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Database: UniProt/SWISS-PROT
Entry: PGH2_RAT
LinkDB: PGH2_RAT
Original site: PGH2_RAT 
ID   PGH2_RAT                Reviewed;         604 AA.
AC   P35355; Q64379; Q925V4;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   12-SEP-2018, entry version 173.
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=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   Flags: Precursor;
GN   Name=Ptgs2; Synonyms=Cox-2, Cox2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7916614; DOI=10.1006/bbrc.1993.2506;
RA   Kennedy B.P., Chan C.C., Culp S.A., Cromlish W.A.;
RT   "Cloning and expression of rat prostaglandin endoperoxide synthase
RT   (cyclooxygenase)-2 cDNA.";
RL   Biochem. Biophys. Res. Commun. 197:494-500(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8352945; DOI=10.1016/0896-6273(93)90192-T;
RA   Yamagata K., Andreasson K.I., Kaufmann W.E., Barnes C.A., Worley P.F.;
RT   "Expression of a mitogen-inducible cyclooxygenase in brain neurons:
RT   regulation by synaptic activity and glucocorticoids.";
RL   Neuron 11:371-386(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar; TISSUE=Intestine;
RX   PubMed=8203528;
RA   Dubois R.N., Tsujii M., Bishop P., Awad J.A., Makita K., Lanahan A.;
RT   "Cloning and characterization of a growth factor-inducible
RT   cyclooxygenase gene from rat intestinal epithelial cells.";
RL   Am. J. Physiol. 266:G822-G827(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Fischer 344;
RX   PubMed=8274023; DOI=10.1006/abbi.1993.1601;
RA   Feng L., Sun W., Xia Y., Tang W.W., Chanmugam P., Soyoola E.,
RA   Wilson C.B., Hwang D.;
RT   "Cloning two isoforms of rat cyclooxygenase: differential regulation
RT   of their expression.";
RL   Arch. Biochem. Biophys. 307:361-368(1993).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10816563; DOI=10.1074/jbc.M001611200;
RA   Xu K., Robida A.M., Murphy T.J.;
RT   "Immediate-early MEK-1-dependent stabilization of rat smooth muscle
RT   cell cyclooxygenase-2 mRNA by Galpha(q)-coupled receptor signaling.";
RL   J. Biol. Chem. 275:23012-23019(2000).
RN   [6]
RP   PROTEIN SEQUENCE OF 18-43.
RX   PubMed=1556140;
RA   Sirois J., Richards J.S.;
RT   "Purification and characterization of a novel, distinct isoform of
RT   prostaglandin endoperoxide synthase induced by human chorionic
RT   gonadotropin in granulosa cells of rat preovulatory follicles.";
RL   J. Biol. Chem. 267:6382-6388(1992).
RN   [7]
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   [8]
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).
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:0000250|UniProtKB:Q05769}.
CC   -!- CATALYTIC ACTIVITY: Arachidonate + AH(2) + 2 O(2) = prostaglandin
CC       H(2) + A + H(2)O. {ECO:0000250|UniProtKB:Q05769}.
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000250|UniProtKB:Q05769};
CC       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
CC       subunit. {ECO:0000250|UniProtKB:Q05769};
CC   -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC       {ECO:0000250|UniProtKB:P35354}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q05769}.
CC   -!- SUBCELLULAR LOCATION: Microsome membrane; Peripheral membrane
CC       protein. Endoplasmic reticulum membrane; Peripheral membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Expressed throughout the forebrain in discrete
CC       populations of neurons and is enriched in the cortex and
CC       hippocampus.
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   -!- 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; L25925; AAA16477.1; -; mRNA.
DR   EMBL; U04300; AAA20246.1; -; mRNA.
DR   EMBL; U03389; AAA03466.1; -; mRNA.
DR   EMBL; S67722; AAB29401.1; -; mRNA.
DR   EMBL; AF233596; AAF36986.1; -; mRNA.
DR   PIR; JC2030; JC2030.
DR   RefSeq; NP_058928.3; NM_017232.3.
DR   UniGene; Rn.217585; -.
DR   UniGene; Rn.44369; -.
DR   ProteinModelPortal; P35355; -.
DR   SMR; P35355; -.
DR   BioGrid; 248163; 6.
DR   CORUM; P35355; -.
DR   IntAct; P35355; 1.
DR   STRING; 10116.ENSRNOP00000003567; -.
DR   BindingDB; P35355; -.
DR   ChEMBL; CHEMBL2977; -.
DR   PeroxiBase; 3975; RnoPGHS02-A.
DR   iPTMnet; P35355; -.
DR   PhosphoSitePlus; P35355; -.
DR   PaxDb; P35355; -.
DR   PRIDE; P35355; -.
DR   Ensembl; ENSRNOT00000003567; ENSRNOP00000003567; ENSRNOG00000002525.
DR   GeneID; 29527; -.
DR   KEGG; rno:29527; -.
DR   UCSC; RGD:620349; rat.
DR   CTD; 5743; -.
DR   RGD; 620349; Ptgs2.
DR   eggNOG; KOG2408; Eukaryota.
DR   eggNOG; ENOG410XPZ3; LUCA.
DR   GeneTree; ENSGT00390000010743; -.
DR   HOGENOM; HOG000013149; -.
DR   HOVERGEN; HBG000366; -.
DR   InParanoid; P35355; -.
DR   KO; K11987; -.
DR   OMA; CNNVKGC; -.
DR   OrthoDB; EOG091G03CD; -.
DR   PhylomeDB; P35355; -.
DR   TreeFam; TF329675; -.
DR   BRENDA; 1.14.99.1; 5301.
DR   Reactome; R-RNO-197264; Nicotinamide salvaging.
DR   Reactome; R-RNO-2142770; Synthesis of 15-eicosatetraenoic acid derivatives.
DR   Reactome; R-RNO-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR   Reactome; R-RNO-9018677; Biosynthesis of DHA-derived SPMs.
DR   Reactome; R-RNO-9018679; Biosynthesis of EPA-derived SPMs.
DR   Reactome; R-RNO-9025094; Biosynthesis of DPAn-3 SPMs.
DR   Reactome; R-RNO-9027604; Biosynthesis of electrophilic Omega-3 PUFA oxo-derivatives.
DR   UniPathway; UPA00662; -.
DR   PRO; PR:P35355; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000002525; Expressed in 9 organ(s), highest expression level in Ammon's horn.
DR   Genevisible; P35355; RN.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR   GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR   GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR   GO; GO:0020037; F:heme binding; ISS: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; IDA:RGD.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004666; F:prostaglandin-endoperoxide synthase activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0007568; P:aging; IEP:RGD.
DR   GO; GO:0001525; P:angiogenesis; IMP:RGD.
DR   GO; GO:0030282; P:bone mineralization; IMP:MGI.
DR   GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0071318; P:cellular response to ATP; IEP:RGD.
DR   GO; GO:0071498; P:cellular response to fluid shear stress; IEA:Ensembl.
DR   GO; GO:0034605; P:cellular response to heat; IEP:RGD.
DR   GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR   GO; GO:0071284; P:cellular response to lead ion; IEP:RGD.
DR   GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
DR   GO; GO:0071471; P:cellular response to non-ionic osmotic stress; IEA:Ensembl.
DR   GO; GO:0034644; P:cellular response to UV; IEP:RGD.
DR   GO; GO:0019371; P:cyclooxygenase pathway; ISS:UniProtKB.
DR   GO; GO:0046697; P:decidualization; IMP:RGD.
DR   GO; GO:0007566; P:embryo implantation; IMP:RGD.
DR   GO; GO:0042633; P:hair cycle; IEP:RGD.
DR   GO; GO:0006954; P:inflammatory response; IMP:RGD.
DR   GO; GO:0007612; P:learning; IMP:RGD.
DR   GO; GO:0035633; P:maintenance of permeability of blood-brain barrier; IMP:RGD.
DR   GO; GO:0007613; P:memory; IMP:RGD.
DR   GO; GO:0097756; P:negative regulation of blood vessel diameter; IMP:RGD.
DR   GO; GO:0051926; P:negative regulation of calcium ion transport; IMP:RGD.
DR   GO; GO:0045786; P:negative regulation of cell cycle; IGI:RGD.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IDA:RGD.
DR   GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR   GO; GO:1902219; P:negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress; IEA:Ensembl.
DR   GO; GO:0045986; P:negative regulation of smooth muscle contraction; IMP:RGD.
DR   GO; GO:0032227; P:negative regulation of synaptic transmission, dopaminergic; IMP:RGD.
DR   GO; GO:0030728; P:ovulation; IMP:RGD.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR   GO; GO:0090336; P:positive regulation of brown fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0010942; P:positive regulation of cell death; IMP:RGD.
DR   GO; GO:0090050; P:positive regulation of cell migration involved in sprouting angiogenesis; IMP:BHF-UCL.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IMP:RGD.
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; IMP:BHF-UCL.
DR   GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:BHF-UCL.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR   GO; GO:0090362; P:positive regulation of platelet-derived growth factor production; IMP:BHF-UCL.
DR   GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; IEA:Ensembl.
DR   GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:RGD.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:RGD.
DR   GO; GO:0045987; P:positive regulation of smooth muscle contraction; IMP:RGD.
DR   GO; GO:0031915; P:positive regulation of synaptic plasticity; IMP:RGD.
DR   GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IMP:RGD.
DR   GO; GO:0071636; P:positive regulation of transforming growth factor beta production; IMP:BHF-UCL.
DR   GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IMP:BHF-UCL.
DR   GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:RGD.
DR   GO; GO:0001516; P:prostaglandin biosynthetic process; IMP:RGD.
DR   GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
DR   GO; GO:1990776; P:response to angiotensin; IEP:RGD.
DR   GO; GO:0034097; P:response to cytokine; IMP:RGD.
DR   GO; GO:0042493; P:response to drug; IEP:RGD.
DR   GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR   GO; GO:0070542; P:response to fatty acid; IEP:RGD.
DR   GO; GO:0009750; P:response to fructose; IEP:RGD.
DR   GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IMP:RGD.
DR   GO; GO:0010226; P:response to lithium ion; IEP:RGD.
DR   GO; GO:0010042; P:response to manganese ion; IEP:RGD.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR   GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR   GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   GO; GO:0009314; P:response to radiation; IEP:RGD.
DR   GO; GO:0034612; P:response to tumor necrosis factor; IEP:RGD.
DR   GO; GO:0033280; P:response to vitamin D; IEP:RGD.
DR   GO; GO:0019233; P:sensory perception of pain; IMP:RGD.
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; 2.
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   Complete proteome; Dioxygenase; Direct protein sequencing;
KW   Disulfide bond; Endoplasmic reticulum; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Glycoprotein; Heme; Iron; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Metal-binding; Microsome; Oxidoreductase;
KW   Peroxidase; Prostaglandin biosynthesis; Prostaglandin metabolism;
KW   Reference proteome; S-nitrosylation; Signal.
FT   SIGNAL        1     17       {ECO:0000269|PubMed:1556140}.
FT   CHAIN        18    604       Prostaglandin G/H synthase 2.
FT                                /FTId=PRO_0000023879.
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   ACT_SITE    371    371       For cyclooxygenase activity.
FT                                {ECO:0000250|UniProtKB:Q05769}.
FT   METAL       374    374       Iron (heme axial ligand).
FT                                {ECO:0000255|PROSITE-ProRule:PRU00298}.
FT   BINDING     106    106       Substrate.
FT                                {ECO:0000250|UniProtKB:Q05769}.
FT   BINDING     341    341       Substrate.
FT                                {ECO:0000250|UniProtKB:Q05769}.
FT   SITE        516    516       Aspirin-acetylated serine.
FT                                {ECO:0000250|UniProtKB:P35354}.
FT   CARBOHYD     53     53       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    130    130       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    396    396       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    580    580       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     21     32       {ECO:0000250|UniProtKB:Q05769}.
FT   DISULFID     22    145       {ECO:0000250|UniProtKB:Q05769}.
FT   DISULFID     26     42       {ECO:0000250|UniProtKB:Q05769}.
FT   DISULFID     44     54       {ECO:0000250|UniProtKB:Q05769}.
FT   DISULFID    555    561       {ECO:0000250|UniProtKB:Q05769}.
FT   CONFLICT     11     13       ALA -> CPG (in Ref. 4 and 5).
FT                                {ECO:0000305}.
FT   CONFLICT     58     58       E -> R (in Ref. 4 and 5). {ECO:0000305}.
FT   CONFLICT     66     66       L -> P (in Ref. 4 and 5). {ECO:0000305}.
FT   CONFLICT     96     98       NSI -> IQS (in Ref. 4 and 5).
FT                                {ECO:0000305}.
FT   CONFLICT    339    339       S -> R (in Ref. 4 and 5). {ECO:0000305}.
FT   CONFLICT    344    344       K -> Q (in Ref. 4 and 5). {ECO:0000305}.
FT   CONFLICT    350    350       E -> D (in Ref. 4 and 5). {ECO:0000305}.
FT   CONFLICT    368    368       N -> K (in Ref. 4 and 5). {ECO:0000305}.
FT   CONFLICT    573    573       P -> A (in Ref. 4 and 5). {ECO:0000305}.
SQ   SEQUENCE   604 AA;  69164 MW;  98E418825D98FF0C CRC64;
     MLFRAVLLCA ALALSHAANP CCSNPCQNRG ECMSIGFDQY KCDCTRTGFY GENCTTPEFL
     TRIKLLLKPT PNTVHYILTH FKGVWNIVNN IPFLRNSIMR YVLTSRSHLI DSPPTYNVHY
     GYKSWEAFSN LSYYTRALPP VADDCPTPMG VKGNKELPDS KEVLEKVLLR REFIPDPQGT
     NMMFAFFAQH FTHQFFKTDQ KRGPGFTRGL GHGVDLNHVY GETLDRQHKL RLFQDGKLKY
     QVIGGEVYPP TVKDTQVDMI YPPHVPEHLR FAVGQEVFGL VPGLMMYATI WLREHNRVCD
     ILKQEHPEWD DERLFQTSRL ILIGETIKIV IEDYVQHLSG YHFKLKFDPE LLFNQQFQYQ
     NRIASEFNTL YHWHPLLPDT FNIEDQEYTF KQFLYNNSIL LEHGLAHFVE SFTRQIAGRV
     AGGRNVPIAV QAVAKASIDQ SREMKYQSLN EYRKRFSLKP YTSFEELTGE KEMAAELKAL
     YHDIDAMELY PALLVEKPRP DAIFGETMVE LGAPFSLKGL MGNPICSPQY WKPSTFGGEV
     GFRIINTASI QSLICNNVKG CPFASFNVQD PQPTKTATIN ASASHSRLDD INPTVLIKRR
     STEL
//
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