ptgs2; Synonyms=Cox-2, Cox2, Pghs-b, Tis10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=SWR/J;
RX   PubMed=1712772;
RA   Kujubu D.A., Fletcher B.S., Varnum B.C., Lim R.W., Herschman H.R.;
RT   "TIS10, a phorbol ester tumor promoter-inducible mRNA from Swiss 3T3
RT   cells, encodes a novel prostaglandin synthase/cyclooxygenase
RT   homologue.";
RL   J. Biol. Chem. 266:12866-12872(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1339449;
RA   Fletcher B.S., Kujubu D.A., Perrin D.M., Herschman H.R.;
RT   "Structure of the mitogen-inducible TIS10 gene and demonstration that
RT   the TIS10-encoded protein is a functional prostaglandin G/H
RT   synthase.";
RL   J. Biol. Chem. 267:4338-4344(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1419907;
RA   Ryseck R.-P., Raynoschek C., Macdonald-Bravo H., Dorfman K.,
RA   Mattei M.-G., Bravo R.;
RT   "Identification of an immediate early gene, pghs-B, whose protein
RT   product has prostaglandin synthase/cyclooxygenase activity.";
RL   Cell Growth Differ. 3:443-450(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1594589; DOI=10.1073/pnas.89.11.4888;
RA   O'Banion M.K., Winn V.D., Young D.A.;
RT   "cDNA cloning and functional activity of a glucocorticoid-regulated
RT   inflammatory cyclooxygenase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:4888-4892(1992).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Hippocampus, Mammary gland, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 281-360.
RX   PubMed=1744122;
RA   O'Banion M.K., Sadowski H.B., Winn V., Young D.A.;
RT   "A serum- and glucocorticoid-regulated 4-kilobase mRNA encodes a
RT   cyclooxygenase-related protein.";
RL   J. Biol. Chem. 266:23261-23267(1991).
RN   [8]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=8482922;
RA   Phillips T.A., Kujubu D.A., Mackay R.J., Herschman H.R., Russell S.W.,
RA   Pace J.L.;
RT   "The mouse macrophage activation-associated marker protein, p71/73, is
RT   an inducible prostaglandin endoperoxide synthase (cyclooxygenase).";
RL   J. Leukoc. Biol. 53:411-419(1993).
RN   [9]
RP   GLYCOSYLATION AT ASN-53; ASN-130; ASN-396 AND ASN-580, AND LACK OF
RP   GLYCOSYLATION AT ASN-592.
RX   PubMed=8349699;
RA   Otto J.C., Dewitt D.L., Smith W.L.;
RT   "N-glycosylation of prostaglandin endoperoxide synthases-1 and -2 and
RT   their orientations in the endoplasmic reticulum.";
RL   J. Biol. Chem. 268:18234-18242(1993).
RN   [10]
RP   FUNCTION IN INTESTINAL WOUND REPAIR, TISSUE SPECIFICITY, DEVELOPMENTAL
RP   STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=22465430; DOI=10.1053/j.gastro.2012.03.037;
RA   Manieri N.A., Drylewicz M.R., Miyoshi H., Stappenbeck T.S.;
RT   "Igf2bp1 is required for full induction of Ptgs2 mRNA in colonic
RT   mesenchymal stem cells in mice.";
RL   Gastroenterology 143:110-121(2012).
RN   [11]
RP   REVIEW ON FUNCTION; TISSUE SPECIFICITY AND INHIBITION BY NSAIDS.
RX   PubMed=10966456; DOI=10.1146/annurev.biochem.69.1.145;
RA   Smith W.L., DeWitt D.L., Garavito R.M.;
RT   "Cyclooxygenases: structural, cellular, and molecular biology.";
RL   Annu. Rev. Biochem. 69:145-182(2000).
RN   [12]
RP   REVIEW ON FUNCTION; INHIBITION BY ASPIRIN AND INVOLVEMENT IN
RP   COLORECTAL CANCER.
RX   PubMed=24605250; DOI=10.4292/wjgpt.v5.i1.40;
RA   Sostres C., Gargallo C.J., Lanas A.;
RT   "Aspirin, cyclooxygenase inhibition and colorectal cancer.";
RL   World J. Gastrointest. Pharmacol. Ther. 5:40-49(2014).
RN   [13] {ECO:0000244|PDB:1CX2, ECO:0000244|PDB:3PGH, ECO:0000244|PDB:4COX, ECO:0000244|PDB:5COX, ECO:0000244|PDB:6COX}
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH
RP   (S)-FLURBIPROFEN; INDOMETHACIN; HEME AND
RP   1-PHENYLSULFONAMIDE-3-TRIFLUOROMETHYL-5-PARABROMOPHENYLPYRAZOLE,
RP   COFACTOR, GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396, AND DISULFIDE
RP   BONDS.
RX   PubMed=8967954; DOI=10.1038/384644a0;
RA   Kurumbail R.G., Stevens A.M., Gierse J.K., McDonald J.J.,
RA   Stegeman R.A., Pay J.Y., Gildehaus D., Miyashiro J.M., Penning T.D.,
RA   Seibert K., Isakson P.C., Stallings W.C.;
RT   "Structural basis for selective inhibition of cyclooxygenase-2 by
RT   anti-inflammatory agents.";
RL   Nature 384:644-648(1996).
RN   [14]
RP   ERRATUM.
RA   Kurumbail R.G., Stevens A.M., Gierse J.K., McDonald J.J.,
RA   Stegeman R.A., Pay J.Y., Gildehaus D., Miyashiro J.M., Penning T.D.,
RA   Seibert K., Isakson P.C., Stallings W.C.;
RL   Nature 385:555-555(1997).
RN   [15] {ECO:0000244|PDB:1CVU, ECO:0000244|PDB:1DDX}
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 18-569 IN COMPLEX WITH
RP   ARACHIDONIC ACID, GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396, AND
RP   DISULFIDE BONDS.
RX   PubMed=10811226; DOI=10.1038/35011103;
RA   Kiefer J.R., Pawlitz J.L., Moreland K.T., Stegeman R.A., Hood W.F.,
RA   Gierse J.K., Stevens A.M., Goodwin D.C., Rowlinson S.W., Marnett L.J.,
RA   Stallings W.C., Kurumbail R.G.;
RT   "Structural insights into the stereochemistry of the cyclooxygenase
RT   reaction.";
RL   Nature 405:97-101(2000).
RN   [16] {ECO:0000244|PDB:1PXX}
RP   X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH HEME AND
RP   DICLOFENAC, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, DISULFIDE BONDS,
RP   ACTIVITY REGULATION, AND GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396.
RX   PubMed=12925531; DOI=10.1074/jbc.M305481200;
RA   Rowlinson S.W., Kiefer J.R., Prusakiewicz J.J., Pawlitz J.L.,
RA   Kozak K.R., Kalgutkar A.S., Stallings W.C., Kurumbail R.G.,
RA   Marnett L.J.;
RT   "A novel mechanism of cyclooxygenase-2 inhibition involving
RT   interactions with Ser-530 and Tyr-385.";
RL   J. Biol. Chem. 278:45763-45769(2003).
RN   [17] {ECO:0000244|PDB:3HS5, ECO:0000244|PDB:3HS6, ECO:0000244|PDB:3HS7, ECO:0000244|PDB:3KRK}
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 20-604 IN COMPLEX WITH HEME;
RP   ACRYLIC ACID; ARACHIDONIC ACID AND DOCOSAHEXAENOIC ACID, CATALYTIC
RP   ACTIVITY, ACTIVE SITE, SUBUNIT, COFACTOR, FUNCTION, DISULFIDE BONDS,
RP   MUTAGENESIS OF LEU-517 AND ASN-580, AND GLYCOSYLATION AT ASN-53;
RP   ASN-130; ASN-396 AND ASN-580.
RX   PubMed=20463020; DOI=10.1074/jbc.M110.119867;
RA   Vecchio A.J., Simmons D.M., Malkowski M.G.;
RT   "Structural basis of fatty acid substrate binding to cyclooxygenase-
RT   2.";
RL   J. Biol. Chem. 285:22152-22163(2010).
RN   [18] {ECO:0000244|PDB:3NT1, ECO:0000244|PDB:3NTB}
RP   X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 18-604 IN COMPLEXES WITH
RP   HEME AND NAPROXEN ANALOGS, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-53; ASN-130 AND
RP   ASN-396.
RX   PubMed=20810665; DOI=10.1074/jbc.M110.162982;
RA   Duggan K.C., Walters M.J., Musee J., Harp J.M., Kiefer J.R.,
RA   Oates J.A., Marnett L.J.;
RT   "Molecular basis for cyclooxygenase inhibition by the non-steroidal
RT   anti-inflammatory drug naproxen.";
RL   J. Biol. Chem. 285:34950-34959(2010).
RN   [19] {ECO:0000244|PDB:3QH0}
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), GLYCOSYLATION AT ASN-53;
RP   ASN-130 AND ASN-396, AND DISULFIDE BONDS.
RX   PubMed=21467029; DOI=10.1074/jbc.M111.231969;
RA   Dong L., Vecchio A.J., Sharma N.P., Jurban B.J., Malkowski M.G.,
RA   Smith W.L.;
RT   "Human cyclooxygenase-2 is a sequence homodimer that functions as a
RT   conformational heterodimer.";
RL   J. Biol. Chem. 286:19035-19046(2011).
RN   [20] {ECO:0000244|PDB:3MDL, ECO:0000244|PDB:3OLT, ECO:0000244|PDB:3OLU}
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 20-599 IN COMPLEX WITH HEME;
RP   ACRYLIC ACID AND ARACHIDONIC ACID, FUNCTION, CATALYTIC ACTIVITY,
RP   GLYCOSYLATION AT ASN-53; ASN-130 AND ASN-396, AND DISULFIDE BONDS.
RX   PubMed=21489986; DOI=10.1074/jbc.M111.230367;
RA   Vecchio A.J., Malkowski M.G.;
RT   "The structural basis of endocannabinoid oxygenation by
RT   cyclooxygenase-2.";
RL   J. Biol. Chem. 286:20736-20745(2011).
CC   -!- FUNCTION: Converts arachidonate to prostaglandin H2 (PGH2), a
CC       committed step in prostanoid synthesis. Constitutively expressed
CC       in some tissues in physiological conditions, such as the
CC       endothelium, kidney and brain, and in pathological conditions,
CC       such as in cancer. PTGS2 is responsible for production of
CC       inflammatory prostaglandins. Up-regulation of PTGS2 is also
CC       associated with increased cell adhesion, phenotypic changes,
CC       resistance to apoptosis and tumor angiogenesis. In cancer cells,
CC       PTGS2 is a key step in the production of prostaglandin E2 (PGE2),
CC       which plays important roles in modulating motility, proliferation
CC       and resistance to apoptosis. {ECO:0000269|PubMed:12925531,
CC       ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665,
CC       ECO:0000269|PubMed:21489986, ECO:0000269|PubMed:22465430}.
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:0000269|PubMed:12925531,
CC         ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:20810665,
CC         ECO:0000269|PubMed:21489986};
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000269|PubMed:12925531,
CC         ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:8967954};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
CC       subunit. {ECO:0000269|PubMed:12925531,
CC       ECO:0000269|PubMed:20463020, ECO:0000269|PubMed:8967954};
CC   -!- ACTIVITY REGULATION: Inhibited by the nonsteroidal anti-
CC       inflammatory drugs aspirin, naproxen, diclofenac, meclofenamic
CC       acid, indomethacin and their analogs.
CC       {ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20810665}.
CC   -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC       {ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020,
CC       ECO:0000269|PubMed:20810665, ECO:0000269|PubMed:21489986}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10811226,
CC       ECO:0000269|PubMed:12925531, ECO:0000269|PubMed:20463020,
CC       ECO:0000269|PubMed:21467029, ECO:0000269|PubMed:21489986,
CC       ECO:0000269|PubMed:8967954}.
CC   -!- INTERACTION:
CC       Q9Z0J4:Nos1; NbExp=4; IntAct=EBI-298933, EBI-397596;
CC   -!- SUBCELLULAR LOCATION: Microsome membrane; Peripheral membrane
CC       protein. Endoplasmic reticulum membrane; Peripheral membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Following colon injury, expressed in the wound
CC       bed mesenchyme during the first phase of repair, probably by
CC       colonic mesenchymal stem cells (at protein level).
CC       {ECO:0000269|PubMed:22465430}.
CC   -!- DEVELOPMENTAL STAGE: During colonic wound repair, highly up-
CC       regulated (more than 1600-fold) in the mesenchyme of the wound bed
CC       2 days after injury as compared to uninjured mucosa. Further
CC       increase in expression is observed at day 4 following injury
CC       (close to 2200-fold). Down-regulated at day 6 (only 93-fold
CC       increase as compared to uninjured mucosa).
CC       {ECO:0000269|PubMed:22465430}.
CC   -!- INDUCTION: By cytokines and mitogens.
CC   -!- PTM: S-nitrosylation by NOS2 (iNOS) activates enzyme activity. S-
CC       nitrosylation may take place on different Cys residues in addition
CC       to Cys-526 (By similarity). {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mutant mice exhibit defects in colonic
CC       mucosal wound repair. {ECO:0000269|PubMed:22465430}.
CC   -!- MISCELLANEOUS: The conversion of arachidonate to prostaglandin H2
CC       is a 2 step reaction: a cyclooxygenase (COX) reaction which
CC       converts arachidonate to prostaglandin G2 (PGG2) and a peroxidase
CC       reaction in which PGG2 is reduced to prostaglandin H2 (PGH2). The
CC       cyclooxygenase reaction occurs in a hydrophobic channel in the
CC       core of the enzyme. The peroxidase reaction occurs at a heme-
CC       containing active site located near the protein surface. The
CC       nonsteroidal anti-inflammatory drugs (NSAIDs) binding site
CC       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. PGHS1 is expressed constitutively and generally
CC       produces prostanoids acutely in response to hormonal stimuli to
CC       fine-tune physiological processes requiring instantaneous,
CC       continuous regulation (e.g. hemostasis). PGHS2 is inducible and
CC       typically produces prostanoids that mediate responses to
CC       physiological stresses such as infection and inflammation.
CC   -!- MISCELLANEOUS: PTGS1 and PTGS2 are the targets of nonsteroidal
CC       anti-inflammatory drugs (NSAIDs) including aspirin and ibuprofen.
CC       Aspirin is able to produce an irreversible inactivation of the
CC       enzyme through a serine acetylation. Inhibition of the PGHSs with
CC       NSAIDs acutely reduces inflammation, pain, and fever, and long-
CC       term use of these drugs reduces fatal thrombotic events, as well
CC       as the development of colon cancer and Alzheimer's disease. PTGS2
CC       is the principal isozyme responsible for production of
CC       inflammatory prostaglandins. New generation PTGSs inhibitors
CC       strive to be selective for PTGS2, to avoid side effects such as
CC       gastrointestinal complications and ulceration.
CC   -!- SIMILARITY: Belongs to the prostaglandin G/H synthase family.
CC       {ECO:0000305}.
DR   EMBL; M64291; AAA39924.1; -; mRNA.
DR   EMBL; M94967; AAA39918.1; -; mRNA.
DR   EMBL; M82866; AAA40448.1; -; Genomic_DNA.
DR   EMBL; M82862; AAA40448.1; JOINED; Genomic_DNA.
DR   EMBL; M82863; AAA40448.1; JOINED; Genomic_DNA.
DR   EMBL; M82864; AAA40448.1; JOINED; Genomic_DNA.
DR   EMBL; M82865; AAA40448.1; JOINED; Genomic_DNA.
DR   EMBL; M88242; AAA37740.1; -; mRNA.
DR   EMBL; AK049923; BAC33986.1; -; mRNA.
DR   EMBL; AK144956; BAE26154.1; -; mRNA.
DR   EMBL; AK166221; BAE38639.1; -; mRNA.
DR   EMBL; AK172161; BAE42855.1; -; mRNA.
DR   EMBL; CH466520; EDL39487.1; -; Genomic_DNA.
DR   CCDS; CCDS15353.1; -.
DR   PIR; A49010; A49010.
DR   RefSeq; NP_035328.2; NM_011198.4.
DR   UniGene; Mm.292547; -.
DR   PDB; 1CVU; X-ray; 2.40 A; A/B=18-569.
DR   PDB; 1CX2; X-ray; 3.00 A; A/B/C/D=18-604.
DR   PDB; 1DCX; Model; -; A/B=18-569.
DR   PDB; 1DD0; Model; -; A/B=18-569.
DR   PDB; 1DDX; X-ray; 3.00 A; A/B/C/D=18-569.
DR   PDB; 1PXX; X-ray; 2.90 A; A/B/C/D=1-604.
DR   PDB; 3HS5; X-ray; 2.10 A; A/B=20-604.
DR   PDB; 3HS6; X-ray; 2.40 A; A/B=20-604.
DR   PDB; 3HS7; X-ray; 2.65 A; A/B=20-604.
DR   PDB; 3KRK; X-ray; 2.40 A; A/B=20-604.
DR   PDB; 3LN0; X-ray; 2.20 A; A/B/C/D=18-604.
DR   PDB; 3LN1; X-ray; 2.40 A; A/B/C/D=18-604.
DR   PDB; 3MDL; X-ray; 2.20 A; A/B=20-599.
DR   PDB; 3MQE; X-ray; 2.80 A; A/B/C/D=18-604.
DR   PDB; 3NT1; X-ray; 1.73 A; A/B=18-604.
DR   PDB; 3NTB; X-ray; 2.27 A; A/B/C/D=18-604.
DR   PDB; 3NTG; X-ray; 2.19 A; A/B/C/D=18-569.
DR   PDB; 3OLT; X-ray; 2.45 A; A/B=20-604.
DR   PDB; 3OLU; X-ray; 2.35 A; A/B=20-604.
DR   PDB; 3PGH; X-ray; 2.50 A; A/B/C/D=18-604.
DR   PDB; 3Q7D; X-ray; 2.40 A; A/B=18-604.
DR   PDB; 3QH0; X-ray; 2.10 A; A/B=1-604.
DR   PDB; 3QMO; X-ray; 3.00 A; A/B=1-604.
DR   PDB; 3RR3; X-ray; 2.84 A; A/B/C/D=18-577.
DR   PDB; 3TZI; X-ray; 2.15 A; A/B=20-604.
DR   PDB; 4COX; X-ray; 2.90 A; A/B/C/D=18-604.
DR   PDB; 4E1G; X-ray; 2.10 A; A/B=1-604.
DR   PDB; 4FM5; X-ray; 2.81 A; A/B/C/D=1-604.
DR   PDB; 4M10; X-ray; 2.01 A; A/B/C/D=18-604.
DR   PDB; 4M11; X-ray; 2.45 A; A/B/C/D=18-569.
DR   PDB; 4OTJ; X-ray; 2.11 A; A/B/C/D=18-604.
DR   PDB; 4OTY; X-ray; 2.35 A; A/B=18-604.
DR   PDB; 4PH9; X-ray; 1.81 A; A/B=20-568.
DR   PDB; 4RRW; X-ray; 2.57 A; A/B/C/D=18-604.
DR   PDB; 4RRX; X-ray; 2.78 A; A/B=18-604.
DR   PDB; 4RRY; X-ray; 2.43 A; A/B/C/D=18-604.
DR   PDB; 4RRZ; X-ray; 2.57 A; A/B/C/D=18-604.
DR   PDB; 4RS0; X-ray; 2.81 A; A=18-604.
DR   PDB; 4RUT; X-ray; 2.16 A; A/B/C/D=18-604.
DR   PDB; 4Z0L; X-ray; 2.29 A; A/B/C/D=18-604.
DR   PDB; 5COX; X-ray; 3.00 A; A/B/C/D=18-604.
DR   PDB; 5FDQ; X-ray; 1.90 A; A/B=20-604.
DR   PDB; 5JVY; X-ray; 2.36 A; A/B=20-568.
DR   PDB; 5JVZ; X-ray; 2.62 A; A/B=20-569.
DR   PDB; 5JW1; X-ray; 2.82 A; A/B=20-569.
DR   PDB; 5W58; X-ray; 2.27 A; A=18-604.
DR   PDB; 6COX; X-ray; 2.80 A; A/B=18-604.
DR   PDBsum; 1CVU; -.
DR   PDBsum; 1CX2; -.
DR   PDBsum; 1DCX; -.
DR   PDBsum; 1DD0; -.
DR   PDBsum; 1DDX; -.
DR   PDBsum; 1PXX; -.
DR   PDBsum; 3HS5; -.
DR   PDBsum; 3HS6; -.
DR   PDBsum; 3HS7; -.
DR   PDBsum; 3KRK; -.
DR   PDBsum; 3LN0; -.
DR   PDBsum; 3LN1; -.
DR   PDBsum; 3MDL; -.
DR   PDBsum; 3MQE; -.
DR   PDBsum; 3NT1; -.
DR   PDBsum; 3NTB; -.
DR   PDBsum; 3NTG; -.
DR   PDBsum; 3OLT; -.
DR   PDBsum; 3OLU; -.
DR   PDBsum; 3PGH; -.
DR   PDBsum; 3Q7D; -.
DR   PDBsum; 3QH0; -.
DR   PDBsum; 3QMO; -.
DR   PDBsum; 3RR3; -.
DR   PDBsum; 3TZI; -.
DR   PDBsum; 4COX; -.
DR   PDBsum; 4E1G; -.
DR   PDBsum; 4FM5; -.
DR   PDBsum; 4M10; -.
DR   PDBsum; 4M11; -.
DR   PDBsum; 4OTJ; -.
DR   PDBsum; 4OTY; -.
DR   PDBsum; 4PH9; -.
DR   PDBsum; 4RRW; -.
DR   PDBsum; 4RRX; -.
DR   PDBsum; 4RRY; -.
DR   PDBsum; 4RRZ; -.
DR   PDBsum; 4RS0; -.
DR   PDBsum; 4RUT; -.
DR   PDBsum; 4Z0L; -.
DR   PDBsum; 5COX; -.
DR   PDBsum; 5FDQ; -.
DR   PDBsum; 5JVY; -.
DR   PDBsum; 5JVZ; -.
DR   PDBsum; 5JW1; -.
DR   PDBsum; 5W58; -.
DR   PDBsum; 6COX; -.
DR   ProteinModelPortal; Q05769; -.
DR   SMR; Q05769; -.
DR   BioGrid; 202463; 6.
DR   DIP; DIP-31082N; -.
DR   IntAct; Q05769; 2.
DR   STRING; 10090.ENSMUSP00000035065; -.
DR   BindingDB; Q05769; -.
DR   ChEMBL; CHEMBL4321; -.
DR   SwissLipids; SLP:000001129; -.
DR   PeroxiBase; 3360; MmPGHS02.
DR   GlyConnect; 514; -.
DR   iPTMnet; Q05769; -.
DR   PhosphoSitePlus; Q05769; -.
DR   SwissPalm; Q05769; -.
DR   UniCarbKB; Q05769; -.
DR   PaxDb; Q05769; -.
DR   PeptideAtlas; Q05769; -.
DR   PRIDE; Q05769; -.
DR   Ensembl; ENSMUST00000035065; ENSMUSP00000035065; ENSMUSG00000032487.
DR   GeneID; 19225; -.
DR   KEGG; mmu:19225; -.
DR   UCSC; uc007cxv.1; mouse.
DR   CTD; 5743; -.
DR   MGI; MGI:97798; Ptgs2.
DR   eggNOG; KOG2408; Eukaryota.
DR   eggNOG; ENOG410XPZ3; LUCA.
DR   GeneTree; ENSGT00390000010743; -.
DR   HOGENOM; HOG000013149; -.
DR   HOVERGEN; HBG000366; -.
DR   InParanoid; Q05769; -.
DR   KO; K11987; -.
DR   OMA; KGCPFTA; -.
DR   OrthoDB; EOG091G03CD; -.
DR   PhylomeDB; Q05769; -.
DR   TreeFam; TF329675; -.
DR   BRENDA; 1.14.99.1; 3474.
DR   Reactome; R-MMU-197264; Nicotinamide salvaging.
DR   Reactome; R-MMU-2142770; Synthesis of 15-eicosatetraenoic acid derivatives.
DR   Reactome; R-MMU-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR   Reactome; R-MMU-9018677; Biosynthesis of DHA-derived SPMs.
DR   Reactome; R-MMU-9018679; Biosynthesis of EPA-derived SPMs.
DR   Reactome; R-MMU-9025094; Biosynthesis of DPAn-3 SPMs.
DR   Reactome; R-MMU-9027604; Biosynthesis of electrophilic Omega-3 PUFA oxo-derivatives.
DR   UniPathway; UPA00662; -.
DR   EvolutionaryTrace; Q05769; -.
DR   PRO; PR:Q05769; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   Bgee; ENSMUSG00000032487; Expressed in 136 organ(s), highest expression level in cumulus cell.
DR   CleanEx; MM_PTGS2; -.
DR   ExpressionAtlas; Q05769; baseline and differential.
DR   Genevisible; Q05769; MM.
DR   GO; GO:0005901; C:caveola; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043005; C:neuron projection; IDA:MGI.
DR   GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0020037; F:heme binding; IDA:UniProtKB.
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; ISO:MGI.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004666; F:prostaglandin-endoperoxide synthase activity; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR   GO; GO:0007568; P:aging; IEA:Ensembl.
DR   GO; GO:0001525; P:angiogenesis; ISO:MGI.
DR   GO; GO:0030282; P:bone mineralization; ISO:MGI.
DR   GO; GO:0050873; P:brown fat cell differentiation; IMP:BHF-UCL.
DR   GO; GO:0071318; P:cellular response to ATP; IEA:Ensembl.
DR   GO; GO:0071498; P:cellular response to fluid shear stress; IDA:MGI.
DR   GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
DR   GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR   GO; GO:0071284; P:cellular response to lead ion; IEA:Ensembl.
DR   GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR   GO; GO:0071471; P:cellular response to non-ionic osmotic stress; IMP:CAFA.
DR   GO; GO:0034644; P:cellular response to UV; IEA:Ensembl.
DR   GO; GO:0019371; P:cyclooxygenase pathway; IDA:UniProtKB.
DR   GO; GO:0046697; P:decidualization; IMP:MGI.
DR   GO; GO:0007566; P:embryo implantation; IMP:MGI.
DR   GO; GO:0042633; P:hair cycle; IEA:Ensembl.
DR   GO; GO:0006954; P:inflammatory response; ISO:MGI.
DR   GO; GO:0030216; P:keratinocyte differentiation; NAS:UniProtKB.
DR   GO; GO:0007612; P:learning; ISO:MGI.
DR   GO; GO:0035633; P:maintenance of permeability of blood-brain barrier; ISO:MGI.
DR   GO; GO:0007613; P:memory; ISO:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:CAFA.
DR   GO; GO:0097756; P:negative regulation of blood vessel diameter; ISO:MGI.
DR   GO; GO:0051926; P:negative regulation of calcium ion transport; ISO:MGI.
DR   GO; GO:0045786; P:negative regulation of cell cycle; ISO:MGI.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; ISO:MGI.
DR   GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:CAFA.
DR   GO; GO:1902219; P:negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress; IMP:CAFA.
DR   GO; GO:0045986; P:negative regulation of smooth muscle contraction; ISO:MGI.
DR   GO; GO:0032227; P:negative regulation of synaptic transmission, dopaminergic; ISO:MGI.
DR   GO; GO:0030728; P:ovulation; ISO:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0090336; P:positive regulation of brown fat cell differentiation; IMP:BHF-UCL.
DR   GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
DR   GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; ISO:MGI.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; ISO:MGI.
DR   GO; GO:0031622; P:positive regulation of fever generation; IDA:BHF-UCL.
DR   GO; GO:0090271; P:positive regulation of fibroblast growth factor production; ISO:MGI.
DR   GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:CAFA.
DR   GO; GO:0090362; P:positive regulation of platelet-derived growth factor production; ISO:MGI.
DR   GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; IMP:CAFA.
DR   GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:MGI.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR   GO; GO:0045987; P:positive regulation of smooth muscle contraction; ISO:MGI.
DR   GO; GO:0031915; P:positive regulation of synaptic plasticity; ISO:MGI.
DR   GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISO:MGI.
DR   GO; GO:0071636; P:positive regulation of transforming growth factor beta production; ISO:MGI.
DR   GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISO:MGI.
DR   GO; GO:0045907; P:positive regulation of vasoconstriction; ISO:MGI.
DR   GO; GO:0001516; P:prostaglandin biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR   GO; GO:0042127; P:regulation of cell proliferation; IGI:MGI.
DR   GO; GO:1990776; P:response to angiotensin; IEA:Ensembl.
DR   GO; GO:0034097; P:response to cytokine; ISO:MGI.
DR   GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR   GO; GO:0070542; P:response to fatty acid; IEA:Ensembl.
DR   GO; GO:0009750; P:response to fructose; IEA:Ensembl.
DR   GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; ISO:MGI.
DR   GO; GO:0010226; P:response to lithium ion; IEA:Ensembl.
DR   GO; GO:0010042; P:response to manganese ion; IEA:Ensembl.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   GO; GO:0034612; P:response to tumor necrosis factor; IEA:Ensembl.
DR   GO; GO:0033280; P:response to vitamin D; IEA:Ensembl.
DR   GO; GO:0019233; P:sensory perception of pain; ISO:MGI.
DR   Gene3D; 1.10.640.10; -; 1.
DR   InterPro; IPR029576; COX-2.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR010255; Haem_peroxidase.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR037120; Haem_peroxidase_sf.
DR   PANTHER; PTHR11903:SF8; PTHR11903:SF8; 1.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   Pfam; PF00008; EGF; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SUPFAM; SSF48113; SSF48113; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Dioxygenase;
KW   Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Glycoprotein; Heme;
KW   Iron; Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding;
KW   Microsome; Oxidoreductase; Peroxidase; Prostaglandin biosynthesis;
KW   Prostaglandin metabolism; Reference proteome; S-nitrosylation; Signal.
FT   SIGNAL        1     17
FT   CHAIN        18    604       Prostaglandin G/H synthase 2.
FT                                /FTId=PRO_0000023876.
FT   DOMAIN       18     55       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   ACT_SITE    193    193       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00298,
FT                                ECO:0000269|PubMed:20463020}.
FT   ACT_SITE    371    371       For cyclooxygenase activity.
FT                                {ECO:0000269|PubMed:20463020}.
FT   METAL       374    374       Iron (heme axial ligand).
FT                                {ECO:0000244|PDB:1CX2,
FT                                ECO:0000244|PDB:1PXX,
FT                                ECO:0000244|PDB:3LN0,
FT                                ECO:0000244|PDB:3LN1,
FT                                ECO:0000244|PDB:3MQE,
FT                                ECO:0000244|PDB:3NTB,
FT                                ECO:0000244|PDB:3NTG,
FT                                ECO:0000244|PDB:3PGH,
FT                                ECO:0000244|PDB:4COX,
FT                                ECO:0000244|PDB:4FM5,
FT                                ECO:0000244|PDB:4M10,
FT                                ECO:0000244|PDB:4M11,
FT                                ECO:0000244|PDB:4PH9,
FT                                ECO:0000244|PDB:5COX,
FT                                ECO:0000244|PDB:6COX,
FT                                ECO:0000269|PubMed:12925531,
FT                                ECO:0000269|PubMed:20463020,
FT                                ECO:0000269|PubMed:20810665,
FT                                ECO:0000269|PubMed:21489986,
FT                                ECO:0000269|PubMed:8967954}.
FT   BINDING     106    106       Substrate. {ECO:0000244|PDB:3KRK,
FT                                ECO:0000269|PubMed:20463020}.
FT   BINDING     341    341       Substrate. {ECO:0000244|PDB:3KRK,
FT                                ECO:0000269|PubMed:20463020}.
FT   SITE        516    516       Aspirin-acetylated serine.
FT   SITE        592    592       Not glycosylated.
FT                                {ECO:0000269|PubMed:8349699}.
FT   CARBOHYD     53     53       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000244|PDB:1CVU,
FT                                ECO:0000244|PDB:1CX2,
FT                                ECO:0000244|PDB:1DDX,
FT                                ECO:0000244|PDB:1PXX,
FT                                ECO:0000244|PDB:3HS5,
FT                                ECO:0000244|PDB:3HS6,
FT                                ECO:0000244|PDB:3HS7,
FT                                ECO:0000244|PDB:3KRK,
FT                                ECO:0000244|PDB:3LN0,
FT                                ECO:0000244|PDB:3LN1,
FT                                ECO:0000244|PDB:3MDL,
FT                                ECO:0000244|PDB:3MQE,
FT                                ECO:0000244|PDB:3NT1,
FT                                ECO:0000244|PDB:3NTB,
FT                                ECO:0000244|PDB:3PGH,
FT                                ECO:0000244|PDB:3QH0,
FT                                ECO:0000244|PDB:3QMO,
FT                                ECO:0000244|PDB:3TZI,
FT                                ECO:0000244|PDB:4COX,
FT                                ECO:0000244|PDB:4E1G,
FT                                ECO:0000244|PDB:4M10,
FT                                ECO:0000244|PDB:4M11,
FT                                ECO:0000244|PDB:4OTJ,
FT                                ECO:0000244|PDB:4OTY,
FT                                ECO:0000244|PDB:4PH9,
FT                                ECO:0000244|PDB:4RRW,
FT                                ECO:0000244|PDB:4RRX,
FT                                ECO:0000244|PDB:4RRY,
FT                                ECO:0000244|PDB:4RRZ,
FT                                ECO:0000244|PDB:4RS0,
FT                                ECO:0000244|PDB:4RUT,
FT                                ECO:0000244|PDB:4Z0L,
FT                                ECO:0000244|PDB:5COX,
FT                                ECO:0000244|PDB:5FDQ,
FT                                ECO:0000244|PDB:5JVY,
FT                                ECO:0000244|PDB:5JVZ,
FT                                ECO:0000244|PDB:5JW1,
FT                                ECO:0000244|PDB:6COX,
FT                                ECO:0000269|PubMed:10811226,
FT                                ECO:0000269|PubMed:12925531,
FT                                ECO:0000269|PubMed:20463020,
FT                                ECO:0000269|PubMed:20810665,
FT                                ECO:0000269|PubMed:21467029,
FT                                ECO:0000269|PubMed:21489986,
FT                                ECO:0000269|PubMed:8349699,
FT                                ECO:0000269|PubMed:8967954}.
FT                                /FTId=CAR_000222.
FT   CARBOHYD    130    130       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000244|PDB:1CVU,
FT                                ECO:0000244|PDB:1CX2,
FT                                ECO:0000244|PDB:1DDX,
FT                                ECO:0000244|PDB:1PXX,
FT                                ECO:0000244|PDB:3HS5,
FT                                ECO:0000244|PDB:3HS6,
FT                                ECO:0000244|PDB:3HS7,
FT                                ECO:0000244|PDB:3KRK,
FT                                ECO:0000244|PDB:3LN0,
FT                                ECO:0000244|PDB:3LN1,
FT                                ECO:0000244|PDB:3MDL,
FT                                ECO:0000244|PDB:3MQE,
FT                                ECO:0000244|PDB:3NT1,
FT                                ECO:0000244|PDB:3NTB,
FT                                ECO:0000244|PDB:3NTG,
FT                                ECO:0000244|PDB:3OLT,
FT                                ECO:0000244|PDB:3OLU,
FT                                ECO:0000244|PDB:3PGH,
FT                                ECO:0000244|PDB:3QH0,
FT                                ECO:0000244|PDB:3QMO,
FT                                ECO:0000244|PDB:3TZI,
FT                                ECO:0000244|PDB:4COX,
FT                                ECO:0000244|PDB:4E1G,
FT                                ECO:0000244|PDB:4FM5,
FT                                ECO:0000244|PDB:4M10,
FT                                ECO:0000244|PDB:4M11,
FT                                ECO:0000244|PDB:4OTJ,
FT                                ECO:0000244|PDB:4OTY,
FT                                ECO:0000244|PDB:4PH9,
FT                                ECO:0000244|PDB:4RRW,
FT                                ECO:0000244|PDB:4RRX,
FT                                ECO:0000244|PDB:4RRY,
FT                                ECO:0000244|PDB:4RRZ,
FT                                ECO:0000244|PDB:4RS0,
FT                                ECO:0000244|PDB:4RUT,
FT                                ECO:0000244|PDB:4Z0L,
FT                                ECO:0000244|PDB:5COX,
FT                                ECO:0000244|PDB:5FDQ,
FT                                ECO:0000244|PDB:5JVY,
FT                                ECO:0000244|PDB:5JVZ,
FT                                ECO:0000244|PDB:5JW1,
FT                                ECO:0000244|PDB:6COX,
FT                                ECO:0000269|PubMed:10811226,
FT                                ECO:0000269|PubMed:12925531,
FT                                ECO:0000269|PubMed:20463020,
FT                                ECO:0000269|PubMed:20810665,
FT                                ECO:0000269|PubMed:21467029,
FT                                ECO:0000269|PubMed:21489986,
FT                                ECO:0000269|PubMed:8349699,
FT                                ECO:0000269|PubMed:8967954}.
FT                                /FTId=CAR_000223.
FT   CARBOHYD    396    396       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000244|PDB:1CVU,
FT                                ECO:0000244|PDB:1CX2,
FT                                ECO:0000244|PDB:1DDX,
FT                                ECO:0000244|PDB:1PXX,
FT                                ECO:0000244|PDB:3HS5,
FT                                ECO:0000244|PDB:3HS6,
FT                                ECO:0000244|PDB:3HS7,
FT                                ECO:0000244|PDB:3KRK,
FT                                ECO:0000244|PDB:3LN0,
FT                                ECO:0000244|PDB:3LN1,
FT                                ECO:0000244|PDB:3MDL,
FT                                ECO:0000244|PDB:3MQE,
FT                                ECO:0000244|PDB:3NT1,
FT                                ECO:0000244|PDB:3NTB,
FT                                ECO:0000244|PDB:3NTG,
FT                                ECO:0000244|PDB:3OLT,
FT                                ECO:0000244|PDB:3OLU,
FT                                ECO:0000244|PDB:3PGH,
FT                                ECO:0000244|PDB:3QH0,
FT                                ECO:0000244|PDB:3QMO,
FT                                ECO:0000244|PDB:3TZI,
FT                                ECO:0000244|PDB:4COX,
FT                                ECO:0000244|PDB:4E1G,
FT                                ECO:0000244|PDB:4M10,
FT                                ECO:0000244|PDB:4M11,
FT                                ECO:0000244|PDB:4OTJ,
FT                                ECO:0000244|PDB:4OTY,
FT                                ECO:0000244|PDB:4PH9,
FT                                ECO:0000244|PDB:4RRW,
FT                                ECO:0000244|PDB:4RRX,
FT                                ECO:0000244|PDB:4RRY,
FT                                ECO:0000244|PDB:4RRZ,
FT                                ECO:0000244|PDB:4RS0,
FT                                ECO:0000244|PDB:4RUT,
FT                                ECO:0000244|PDB:4Z0L,
FT                                ECO:0000244|PDB:5COX,
FT                                ECO:0000244|PDB:5FDQ,
FT                                ECO:0000244|PDB:5JVY,
FT                                ECO:0000244|PDB:5JVZ,
FT                                ECO:0000244|PDB:5JW1,
FT                                ECO:0000244|PDB:6COX,
FT                                ECO:0000269|PubMed:10811226,
FT                                ECO:0000269|PubMed:12925531,
FT                                ECO:0000269|PubMed:20463020,
FT                                ECO:0000269|PubMed:20810665,
FT                                ECO:0000269|PubMed:21467029,
FT                                ECO:0000269|PubMed:21489986,
FT                                ECO:0000269|PubMed:8349699,
FT                                ECO:0000269|PubMed:8967954}.
FT                                /FTId=CAR_000224.
FT   CARBOHYD    580    580       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:20463020,
FT                                ECO:0000269|PubMed:8349699}.
FT                                /FTId=CAR_000225.
FT   DISULFID     21     32       {ECO:0000244|PDB:1CVU,
FT                                ECO:0000244|PDB:1CX2,
FT                                ECO:0000244|PDB:1DDX,
FT                                ECO:0000244|PDB:1PXX,
FT                                ECO:0000244|PDB:3HS5,
FT                                ECO:0000244|PDB:3HS6,
FT                                ECO:0000244|PDB:3HS7,
FT                                ECO:0000244|PDB:3KRK,
FT                                ECO:0000244|PDB:3LN0,
FT                                ECO:0000244|PDB:3LN1,
FT                                ECO:0000244|PDB:3MDL,
FT                                ECO:0000244|PDB:3MQE,
FT                                ECO:0000244|PDB:3NT1,
FT                                ECO:0000244|PDB:3NTB,
FT                                ECO:0000244|PDB:3NTG,
FT                                ECO:0000244|PDB:3OLT,
FT                                ECO:0000244|PDB:3OLU,
FT                                ECO:0000244|PDB:3PGH,
FT                                ECO:0000244|PDB:3Q7D,
FT                                ECO:0000244|PDB:3QH0,
FT                                ECO:0000244|PDB:3QMO,
FT                                ECO:0000244|PDB:3RR3,
FT                                ECO:0000244|PDB:3TZI,
FT                                ECO:0000244|PDB:4COX,
FT                                ECO:0000244|PDB:4E1G,
FT                                ECO:0000244|PDB:4FM5,
FT                                ECO:0000244|PDB:4M10,
FT                                ECO:0000244|PDB:4M11,
FT                                ECO:0000244|PDB:4OTJ,
FT                                ECO:0000244|PDB:4OTY,
FT                                ECO:0000244|PDB:4PH9,
FT                                ECO:0000244|PDB:4RRW,
FT                                ECO:0000244|PDB:4RRX,
FT                                ECO:0000244|PDB:4RRY,
FT                                ECO:0000244|PDB:4RRZ,
FT                                ECO:0000244|PDB:4RS0,
FT                                ECO:0000244|PDB:4RUT,
FT                                ECO:0000244|PDB:4Z0L,
FT                                ECO:0000244|PDB:5COX,
FT                                ECO:0000244|PDB:5FDQ,
FT                                ECO:0000244|PDB:5JVY,
FT                                ECO:0000244|PDB:5JVZ,
FT                                ECO:0000244|PDB:5JW1,
FT                                ECO:0000244|PDB:5W58,
FT                                ECO:0000244|PDB:6COX,
FT                                ECO:0000269|PubMed:10811226,
FT                                ECO:0000269|PubMed:12925531,
FT                                ECO:0000269|PubMed:20463020,
FT                                ECO:0000269|PubMed:20810665,
FT                                ECO:0000269|PubMed:21467029,
FT                                ECO:0000269|PubMed:21489986,
FT                                ECO:0000269|PubMed:8967954}.
FT   DISULFID     22    145       {ECO:0000244|PDB:1CVU,
FT                                ECO:0000244|PDB:1CX2,
FT                                ECO:0000244|PDB:1DDX,
FT                                ECO:0000244|PDB:1PXX,
FT                                ECO:0000244|PDB:3HS5,
FT                                ECO:0000244|PDB:3HS6,
FT                                ECO:0000244|PDB:3HS7,
FT                                ECO:0000244|PDB:3KRK,
FT                                ECO:0000244|PDB:3LN0,
FT                                ECO:0000244|PDB:3LN1,
FT                                ECO:0000244|PDB:3MDL,
FT                                ECO:0000244|PDB:3MQE,
FT                                ECO:0000244|PDB:3NT1,
FT                                ECO:0000244|PDB:3NTB,
FT                                ECO:0000244|PDB:3NTG,
FT                                ECO:0000244|PDB:3OLT,
FT                                ECO:0000244|PDB:3OLU,
FT                                ECO:0000244|PDB:3PGH,
FT                                ECO:0000244|PDB:3Q7D,
FT                                ECO:0000244|PDB:3QH0,
FT                                ECO:0000244|PDB:3QMO,
FT                                ECO:0000244|PDB:3RR3,
FT                                ECO:0000244|PDB:3TZI,
FT                                ECO:0000244|PDB:4COX,
FT                                ECO:0000244|PDB:4E1G,
FT                                ECO:0000244|PDB:4FM5,
FT                                ECO:0000244|PDB:4M10,
FT                                ECO:0000244|PDB:4M11,
FT                                ECO:0000244|PDB:4OTJ,
FT                                ECO:0000244|PDB:4OTY,
FT                                ECO:0000244|PDB:4PH9,
FT                                ECO:0000244|PDB:4RRW,
FT                                ECO:0000244|PDB:4RRX,
FT                                ECO:0000244|PDB:4RRY,
FT                                ECO:0000244|PDB:4RRZ,
FT                                ECO:0000244|PDB:4RS0,
FT                                ECO:0000244|PDB:4RUT,
FT                                ECO:0000244|PDB:4Z0L,
FT                                ECO:0000244|PDB:5COX,
FT                                ECO:0000244|PDB:5FDQ,
FT                                ECO:0000244|PDB:5JVY,
FT                                ECO:0000244|PDB:5JVZ,
FT                                ECO:0000244|PDB:5JW1,
FT                                ECO:0000244|PDB:5W58,
FT                                ECO:0000244|PDB:6COX,
FT                                ECO:0000269|PubMed:10811226,
FT                                ECO:0000269|PubMed:12925531,
FT                                ECO:0000269|PubMed:20463020,
FT                                ECO:0000269|PubMed:20810665,
FT                                ECO:0000269|PubMed:21467029,
FT                                ECO:0000269|PubMed:21489986,
FT                                ECO:0000269|PubMed:8967954}.
FT   DISULFID     26     42       {ECO:0000244|PDB:1CVU,
FT                                ECO:0000244|PDB:1CX2,
FT                                ECO:0000244|PDB:1DDX,
FT                                ECO:0000244|PDB:1PXX,
FT                                ECO:0000244|PDB:3HS5,
FT                                ECO:0000244|PDB:3HS6,
FT                                ECO:0000244|PDB:3HS7,
FT                                ECO:0000244|PDB:3KRK,
FT                                ECO:0000244|PDB:3LN0,
FT                                ECO:0000244|PDB:3LN1,
FT                                ECO:0000244|PDB:3MDL,
FT                                ECO:0000244|PDB:3MQE,
FT                                ECO:0000244|PDB:3NT1,
FT                                ECO:0000244|PDB:3NTB,
FT                                ECO:0000244|PDB:3NTG,
FT                                ECO:0000244|PDB:3OLT,
FT                                ECO:0000244|PDB:3OLU,
FT                                ECO:0000244|PDB:3PGH,
FT                                ECO:0000244|PDB:3Q7D,
FT                                ECO:0000244|PDB:3QH0,
FT                                ECO:0000244|PDB:3QMO,
FT                                ECO:0000244|PDB:3RR3,
FT                                ECO:0000244|PDB:3TZI,
FT                                ECO:0000244|PDB:4COX,
FT                                ECO:0000244|PDB:4E1G,
FT                                ECO:0000244|PDB:4FM5,
FT                                ECO:0000244|PDB:4M10,
FT                                ECO:0000244|PDB:4M11,
FT                                ECO:0000244|PDB:4OTJ,
FT                                ECO:0000244|PDB:4OTY,
FT                                ECO:0000244|PDB:4PH9,
FT                                ECO:0000244|PDB:4RRW,
FT                                ECO:0000244|PDB:4RRX,
FT                                ECO:0000244|PDB:4RRY,
FT                                ECO:0000244|PDB:4RRZ,
FT                                ECO:0000244|PDB:4RS0,
FT                                ECO:0000244|PDB:4RUT,
FT                                ECO:0000244|PDB:4Z0L,
FT                                ECO:0000244|PDB:5COX,
FT                                ECO:0000244|PDB:5FDQ,
FT                                ECO:0000244|PDB:5JVY,
FT                                ECO:0000244|PDB:5JVZ,
FT                                ECO:0000244|PDB:5JW1,
FT                                ECO:0000244|PDB:5W58,
FT                                ECO:0000244|PDB:6COX,
FT                                ECO:0000269|PubMed:10811226,
FT                                ECO:0000269|PubMed:12925531,
FT                                ECO:0000269|PubMed:20463020,
FT                                ECO:0000269|PubMed:20810665,
FT                                ECO:0000269|PubMed:21467029,
FT                                ECO:0000269|PubMed:21489986,
FT                                ECO:0000269|PubMed:8967954}.
FT   DISULFID     44     54       {ECO:0000244|PDB:1CVU,
FT                                ECO:0000244|PDB:1CX2,
FT                                ECO:0000244|PDB:1DDX,
FT                                ECO:0000244|PDB:1PXX,
FT                                ECO:0000244|PDB:3HS5,
FT                                ECO:0000244|PDB:3HS6,
FT                                ECO:0000244|PDB:3HS7,
FT                                ECO:0000244|PDB:3KRK,
FT                                ECO:0000244|PDB:3LN0,
FT                                ECO:0000244|PDB:3LN1,
FT                                ECO:0000244|PDB:3MDL,
FT                                ECO:0000244|PDB:3MQE,
FT                                ECO:0000244|PDB:3NT1,
FT                                ECO:0000244|PDB:3NTB,
FT                                ECO:0000244|PDB:3NTG,
FT                                ECO:0000244|PDB:3OLT,
FT                                ECO:0000244|PDB:3OLU,
FT                                ECO:0000244|PDB:3PGH,
FT                                ECO:0000244|PDB:3Q7D,
FT                                ECO:0000244|PDB:3QH0,
FT                                ECO:0000244|PDB:3QMO,
FT                                ECO:0000244|PDB:3RR3,
FT                                ECO:0000244|PDB:3TZI,
FT                                ECO:0000244|PDB:4COX,
FT                                ECO:0000244|PDB:4E1G,
FT                                ECO:0000244|PDB:4FM5,
FT                                ECO:0000244|PDB:4M10,
FT                                ECO:0000244|PDB:4M11,
FT                                ECO:0000244|PDB:4OTJ,
FT                                ECO:0000244|PDB:4OTY,
FT                                ECO:0000244|PDB:4PH9,
FT                                ECO:0000244|PDB:4RRW,
FT                                ECO:0000244|PDB:4RRX,
FT                                ECO:0000244|PDB:4RRY,
FT                                ECO:0000244|PDB:4RRZ,
FT                                ECO:0000244|PDB:4RS0,
FT                                ECO:0000244|PDB:4RUT,
FT                                ECO:0000244|PDB:4Z0L,
FT                                ECO:0000244|PDB:5COX,
FT                                ECO:0000244|PDB:5FDQ,
FT                                ECO:0000244|PDB:5JVY,
FT                                ECO:0000244|PDB:5JVZ,
FT                                ECO:0000244|PDB:5JW1,
FT                                ECO:0000244|PDB:5W58,
FT                                ECO:0000244|PDB:6COX,
FT                                ECO:0000269|PubMed:10811226,
FT                                ECO:0000269|PubMed:12925531,
FT                                ECO:0000269|PubMed:20463020,
FT                                ECO:0000269|PubMed:20810665,
FT                                ECO:0000269|PubMed:21467029,
FT                                ECO:0000269|PubMed:21489986,
FT                                ECO:0000269|PubMed:8967954}.
FT   DISULFID    555    561       {ECO:0000244|PDB:1CVU,
FT                                ECO:0000244|PDB:1CX2,
FT                                ECO:0000244|PDB:1DDX,
FT                                ECO:0000244|PDB:1PXX,
FT                                ECO:0000244|PDB:3HS5,
FT                                ECO:0000244|PDB:3HS6,
FT                                ECO:0000244|PDB:3HS7,
FT                                ECO:0000244|PDB:3KRK,
FT                                ECO:0000244|PDB:3LN0,
FT                                ECO:0000244|PDB:3LN1,
FT                                ECO:0000244|PDB:3MDL,
FT                                ECO:0000244|PDB:3MQE,
FT                                ECO:0000244|PDB:3NT1,
FT                                ECO:0000244|PDB:3NTB,
FT                                ECO:0000244|PDB:3NTG,
FT                                ECO:0000244|PDB:3OLT,
FT                                ECO:0000244|PDB:3OLU,
FT                                ECO:0000244|PDB:3PGH,
FT                                ECO:0000244|PDB:3Q7D,
FT                                ECO:0000244|PDB:3QH0,
FT                                ECO:0000244|PDB:3QMO,
FT                                ECO:0000244|PDB:3RR3,
FT                                ECO:0000244|PDB:3TZI,
FT                                ECO:0000244|PDB:4COX,
FT                                ECO:0000244|PDB:4E1G,
FT                                ECO:0000244|PDB:4FM5,
FT                                ECO:0000244|PDB:4M10,
FT                                ECO:0000244|PDB:4M11,
FT                                ECO:0000244|PDB:4OTJ,
FT                                ECO:0000244|PDB:4OTY,
FT                                ECO:0000244|PDB:4PH9,
FT                                ECO:0000244|PDB:4RRW,
FT                                ECO:0000244|PDB:4RRX,
FT                                ECO:0000244|PDB:4RRY,
FT                                ECO:0000244|PDB:4RRZ,
FT                                ECO:0000244|PDB:4RS0,
FT                                ECO:0000244|PDB:4RUT,
FT                                ECO:0000244|PDB:4Z0L,
FT                                ECO:0000244|PDB:5COX,
FT                                ECO:0000244|PDB:5FDQ,
FT                                ECO:0000244|PDB:5JVY,
FT                                ECO:0000244|PDB:5JVZ,
FT                                ECO:0000244|PDB:5JW1,
FT                                ECO:0000244|PDB:5W58,
FT                                ECO:0000244|PDB:6COX,
FT                                ECO:0000269|PubMed:10811226,
FT                                ECO:0000269|PubMed:12925531,
FT                                ECO:0000269|PubMed:20463020,
FT                                ECO:0000269|PubMed:20810665,
FT                                ECO:0000269|PubMed:21467029,
FT                                ECO:0000269|PubMed:21489986,
FT                                ECO:0000269|PubMed:8967954}.
FT   MUTAGEN     517    517       L->A,F,P,T: Slightly reduced activity.
FT                                {ECO:0000269|PubMed:20463020}.
FT   MUTAGEN     580    580       N->A: Loss of glycosylation site.
FT                                {ECO:0000269|PubMed:20463020}.
FT   CONFLICT     98     98       I -> T (in Ref. 1; AAA39924).
FT                                {ECO:0000305}.
FT   CONFLICT    142    142       A -> R (in Ref. 3; AAA39918).
FT                                {ECO:0000305}.
FT   CONFLICT    301    301       I -> L (in Ref. 7; no nucleotide entry).
FT                                {ECO:0000305}.
FT   CONFLICT    585    585       H -> R (in Ref. 3; AAA39918).
FT                                {ECO:0000305}.
FT   TURN         20     23       {ECO:0000244|PDB:3NT1}.
FT   HELIX        27     29       {ECO:0000244|PDB:6COX}.
FT   STRAND       31     36       {ECO:0000244|PDB:3NT1}.
FT   STRAND       39     43       {ECO:0000244|PDB:3NT1}.
FT   STRAND       47     50       {ECO:0000244|PDB:3NT1}.
FT   TURN         51     54       {ECO:0000244|PDB:3NT1}.
FT   HELIX        59     67       {ECO:0000244|PDB:3NT1}.
FT   HELIX        71     78       {ECO:0000244|PDB:3NT1}.
FT   HELIX        82     89       {ECO:0000244|PDB:3NT1}.
FT   HELIX        92    107       {ECO:0000244|PDB:3NT1}.
FT   STRAND      108    110       {ECO:0000244|PDB:5JW1}.
FT   STRAND      116    119       {ECO:0000244|PDB:4RRX}.
FT   STRAND      120    122       {ECO:0000244|PDB:3NT1}.
FT   HELIX       125    129       {ECO:0000244|PDB:3NT1}.
FT   STRAND      131    133       {ECO:0000244|PDB:1DDX}.
FT   STRAND      135    138       {ECO:0000244|PDB:3NT1}.
FT   STRAND      145    147       {ECO:0000244|PDB:1DDX}.
FT   STRAND      150    153       {ECO:0000244|PDB:3NT1}.
FT   HELIX       160    167       {ECO:0000244|PDB:3NT1}.
FT   HELIX       182    192       {ECO:0000244|PDB:3NT1}.
FT   TURN        193    195       {ECO:0000244|PDB:3NT1}.
FT   TURN        200    202       {ECO:0000244|PDB:3NT1}.
FT   STRAND      206    208       {ECO:0000244|PDB:3NT1}.
FT   STRAND      213    215       {ECO:0000244|PDB:4PH9}.
FT   HELIX       217    220       {ECO:0000244|PDB:3NT1}.
FT   HELIX       224    230       {ECO:0000244|PDB:3NT1}.
FT   STRAND      241    243       {ECO:0000244|PDB:3NT1}.
FT   STRAND      246    248       {ECO:0000244|PDB:3NT1}.
FT   HELIX       252    255       {ECO:0000244|PDB:3NT1}.
FT   STRAND      263    265       {ECO:0000244|PDB:6COX}.
FT   HELIX       267    269       {ECO:0000244|PDB:3NT1}.
FT   TURN        276    279       {ECO:0000244|PDB:3NT1}.
FT   HELIX       282    305       {ECO:0000244|PDB:3NT1}.
FT   HELIX       311    332       {ECO:0000244|PDB:3NT1}.
FT   HELIX       334    339       {ECO:0000244|PDB:3NT1}.
FT   HELIX       349    352       {ECO:0000244|PDB:3NT1}.
FT   HELIX       365    370       {ECO:0000244|PDB:3NT1}.
FT   HELIX       374    376       {ECO:0000244|PDB:3NT1}.
FT   STRAND      379    383       {ECO:0000244|PDB:3NT1}.
FT   STRAND      386    388       {ECO:0000244|PDB:3NT1}.
FT   HELIX       390    393       {ECO:0000244|PDB:3NT1}.
FT   HELIX       398    414       {ECO:0000244|PDB:3NT1}.
FT   STRAND      420    424       {ECO:0000244|PDB:3NT1}.
FT   HELIX       428    430       {ECO:0000244|PDB:3NT1}.
FT   HELIX       431    443       {ECO:0000244|PDB:3NT1}.
FT   HELIX       449    455       {ECO:0000244|PDB:3NT1}.
FT   HELIX       464    468       {ECO:0000244|PDB:3NT1}.
FT   STRAND      469    471       {ECO:0000244|PDB:3NT1}.
FT   HELIX       472    481       {ECO:0000244|PDB:3NT1}.
FT   HELIX       484    486       {ECO:0000244|PDB:3NT1}.
FT   HELIX       489    495       {ECO:0000244|PDB:3NT1}.
FT   STRAND      503    505       {ECO:0000244|PDB:4PH9}.
FT   HELIX       506    521       {ECO:0000244|PDB:3NT1}.
FT   HELIX       524    526       {ECO:0000244|PDB:3NT1}.
FT   TURN        528    530       {ECO:0000244|PDB:3NT1}.
FT   HELIX       533    536       {ECO:0000244|PDB:3NT1}.
FT   HELIX       539    546       {ECO:0000244|PDB:3NT1}.
FT   HELIX       550    557       {ECO:0000244|PDB:3NT1}.
FT   STRAND      558    560       {ECO:0000244|PDB:3Q7D}.
SQ   SEQUENCE   604 AA;  69013 MW;  DFE1658295C92064 CRC64;
     MLFRAVLLCA ALGLSQAANP CCSNPCQNRG ECMSTGFDQY KCDCTRTGFY GENCTTPEFL
     TRIKLLLKPT PNTVHYILTH FKGVWNIVNN IPFLRSLIMK YVLTSRSYLI DSPPTYNVHY
     GYKSWEAFSN LSYYTRALPP VADDCPTPMG VKGNKELPDS KEVLEKVLLR REFIPDPQGS
     NMMFAFFAQH FTHQFFKTDH KRGPGFTRGL GHGVDLNHIY GETLDRQHKL RLFKDGKLKY
     QVIGGEVYPP TVKDTQVEMI YPPHIPENLQ FAVGQEVFGL VPGLMMYATI WLREHNRVCD
     ILKQEHPEWG DEQLFQTSRL ILIGETIKIV IEDYVQHLSG YHFKLKFDPE LLFNQQFQYQ
     NRIASEFNTL YHWHPLLPDT FNIEDQEYSF KQFLYNNSIL LEHGLTQFVE SFTRQIAGRV
     AGGRNVPIAV QAVAKASIDQ SREMKYQSLN EYRKRFSLKP YTSFEELTGE KEMAAELKAL
     YSDIDVMELY PALLVEKPRP DAIFGETMVE LGAPFSLKGL MGNPICSPQY WKPSTFGGEV
     GFKIINTASI QSLICNNVKG CPFTSFNVQD PQPTKTATIN ASASHSRLDD INPTVLIKRR
     STEL
//
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