PGES2_MOUSE
ID PGES2_MOUSE Reviewed; 384 AA.
AC Q8BWM0; A2ASQ2; Q99J30;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Prostaglandin E synthase 2;
DE EC=5.3.99.3 {ECO:0000250|UniProtKB:Q9H7Z7};
DE AltName: Full=GATE-binding factor 1 {ECO:0000303|PubMed:12050152};
DE Short=GBF-1 {ECO:0000303|PubMed:12050152};
DE AltName: Full=Microsomal prostaglandin E synthase 2;
DE Short=mPGES-2;
DE Contains:
DE RecName: Full=Prostaglandin E synthase 2 truncated form;
GN Name=Ptges2; Synonyms=Gbf1, Pges2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], POSSIBLE FUNCTION, POSSIBLE SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=12050152; DOI=10.1074/jbc.m202679200;
RA Hu J., Meng Q., Roy S.K., Raha A., Hu J., Zhang J., Hashimoto K.,
RA Kalvakolanu D.V.;
RT "A novel transactivating factor that regulates interferon-gamma-dependent
RT gene expression.";
RL J. Biol. Chem. 277:30253-30263(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=12835322; DOI=10.1074/jbc.m305108200;
RA Murakami M., Nakashima K., Kamei D., Masuda S., Ishikawa Y., Ishii T.,
RA Ohmiya Y., Watanabe K., Kudo I.;
RT "Cellular prostaglandin E2 production by membrane-bound prostaglandin E
RT synthase-2 via both cyclooxygenases-1 and -2.";
RL J. Biol. Chem. 278:37937-37947(2003).
RN [7]
RP INDUCTION.
RX PubMed=15584915; DOI=10.1111/j.1471-4159.2004.02829.x;
RA Bosetti F., Langenbach R., Weerasinghe G.R.;
RT "Prostaglandin E2 and microsomal prostaglandin E synthase-2 expression are
RT decreased in the cyclooxygenase-2-deficient mouse brain despite
RT compensatory induction of cyclooxygenase-1 and Ca2+-dependent phospholipase
RT A2.";
RL J. Neurochem. 91:1389-1397(2004).
RN [8]
RP INTERACTION WITH CEBPB.
RX PubMed=15879117; DOI=10.4049/jimmunol.174.10.6203;
RA Meng Q., Raha A., Roy S., Hu J., Kalvakolanu D.V.;
RT "IFN-gamma-stimulated transcriptional activation by IFN-gamma-activated
RT transcriptional element-binding factor 1 occurs via an inducible
RT interaction with CAAAT/enhancer-binding protein-beta.";
RL J. Immunol. 174:6203-6211(2005).
RN [9]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=19010439; DOI=10.1016/j.prostaglandins.2008.10.003;
RA Jania L.A., Chandrasekharan S., Backlund M.G., Foley N.A., Snouwaert J.,
RA Wang I.M., Clark P., Audoly L.P., Koller B.H.;
RT "Microsomal prostaglandin E synthase-2 is not essential for in vivo
RT prostaglandin E2 biosynthesis.";
RL Prostaglandins Other Lipid Mediat. 88:73-81(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=25076362; DOI=10.1016/j.jhep.2014.07.018;
RA Sun Y., Jia Z., Yang G., Kakizoe Y., Liu M., Yang K.T., Liu Y., Yang B.,
RA Yang T.;
RT "mPGES-2 deletion remarkably enhances liver injury in streptozotocin-
RT treated mice via induction of GLUT2.";
RL J. Hepatol. 61:1328-1336(2014).
CC -!- FUNCTION: Isomerase that catalyzes the conversion of PGH2 into the more
CC stable prostaglandin E2 (PGE2) (in vitro). The biological function and
CC the GSH-dependent property of PTGES2 is still under debate (By
CC similarity). In vivo, PTGES2 could form a complex with GSH and heme and
CC would not participate in PGE2 synthesis but would catalyze the
CC degradation of prostaglandin E2 H2 (PGH2) to 12(S)-hydroxy-
CC 5(Z),8(E),10(E)-heptadecatrienoic acid (HHT) and malondialdehyde (MDA)
CC (By similarity). May also have transactivation activity toward IFN-
CC gamma (IFNG), possibly via an interaction with CEBPB; however, the
CC relevance of transcription activation activity remains unclear
CC (PubMed:12050152). {ECO:0000250|UniProtKB:Q9H7Z7,
CC ECO:0000250|UniProtKB:Q9N0A4, ECO:0000303|PubMed:12050152}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=prostaglandin H2 = prostaglandin E2; Xref=Rhea:RHEA:12893,
CC ChEBI:CHEBI:57405, ChEBI:CHEBI:606564; EC=5.3.99.3;
CC Evidence={ECO:0000250|UniProtKB:Q9H7Z7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12894;
CC Evidence={ECO:0000250|UniProtKB:Q9H7Z7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=prostaglandin H2 = (12S)-hydroxy-(5Z,8E,10E)-
CC heptadecatrienoate + malonaldehyde; Xref=Rhea:RHEA:48644,
CC ChEBI:CHEBI:57405, ChEBI:CHEBI:90694, ChEBI:CHEBI:566274;
CC Evidence={ECO:0000250|UniProtKB:Q9H7Z7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48645;
CC Evidence={ECO:0000250|UniProtKB:Q9H7Z7};
CC -!- ACTIVITY REGULATION: Isomerase activity is increased by sulfhydril
CC compounds. Dithiothreitol (DTT) is most effective, followed by
CC glutathione (GSH) and 2-mercaptoethanol.
CC {ECO:0000250|UniProtKB:Q66LN0}.
CC -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC -!- SUBUNIT: Homodimer. Interacts with EXOSC10 (By similarity). May
CC interact with CEBPB. {ECO:0000250|UniProtKB:Q66LN0,
CC ECO:0000250|UniProtKB:Q9H7Z7, ECO:0000269|PubMed:15879117}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9H7Z7}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9H7Z7}. Nucleus {ECO:0000269|PubMed:12050152}.
CC Note=According to PubMed:12050152, some fraction may be nuclear.
CC {ECO:0000269|PubMed:12050152}.
CC -!- SUBCELLULAR LOCATION: [Prostaglandin E synthase 2 truncated form]:
CC Cytoplasm {ECO:0000250|UniProtKB:Q9H7Z7}. Note=Synthesized as a Golgi
CC membrane-bound protein, which is further cleaved into the predominant
CC soluble truncated form. {ECO:0000250|UniProtKB:Q9H7Z7}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in brain, heart, liver,
CC colon and lung. {ECO:0000269|PubMed:12050152,
CC ECO:0000269|PubMed:12835322, ECO:0000269|PubMed:19010439}.
CC -!- INDUCTION: Constitutively expressed. Not induced during tissue
CC inflammation. Down-regulated in the absence of PTGES.
CC {ECO:0000269|PubMed:12835322, ECO:0000269|PubMed:15584915}.
CC -!- PTM: Synthesized as a Golgi membrane-associated protein, and the
CC proteolytic removal of the N-terminal hydrophobic domain leads to the
CC formation of a mature cytosolic enzyme. {ECO:0000250|UniProtKB:Q9H7Z7}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice displays no obvious phenotype and
CC are fertile. Loss of PTGES2 expression does not result in a measurable
CC decrease in PGE2 levels in any tissue or cell type examined from
CC healthy mice (PubMed:19010439). Injection of the diabetogenic agent
CC streptozotocin (STZ) at a dose to induce type-1 diabetes to knockout
CC (KO) mice aggravates STZ-induced liver toxicity associated with high
CC lethality, despite similar glucose levels (PubMed:25076362).
CC {ECO:0000269|PubMed:19010439, ECO:0000269|PubMed:25076362}.
CC -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
CC -!- CAUTION: It is not known if heme and GST are required for prostaglandin
CC synthase activity. The protein copurifies with heme and GST when DTT is
CC omitted during the purification procedure. The GSH-heme complex-bound
CC enzyme has been proposed to act as a lyase and catalyze the degradation
CC of prostaglandin E2 H2 (PGH2) to 12(S)-hydroxy-5(Z),8(E),10(E)-
CC heptadecatrienoic acid (HHT) and malondialdehyde (MDA). Boiling the
CC enzyme leads to loss of prostaglandin synthase activity, but does not
CC eliminate the lyase activity. Besides, free heme can catalyze the
CC formation of 12L-hydroxy-5,8,10-heptadecatrienoic acid (HHT) (By
CC similarity). A more recent study demonstrates the GSH-dependent
CC property of PTGES2, DTT dissociates the bound heme to produce active
CC PGE2 synthase in vitro (By similarity). PTGES2 can only catalyzes PGE2
CC synthesis in the free state as an enzyme, while in vivo it forms a
CC complex with heme and does not participate in PGE2 synthesis (By
CC similarity). In agreement with this study, the in vivo evidence from
CC PTGES2 deficient mice do not show that this protein is responsible for
CC the PGE2 production under basal or pathophysiological conditions
CC (PubMed:19010439). {ECO:0000250|UniProtKB:Q9H7Z7,
CC ECO:0000250|UniProtKB:Q9N0A4, ECO:0000269|PubMed:19010439,
CC ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK050616; BAC34345.1; -; mRNA.
DR EMBL; AL928669; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466542; EDL08547.1; -; Genomic_DNA.
DR EMBL; BC004846; AAH04846.1; -; mRNA.
DR CCDS; CCDS15914.1; -.
DR RefSeq; NP_598544.2; NM_133783.2.
DR AlphaFoldDB; Q8BWM0; -.
DR SMR; Q8BWM0; -.
DR BioGRID; 220557; 2.
DR IntAct; Q8BWM0; 2.
DR STRING; 10090.ENSMUSP00000028162; -.
DR iPTMnet; Q8BWM0; -.
DR PhosphoSitePlus; Q8BWM0; -.
DR SwissPalm; Q8BWM0; -.
DR EPD; Q8BWM0; -.
DR jPOST; Q8BWM0; -.
DR MaxQB; Q8BWM0; -.
DR PaxDb; Q8BWM0; -.
DR PeptideAtlas; Q8BWM0; -.
DR PRIDE; Q8BWM0; -.
DR ProteomicsDB; 288182; -.
DR Antibodypedia; 17330; 328 antibodies from 34 providers.
DR DNASU; 96979; -.
DR Ensembl; ENSMUST00000028162; ENSMUSP00000028162; ENSMUSG00000026820.
DR GeneID; 96979; -.
DR KEGG; mmu:96979; -.
DR UCSC; uc008jfm.2; mouse.
DR CTD; 80142; -.
DR MGI; MGI:1917592; Ptges2.
DR VEuPathDB; HostDB:ENSMUSG00000026820; -.
DR eggNOG; KOG3029; Eukaryota.
DR GeneTree; ENSGT00390000000224; -.
DR HOGENOM; CLU_011226_0_0_1; -.
DR InParanoid; Q8BWM0; -.
DR OMA; LWTGGCA; -.
DR OrthoDB; 1042777at2759; -.
DR PhylomeDB; Q8BWM0; -.
DR TreeFam; TF314304; -.
DR Reactome; R-MMU-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR UniPathway; UPA00662; -.
DR BioGRID-ORCS; 96979; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Ptges2; mouse.
DR PRO; PR:Q8BWM0; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8BWM0; protein.
DR Bgee; ENSMUSG00000026820; Expressed in right kidney and 255 other tissues.
DR ExpressionAtlas; Q8BWM0; baseline and differential.
DR Genevisible; Q8BWM0; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0036134; F:12-hydroxyheptadecatrienoic acid synthase activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0043295; F:glutathione binding; ISS:UniProtKB.
DR GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR GO; GO:0016829; F:lyase activity; ISS:UniProtKB.
DR GO; GO:0050220; F:prostaglandin-E synthase activity; ISO:MGI.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046903; P:secretion; IDA:MGI.
DR CDD; cd03197; GST_C_mPGES2; 1.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR034334; PGES2.
DR InterPro; IPR034335; PGES2_C.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF13417; GST_N_3; 1.
DR SFLD; SFLDG01203; Prostaglandin_E_synthase_like1; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism; Golgi apparatus;
KW Isomerase; Lipid biosynthesis; Lipid metabolism; Membrane; Nucleus;
KW Prostaglandin biosynthesis; Prostaglandin metabolism; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..384
FT /note="Prostaglandin E synthase 2"
FT /id="PRO_0000013131"
FT CHAIN 87..384
FT /note="Prostaglandin E synthase 2 truncated form"
FT /evidence="ECO:0000250|UniProtKB:Q66LN0"
FT /id="PRO_0000013132"
FT TOPO_DOM 1..56
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 89..192
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT DOMAIN 262..376
FT /note="GST C-terminal"
FT BINDING 147
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q9N0A4"
FT BINDING 163..164
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q9N0A4"
FT SITE 86..87
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q66LN0"
FT CONFLICT 210
FT /note="L -> P (in Ref. 5; AAH04846)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 384 AA; 43324 MW; 5A737A01466582CA CRC64;
MAQAARLSWV LVSSRCALTE GLLTRPWQPL SAQSRAGFTR VAAGSRGAAV RKGSPRLLGA
AALALGGALG LYHTVRWHQR SQDLRAERSA AQLPLSNSLQ LTLYQYKTCP FCSKVRAFLD
FHSLPYQVVE VNPVRRTEIK FSSYRKVPIL VAQEGDSLQQ LNDSSVIISA LKTYLVSGQP
LEEVITYYPP MKAMNDQGKE VTEFCNKYWL MLDEKEAQQM YGGKEARTEE MKWRQWADDW
LVHLISPNVY RTPAEALASF DYIVREGKFG AVEAAMAKYV GAAAMYLISK RLKSRHHLQD
DVRVDLYEAA NKWVTAVGKD RPFMGGQKPN LADLAVYGVL RVMEGLEAFD DLMRHSHIQP
WYLRMERAIE EAPSVHHVNP SCKD
