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Database: UniProt/SWISS-PROT
Entry: PGH1_SHEEP
LinkDB: PGH1_SHEEP
Original site: PGH1_SHEEP 
ID   PGH1_SHEEP              Reviewed;         600 AA.
AC   P05979;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   04-FEB-2015, sequence version 3.
DT   25-APR-2018, entry version 158.
DE   RecName: Full=Prostaglandin G/H synthase 1;
DE            EC=1.14.99.1;
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   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANT
RP   GLY-164.
RC   TISSUE=Seminal vesicle;
RX   PubMed=3125548; DOI=10.1073/pnas.85.5.1412;
RA   Dewitt D.L., Smith W.L.;
RT   "Primary structure of prostaglandin G/H synthase from sheep vesicular
RT   gland determined from the complementary DNA sequence.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:1412-1416(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=3129310; DOI=10.1016/0014-5793(88)80847-0;
RA   Yokoyama C., Takai T., Tanabe T.;
RT   "Primary structure of sheep prostaglandin endoperoxide synthase
RT   deduced from cDNA sequence.";
RL   FEBS Lett. 231:347-351(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT GLY-164.
RX   PubMed=2831188;
RA   Merlie J., Fagan D., Mudd J., Needleman P.;
RT   "Isolation and characterization of the complementary DNA for sheep
RT   seminal vesicle prostaglandin endoperoxide synthase
RT   (cyclooxygenase).";
RL   J. Biol. Chem. 263:3550-3553(1988).
RN   [4]
RP   PROTEIN SEQUENCE OF 523-544.
RX   PubMed=6414516; DOI=10.1021/bi00289a010;
RA   Roth G.J., Machuga E.T., Ozols J.;
RT   "Isolation and covalent structure of the aspirin-modified, active-site
RT   region of prostaglandin synthetase.";
RL   Biochemistry 22:4672-4675(1983).
RN   [5]
RP   HEME-BINDING SITE.
RX   PubMed=2108169;
RA   Dewitt D.L., El-Harith E.A., Kraemer S.A., Andrews M.J., Yao E.F.,
RA   Armstrong R.L., Smith W.L.;
RT   "The aspirin and heme-binding sites of ovine and murine prostaglandin
RT   endoperoxide synthases.";
RL   J. Biol. Chem. 265:5192-5198(1990).
RN   [6]
RP   ACTIVE SITE TYR-385, AND MUTAGENESIS OF TYR-385.
RX   PubMed=2122967;
RA   Shimokawa T., Kulmacz R.J., Dewitt D.L., Smith W.L.;
RT   "Tyrosine 385 of prostaglandin endoperoxide synthase is required for
RT   cyclooxygenase catalysis.";
RL   J. Biol. Chem. 265:20073-20076(1990).
RN   [7]
RP   GLYCOSYLATION AT ASN-68; ASN-144 AND ASN-410, AND LACK OF
RP   GLYCOSYLATION AT ASN-104.
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   [8]
RP   FUNCTION, AND INHIBITION BY NSAIDS.
RX   PubMed=10438452; DOI=10.1074/jbc.274.33.22903;
RA   Marnett L.J., Rowlinson S.W., Goodwin D.C., Kalgutkar A.S.,
RA   Lanzo C.A.;
RT   "Arachidonic acid oxygenation by COX-1 and COX-2. Mechanisms of
RT   catalysis and inhibition.";
RL   J. Biol. Chem. 274:22903-22906(1999).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
RX   PubMed=8121489; DOI=10.1038/367243a0;
RA   Picot D., Loll P.J., Garavito R.M.;
RT   "The X-ray crystal structure of the membrane protein prostaglandin H2
RT   synthase-1.";
RL   Nature 367:243-249(1994).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS).
RX   PubMed=7552725; DOI=10.1038/nsb0895-637;
RA   Loll P.J., Picot D., Garavito R.M.;
RT   "The structural basis of aspirin activity inferred from the crystal
RT   structure of inactivated prostaglandin H2 synthase.";
RL   Nat. Struct. Biol. 2:637-643(1995).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
RX   PubMed=8652509; DOI=10.1021/bi952776w;
RA   Loll P.J., Picot D., Ekabo O., Garavito R.M.;
RT   "Synthesis and use of iodinated antiinflammatory drug analogs as
RT   crystallographic probes of the prostaglandin H2 synthase
RT   cyclooxygenase active site.";
RL   Biochemistry 35:7330-7340(1996).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX   PubMed=10988074; DOI=10.1126/science.289.5486.1933;
RA   Malkowski M.G., Ginell S.L., Smith W.L., Garavito R.M.;
RT   "The productive conformation of arachidonic acid bound to
RT   prostaglandin synthase.";
RL   Science 289:1933-1937(2000).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX   PubMed=11121413; DOI=10.1074/jbc.M009378200;
RA   Thuresson E.D., Malkowski M.G., Lakkides K.M., Rieke C.J.,
RA   Mulichak A.M., Ginell S.L., Garavito R.M., Smith W.L.;
RT   "Mutational and X-ray crystallographic analysis of the interaction of
RT   dihomo-gamma-linolenic acid with prostaglandin endoperoxide H
RT   synthases.";
RL   J. Biol. Chem. 276:10358-10365(2001).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS).
RX   PubMed=11318639; DOI=10.1021/bi010045s;
RA   Selinsky B.S., Gupta K., Sharkey C.T., Loll P.J.;
RT   "Structural analysis of NSAID binding by prostaglandin H2 synthase:
RT   time-dependent and time-independent inhibitors elicit identical enzyme
RT   conformations.";
RL   Biochemistry 40:5172-5180(2001).
CC   -!- FUNCTION: Converts arachidonate to prostaglandin H2 (PGH2), a
CC       committed step in prostanoid synthesis. Involved in the
CC       constitutive production of prostanoids in particular in the
CC       stomach and platelets. In gastric epithelial cells, it is a key
CC       step in the generation of prostaglandins, such as prostaglandin E2
CC       (PGE2), which plays an important role in cytoprotection. In
CC       platelets, it is involved in the generation of thromboxane A2
CC       (TXA2), which promotes platelet activation and aggregation,
CC       vasoconstriction and proliferation of vascular smooth muscle
CC       cells. {ECO:0000269|PubMed:10438452}.
CC   -!- CATALYTIC ACTIVITY: Arachidonate + AH(2) + 2 O(2) = prostaglandin
CC       H(2) + A + H(2)O.
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
CC       subunit.;
CC   -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein. Microsome membrane; Multi-pass membrane protein.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA31576.1; Type=Frameshift; Positions=63, 92; Evidence={ECO:0000305};
DR   EMBL; J03599; AAA31576.1; ALT_FRAME; mRNA.
DR   EMBL; Y00750; CAA68719.1; -; mRNA.
DR   EMBL; M18243; AAA31511.1; -; mRNA.
DR   PIR; A28960; A28960.
DR   PIR; A29947; A29947.
DR   PIR; S00561; S00561.
DR   RefSeq; NP_001009476.1; NM_001009476.1.
DR   UniGene; Oar.445; -.
DR   PDB; 1CQE; X-ray; 3.10 A; A/B=21-600.
DR   PDB; 1DIY; X-ray; 3.00 A; A=32-584.
DR   PDB; 1DJJ; Model; -; A=25-600.
DR   PDB; 1EBV; X-ray; 3.20 A; A=33-583.
DR   PDB; 1EQG; X-ray; 2.61 A; A/B=21-600.
DR   PDB; 1EQH; X-ray; 2.70 A; A/B=21-600.
DR   PDB; 1FE2; X-ray; 3.00 A; A=25-600.
DR   PDB; 1HT5; X-ray; 2.75 A; A/B=33-583.
DR   PDB; 1HT8; X-ray; 2.69 A; A/B=33-583.
DR   PDB; 1IGX; X-ray; 3.10 A; A=25-600.
DR   PDB; 1IGZ; X-ray; 2.90 A; A=25-600.
DR   PDB; 1PGE; X-ray; 3.50 A; A/B=25-600.
DR   PDB; 1PGF; X-ray; 4.50 A; A/B=25-600.
DR   PDB; 1PGG; X-ray; 4.50 A; A/B=25-600.
DR   PDB; 1PRH; X-ray; 3.50 A; A/B=33-586.
DR   PDB; 1PTH; X-ray; 3.40 A; A/B=25-600.
DR   PDB; 1Q4G; X-ray; 2.00 A; A/B=32-584.
DR   PDB; 1U67; X-ray; 3.10 A; A=1-600.
DR   PDB; 2AYL; X-ray; 2.00 A; A/B=32-584.
DR   PDB; 2OYE; X-ray; 2.85 A; P=1-600.
DR   PDB; 2OYU; X-ray; 2.70 A; P=1-600.
DR   PDB; 3KK6; X-ray; 2.75 A; A/B=32-584.
DR   PDB; 3N8V; X-ray; 3.05 A; A/B=32-584.
DR   PDB; 3N8W; X-ray; 2.75 A; A/B=32-584.
DR   PDB; 3N8X; X-ray; 2.75 A; A/B=32-584.
DR   PDB; 3N8Y; X-ray; 2.60 A; A/B=32-584.
DR   PDB; 3N8Z; X-ray; 2.90 A; A/B=32-584.
DR   PDB; 4O1Z; X-ray; 2.40 A; A/B=32-600.
DR   PDB; 5U6X; X-ray; 2.93 A; A/B=1-600.
DR   PDB; 5WBE; X-ray; 2.75 A; A/B=1-600.
DR   PDBsum; 1CQE; -.
DR   PDBsum; 1DIY; -.
DR   PDBsum; 1DJJ; -.
DR   PDBsum; 1EBV; -.
DR   PDBsum; 1EQG; -.
DR   PDBsum; 1EQH; -.
DR   PDBsum; 1FE2; -.
DR   PDBsum; 1HT5; -.
DR   PDBsum; 1HT8; -.
DR   PDBsum; 1IGX; -.
DR   PDBsum; 1IGZ; -.
DR   PDBsum; 1PGE; -.
DR   PDBsum; 1PGF; -.
DR   PDBsum; 1PGG; -.
DR   PDBsum; 1PRH; -.
DR   PDBsum; 1PTH; -.
DR   PDBsum; 1Q4G; -.
DR   PDBsum; 1U67; -.
DR   PDBsum; 2AYL; -.
DR   PDBsum; 2OYE; -.
DR   PDBsum; 2OYU; -.
DR   PDBsum; 3KK6; -.
DR   PDBsum; 3N8V; -.
DR   PDBsum; 3N8W; -.
DR   PDBsum; 3N8X; -.
DR   PDBsum; 3N8Y; -.
DR   PDBsum; 3N8Z; -.
DR   PDBsum; 4O1Z; -.
DR   PDBsum; 5U6X; -.
DR   PDBsum; 5WBE; -.
DR   SMR; P05979; -.
DR   BindingDB; P05979; -.
DR   ChEMBL; CHEMBL2949; -.
DR   MoonProt; P05979; -.
DR   PeroxiBase; 4121; OarPGHS01.
DR   iPTMnet; P05979; -.
DR   PRIDE; P05979; -.
DR   GeneID; 443551; -.
DR   KEGG; oas:443551; -.
DR   CTD; 5742; -.
DR   HOVERGEN; HBG000366; -.
DR   KO; K00509; -.
DR   BRENDA; 1.14.99.1; 2668.
DR   SABIO-RK; P05979; -.
DR   UniPathway; UPA00662; -.
DR   EvolutionaryTrace; P05979; -.
DR   PRO; PR:P05979; -.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
DR   GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008144; F:drug binding; IDA:CAFA.
DR   GO; GO:0020037; F:heme binding; IDA:CAFA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004666; F:prostaglandin-endoperoxide synthase activity; IMP:CAFA.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR   GO; GO:0019371; P:cyclooxygenase pathway; IMP:CAFA.
DR   GO; GO:0006954; P:inflammatory response; IEA:InterPro.
DR   GO; GO:0001516; P:prostaglandin biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   Gene3D; 1.10.640.10; -; 1.
DR   InterPro; IPR029580; COX-1.
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:SF6; PTHR11903:SF6; 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; EGF-like domain;
KW   Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Glycoprotein; Heme; Iron; Lipid biosynthesis; Lipid metabolism;
KW   Membrane; Metal-binding; Microsome; Oxidoreductase; Peroxidase;
KW   Prostaglandin biosynthesis; Prostaglandin metabolism;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     24
FT   CHAIN        25    600       Prostaglandin G/H synthase 1.
FT                                /FTId=PRO_0000023871.
FT   TRANSMEM     74     82       Helical.
FT   TRANSMEM     86     92       Helical.
FT   TRANSMEM     97    105       Helical.
FT   TRANSMEM    108    122       Helical.
FT   DOMAIN       32     70       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   ACT_SITE    207    207       Proton acceptor.
FT   ACT_SITE    385    385       For cyclooxygenase activity.
FT                                {ECO:0000269|PubMed:2122967}.
FT   METAL       388    388       Iron (heme axial ligand).
FT   SITE        104    104       Not glycosylated.
FT                                {ECO:0000269|PubMed:8349699}.
FT   SITE        530    530       Aspirin-acetylated serine.
FT   CARBOHYD     68     68       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:8349699}.
FT   CARBOHYD    144    144       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:8349699}.
FT   CARBOHYD    410    410       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:8349699}.
FT   DISULFID     36     47
FT   DISULFID     37    159
FT   DISULFID     41     57
FT   DISULFID     59     69
FT   DISULFID    569    575
FT   VARIANT      97     97       R -> H.
FT   VARIANT     164    164       D -> G. {ECO:0000269|PubMed:2831188,
FT                                ECO:0000269|PubMed:3125548}.
FT   VARIANT     456    456       R -> Q.
FT   VARIANT     520    520       E -> K.
FT   VARIANT     520    520       E -> Q.
FT   VARIANT     525    525       M -> I.
FT   MUTAGEN     385    385       Y->F: Abolishes cyclooxygenase activity.
FT                                {ECO:0000269|PubMed:2122967}.
FT   CONFLICT      1      5       MSRQS -> MVQG (in Ref. 3; AAA31511).
FT                                {ECO:0000305}.
FT   CONFLICT    193    193       S -> G (in Ref. 1; AAA31576 and 3;
FT                                AAA31511). {ECO:0000305}.
FT   CONFLICT    540    540       C -> E (in Ref. 4; AA sequence).
FT                                {ECO:0000305}.
FT   HELIX        35     38       {ECO:0000244|PDB:1Q4G}.
FT   STRAND       46     50       {ECO:0000244|PDB:1Q4G}.
FT   TURN         51     53       {ECO:0000244|PDB:1Q4G}.
FT   STRAND       54     58       {ECO:0000244|PDB:1Q4G}.
FT   STRAND       62     65       {ECO:0000244|PDB:1Q4G}.
FT   TURN         66     69       {ECO:0000244|PDB:1Q4G}.
FT   HELIX        74     82       {ECO:0000244|PDB:1Q4G}.
FT   HELIX        86     93       {ECO:0000244|PDB:1Q4G}.
FT   HELIX        97    103       {ECO:0000244|PDB:1Q4G}.
FT   HELIX       108    121       {ECO:0000244|PDB:1Q4G}.
FT   STRAND      130    133       {ECO:0000244|PDB:1Q4G}.
FT   STRAND      134    136       {ECO:0000244|PDB:1EQG}.
FT   HELIX       139    143       {ECO:0000244|PDB:1Q4G}.
FT   STRAND      149    152       {ECO:0000244|PDB:1Q4G}.
FT   STRAND      159    161       {ECO:0000244|PDB:1EQG}.
FT   STRAND      164    167       {ECO:0000244|PDB:1Q4G}.
FT   HELIX       174    181       {ECO:0000244|PDB:1Q4G}.
FT   HELIX       196    206       {ECO:0000244|PDB:1Q4G}.
FT   TURN        207    209       {ECO:0000244|PDB:1Q4G}.
FT   TURN        214    216       {ECO:0000244|PDB:1Q4G}.
FT   STRAND      220    222       {ECO:0000244|PDB:1Q4G}.
FT   STRAND      227    229       {ECO:0000244|PDB:1Q4G}.
FT   HELIX       231    234       {ECO:0000244|PDB:1Q4G}.
FT   HELIX       238    244       {ECO:0000244|PDB:1Q4G}.
FT   STRAND      255    257       {ECO:0000244|PDB:1Q4G}.
FT   STRAND      260    262       {ECO:0000244|PDB:1Q4G}.
FT   TURN        266    268       {ECO:0000244|PDB:1Q4G}.
FT   HELIX       281    283       {ECO:0000244|PDB:1Q4G}.
FT   STRAND      288    291       {ECO:0000244|PDB:3KK6}.
FT   HELIX       292    294       {ECO:0000244|PDB:1Q4G}.
FT   HELIX       296    319       {ECO:0000244|PDB:1Q4G}.
FT   HELIX       325    346       {ECO:0000244|PDB:1Q4G}.
FT   HELIX       348    353       {ECO:0000244|PDB:1Q4G}.
FT   HELIX       363    366       {ECO:0000244|PDB:1Q4G}.
FT   STRAND      367    369       {ECO:0000244|PDB:5WBE}.
FT   HELIX       379    384       {ECO:0000244|PDB:1Q4G}.
FT   HELIX       388    390       {ECO:0000244|PDB:1Q4G}.
FT   STRAND      393    397       {ECO:0000244|PDB:1Q4G}.
FT   STRAND      400    402       {ECO:0000244|PDB:1Q4G}.
FT   HELIX       404    407       {ECO:0000244|PDB:1Q4G}.
FT   HELIX       413    417       {ECO:0000244|PDB:1Q4G}.
FT   HELIX       419    428       {ECO:0000244|PDB:1Q4G}.
FT   STRAND      434    438       {ECO:0000244|PDB:1Q4G}.
FT   TURN        442    444       {ECO:0000244|PDB:1Q4G}.
FT   HELIX       445    457       {ECO:0000244|PDB:1Q4G}.
FT   HELIX       463    469       {ECO:0000244|PDB:1Q4G}.
FT   HELIX       478    482       {ECO:0000244|PDB:1Q4G}.
FT   STRAND      483    485       {ECO:0000244|PDB:1Q4G}.
FT   HELIX       486    495       {ECO:0000244|PDB:1Q4G}.
FT   HELIX       498    500       {ECO:0000244|PDB:1Q4G}.
FT   HELIX       503    509       {ECO:0000244|PDB:1Q4G}.
FT   STRAND      517    519       {ECO:0000244|PDB:2OYU}.
FT   HELIX       520    535       {ECO:0000244|PDB:1Q4G}.
FT   HELIX       538    540       {ECO:0000244|PDB:1Q4G}.
FT   TURN        542    544       {ECO:0000244|PDB:1Q4G}.
FT   HELIX       547    550       {ECO:0000244|PDB:1Q4G}.
FT   HELIX       553    560       {ECO:0000244|PDB:1Q4G}.
FT   HELIX       564    569       {ECO:0000244|PDB:1Q4G}.
FT   STRAND      572    574       {ECO:0000244|PDB:1Q4G}.
SQ   SEQUENCE   600 AA;  68861 MW;  809887C7BB5A715C CRC64;
     MSRQSISLRF PLLLLLLSPS PVFSADPGAP APVNPCCYYP CQHQGICVRF GLDRYQCDCT
     RTGYSGPNCT IPEIWTWLRT TLRPSPSFIH FLLTHGRWLW DFVNATFIRD TLMRLVLTVR
     SNLIPSPPTY NIAHDYISWE SFSNVSYYTR ILPSVPRDCP TPMDTKGKKQ LPDAEFLSRR
     FLLRRKFIPD PQSTNLMFAF FAQHFTHQFF KTSGKMGPGF TKALGHGVDL GHIYGDNLER
     QYQLRLFKDG KLKYQMLNGE VYPPSVEEAP VLMHYPRGIP PQSQMAVGQE VFGLLPGLML
     YATIWLREHN RVCDLLKAEH PTWGDEQLFQ TARLILIGET IKIVIEEYVQ QLSGYFLQLK
     FDPELLFGAQ FQYRNRIAME FNQLYHWHPL MPDSFRVGPQ DYSYEQFLFN TSMLVDYGVE
     ALVDAFSRQP AGRIGGGRNI DHHILHVAVD VIKESRVLRL QPFNEYRKRF GMKPYTSFQE
     LTGEKEMAAE LEELYGDIDA LEFYPGLLLE KCHPNSIFGE SMIEMGAPFS LKGLLGNPIC
     SPEYWKASTF GGEVGFNLVK TATLKKLVCL NTKTCPYVSF HVPDPRQEDR PGVERPPTEL
//
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