ANPRA_RAT
ID ANPRA_RAT Reviewed; 1057 AA.
AC P18910; A1A5N8;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Atrial natriuretic peptide receptor 1;
DE EC=4.6.1.2 {ECO:0000269|PubMed:2563900};
DE AltName: Full=Atrial natriuretic peptide receptor type A;
DE Short=ANP-A;
DE Short=ANPR-A;
DE Short=NPR-A;
DE AltName: Full=Guanylate cyclase A;
DE Short=GC-A {ECO:0000303|PubMed:2563900};
DE Flags: Precursor;
GN Name=Npr1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=2563900; DOI=10.1038/338078a0;
RA Chinkers M., Garbers D.L., Chang M.S., Lowe D.G., Chin H., Goeddel D.V.,
RA Schulz S.;
RT "A membrane form of guanylate cyclase is an atrial natriuretic peptide
RT receptor.";
RL Nature 338:78-83(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1978722; DOI=10.1016/s0021-9258(17)30520-3;
RA Yamaguchi M., Rutledge L.J., Garbers D.L.;
RT "The primary structure of the rat guanylyl cyclase A/atrial natriuretic
RT peptide receptor gene.";
RL J. Biol. Chem. 265:20414-20420(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF GLU-338 AND LEU-364.
RX PubMed=1679239; DOI=10.1073/pnas.88.17.7882;
RA Duda T., Goraczniak R.M., Sharma R.K.;
RT "Site-directed mutational analysis of a membrane guanylate cyclase cDNA
RT reveals the atrial natriuretic factor signaling site.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:7882-7886(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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 [5]
RP PHOSPHORYLATION AT SER-525; THR-528; SER-530; SER-534; SER-538 AND THR-541,
RP AND MUTAGENESIS OF SER-522; SER-525; THR-528; SER-530; SER-534; SER-538;
RP THR-541 AND THR-542.
RX PubMed=9528788; DOI=10.1128/mcb.18.4.2164;
RA Potter L.R., Hunter T.;
RT "Phosphorylation of the kinase homology domain is essential for activation
RT of the A-type natriuretic peptide receptor.";
RL Mol. Cell. Biol. 18:2164-2172(1998).
RN [6]
RP PHOSPHORYLATION AT SER-515; SER-525; THR-528; SER-530; SER-534; SER-538 AND
RP THR-541.
RX PubMed=20977274; DOI=10.1021/bi101700e;
RA Yoder A.R., Stone M.D., Griffin T.J., Potter L.R.;
RT "Mass spectrometric identification of phosphorylation sites in guanylyl
RT cyclase A and B.";
RL Biochemistry 49:10137-10145(2010).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 29-463 IN COMPLEX WITH CHLORIDE,
RP MUTAGENESIS OF GLU-197 AND HIS-213, SUBUNIT, AND GLYCOSYLATION AT ASN-208.
RX PubMed=10894551; DOI=10.1038/35017602;
RA van den Akker F., Zhang X., Miyagi M., Huo X., Misono K.S., Yee V.C.;
RT "Structure of the dimerized hormone-binding domain of a guanylyl-cyclase-
RT coupled receptor.";
RL Nature 406:101-104(2000).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 29-463 IN COMPLEX WITH NPPA AND
RP CHLORIDE, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-208.
RX PubMed=15117952; DOI=10.1074/jbc.m313222200;
RA Ogawa H., Qiu Y., Ogata C.M., Misono K.S.;
RT "Crystal structure of hormone-bound atrial natriuretic peptide receptor
RT extracellular domain: rotation mechanism for transmembrane signal
RT transduction.";
RL J. Biol. Chem. 279:28625-28631(2004).
CC -!- FUNCTION: Receptor for the atrial natriuretic peptide NPPA/ANP and the
CC brain natriuretic peptide NPPB/BNP which are potent vasoactive hormones
CC playing a key role in cardiovascular homeostasis. Has guanylate cyclase
CC activity upon binding of the ligand. {ECO:0000269|PubMed:2563900}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2;
CC Evidence={ECO:0000269|PubMed:2563900};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13666;
CC Evidence={ECO:0000269|PubMed:2563900};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10894551,
CC ECO:0000269|PubMed:15117952}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:2563900}; Single-
CC pass type I membrane protein {ECO:0000255}.
CC -!- PTM: Phosphorylation of the protein kinase-like domain is required for
CC full activation by ANP. {ECO:0000269|PubMed:20977274,
CC ECO:0000269|PubMed:9528788}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR EMBL; X14773; CAA32881.1; -; mRNA.
DR EMBL; J05677; AAA41200.1; -; Genomic_DNA.
DR EMBL; M74535; AAA41202.1; -; mRNA.
DR EMBL; BC128742; AAI28743.1; -; mRNA.
DR PIR; S03348; OYRTR.
DR RefSeq; NP_036745.1; NM_012613.1.
DR RefSeq; XP_006232653.1; XM_006232591.3.
DR PDB; 1DP4; X-ray; 2.00 A; A/C=29-463.
DR PDB; 1T34; X-ray; 2.95 A; A/B=29-463.
DR PDB; 3A3K; X-ray; 2.50 A; A/B=29-463.
DR PDB; 7BRG; X-ray; 2.45 A; A/B=29-463.
DR PDB; 7BRH; X-ray; 2.45 A; A/B=29-463.
DR PDB; 7BRI; X-ray; 2.45 A; A/B=29-463.
DR PDB; 7BRJ; X-ray; 2.70 A; A/B=29-463.
DR PDB; 7BRK; X-ray; 2.85 A; A/B=29-463.
DR PDB; 7BRL; X-ray; 3.20 A; A/B=29-463.
DR PDBsum; 1DP4; -.
DR PDBsum; 1T34; -.
DR PDBsum; 3A3K; -.
DR PDBsum; 7BRG; -.
DR PDBsum; 7BRH; -.
DR PDBsum; 7BRI; -.
DR PDBsum; 7BRJ; -.
DR PDBsum; 7BRK; -.
DR PDBsum; 7BRL; -.
DR AlphaFoldDB; P18910; -.
DR SMR; P18910; -.
DR ComplexPortal; CPX-33; ANPR-A receptor complex.
DR IntAct; P18910; 2.
DR MINT; P18910; -.
DR STRING; 10116.ENSRNOP00000020307; -.
DR BindingDB; P18910; -.
DR ChEMBL; CHEMBL5277; -.
DR GuidetoPHARMACOLOGY; 1747; -.
DR GlyGen; P18910; 6 sites.
DR iPTMnet; P18910; -.
DR PhosphoSitePlus; P18910; -.
DR jPOST; P18910; -.
DR PaxDb; P18910; -.
DR PRIDE; P18910; -.
DR Ensembl; ENSRNOT00000020307; ENSRNOP00000020307; ENSRNOG00000014684.
DR GeneID; 24603; -.
DR KEGG; rno:24603; -.
DR UCSC; RGD:3195; rat.
DR CTD; 4881; -.
DR RGD; 3195; Npr1.
DR eggNOG; KOG1023; Eukaryota.
DR GeneTree; ENSGT00940000156223; -.
DR HOGENOM; CLU_001072_1_3_1; -.
DR InParanoid; P18910; -.
DR OMA; KCAYEKS; -.
DR OrthoDB; 229634at2759; -.
DR PhylomeDB; P18910; -.
DR TreeFam; TF106338; -.
DR BRENDA; 4.6.1.2; 5301.
DR Reactome; R-RNO-5578768; Physiological factors.
DR EvolutionaryTrace; P18910; -.
DR PRO; PR:P18910; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000014684; Expressed in lung and 19 other tissues.
DR Genevisible; P18910; RN.
DR GO; GO:1990620; C:ANPR-A receptor complex; IPI:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004383; F:guanylate cyclase activity; IDA:RGD.
DR GO; GO:0042562; F:hormone binding; ISO:RGD.
DR GO; GO:0016941; F:natriuretic peptide receptor activity; ISO:RGD.
DR GO; GO:0017046; F:peptide hormone binding; ISO:RGD.
DR GO; GO:0001653; F:peptide receptor activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IMP:RGD.
DR GO; GO:0006182; P:cGMP biosynthetic process; ISO:RGD.
DR GO; GO:0019934; P:cGMP-mediated signaling; IMP:RGD.
DR GO; GO:0042417; P:dopamine metabolic process; IMP:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:RGD.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IMP:RGD.
DR GO; GO:0010753; P:positive regulation of cGMP-mediated signaling; IDA:RGD.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IDA:ComplexPortal.
DR GO; GO:0008217; P:regulation of blood pressure; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd07302; CHD; 1.
DR Gene3D; 3.30.70.1230; -; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR001170; ANPR/GUC.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00255; NATPEPTIDER.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
DR SUPFAM; SSF55073; SSF55073; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00458; ANF_RECEPTORS; 1.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; cGMP biosynthesis; Chloride; Disulfide bond; Glycoprotein;
KW GTP-binding; Lyase; Membrane; Nucleotide-binding; Phosphoprotein; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Vasoactive.
FT SIGNAL 1..28
FT CHAIN 29..1057
FT /note="Atrial natriuretic peptide receptor 1"
FT /id="PRO_0000012362"
FT TOPO_DOM 29..469
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..1057
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 524..801
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 872..1002
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT BINDING 81
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000269|PubMed:10894551,
FT ECO:0000269|PubMed:15117952"
FT BINDING 113
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000269|PubMed:10894551,
FT ECO:0000269|PubMed:15117952"
FT BINDING 114
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000269|PubMed:10894551,
FT ECO:0000269|PubMed:15117952"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20977274"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20977274,
FT ECO:0000269|PubMed:9528788"
FT MOD_RES 528
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:20977274,
FT ECO:0000269|PubMed:9528788"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20977274,
FT ECO:0000269|PubMed:9528788"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20977274,
FT ECO:0000269|PubMed:9528788"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20977274,
FT ECO:0000269|PubMed:9528788"
FT MOD_RES 541
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:20977274,
FT ECO:0000269|PubMed:9528788"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10894551,
FT ECO:0000269|PubMed:15117952"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 88..114
FT /evidence="ECO:0000269|PubMed:15117952"
FT DISULFID 192..241
FT /evidence="ECO:0000269|PubMed:15117952"
FT DISULFID 451..460
FT /evidence="ECO:0000269|PubMed:15117952"
FT MUTAGEN 197
FT /note="E->K: Abolishes hormone binding."
FT /evidence="ECO:0000269|PubMed:10894551"
FT MUTAGEN 213
FT /note="H->D: Abolishes hormone binding."
FT /evidence="ECO:0000269|PubMed:10894551"
FT MUTAGEN 338
FT /note="E->H: Decreased ANP-dependent guanylate cyclase
FT activity; when associated with P-364."
FT /evidence="ECO:0000269|PubMed:1679239"
FT MUTAGEN 364
FT /note="L->P: Decreased ANP-dependent guanylate cyclase
FT activity; when associated with H-338."
FT /evidence="ECO:0000269|PubMed:1679239"
FT MUTAGEN 364
FT /note="Missing: Loss of ANP binding and ANP-dependent
FT guanylate cyclase activities."
FT /evidence="ECO:0000269|PubMed:1679239"
FT MUTAGEN 522
FT /note="S->A: No effect on phosphorylation, 15% loss of ANP-
FT dependent activity."
FT /evidence="ECO:0000269|PubMed:9528788"
FT MUTAGEN 525
FT /note="S->A: Reduced phosphorylation, 80% loss of ANP-
FT dependent activity."
FT /evidence="ECO:0000269|PubMed:9528788"
FT MUTAGEN 525
FT /note="S->E: No effect on ANP-dependent activity."
FT /evidence="ECO:0000269|PubMed:9528788"
FT MUTAGEN 528
FT /note="T->A: Reduced phosphorylation, 50% loss of ANP-
FT dependent activity."
FT /evidence="ECO:0000269|PubMed:9528788"
FT MUTAGEN 530
FT /note="S->A: Reduced phosphorylation, 50% loss of ANP-
FT dependent activity."
FT /evidence="ECO:0000269|PubMed:9528788"
FT MUTAGEN 534
FT /note="S->A: Reduced phosphorylation, 50% loss of ANP-
FT dependent activity."
FT /evidence="ECO:0000269|PubMed:9528788"
FT MUTAGEN 538
FT /note="S->A: Reduced phosphorylation, 60% loss of CNP-
FT dependent activity."
FT /evidence="ECO:0000269|PubMed:9528788"
FT MUTAGEN 541
FT /note="T->A: Markedly reduced phosphorylation, 50% loss of
FT CNP-dependent activity."
FT /evidence="ECO:0000269|PubMed:9528788"
FT MUTAGEN 542
FT /note="T->A: No effect on phosphorylation, 30% loss of ANP-
FT dependent activity."
FT /evidence="ECO:0000269|PubMed:9528788"
FT CONFLICT 366
FT /note="Q -> H (in Ref. 3; AAA41202)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="L -> P (in Ref. 3; AAA41202)"
FT /evidence="ECO:0000305"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:1DP4"
FT HELIX 48..63
FT /evidence="ECO:0007829|PDB:1DP4"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:7BRH"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:1DP4"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:1DP4"
FT HELIX 92..104
FT /evidence="ECO:0007829|PDB:1DP4"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:1DP4"
FT HELIX 115..128
FT /evidence="ECO:0007829|PDB:1DP4"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:1DP4"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:1DP4"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:1DP4"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:1DP4"
FT HELIX 158..172
FT /evidence="ECO:0007829|PDB:1DP4"
FT STRAND 176..183
FT /evidence="ECO:0007829|PDB:1DP4"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:1DP4"
FT HELIX 191..207
FT /evidence="ECO:0007829|PDB:1DP4"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:1DP4"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:1DP4"
FT HELIX 224..234
FT /evidence="ECO:0007829|PDB:1DP4"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:1DP4"
FT HELIX 244..256
FT /evidence="ECO:0007829|PDB:1DP4"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:1DP4"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:1DP4"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:7BRG"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:1DP4"
FT HELIX 295..301
FT /evidence="ECO:0007829|PDB:1DP4"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:1DP4"
FT STRAND 305..310
FT /evidence="ECO:0007829|PDB:1DP4"
FT HELIX 316..333
FT /evidence="ECO:0007829|PDB:1DP4"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:1DP4"
FT HELIX 344..365
FT /evidence="ECO:0007829|PDB:1DP4"
FT HELIX 373..378
FT /evidence="ECO:0007829|PDB:1DP4"
FT TURN 379..382
FT /evidence="ECO:0007829|PDB:1DP4"
FT STRAND 383..387
FT /evidence="ECO:0007829|PDB:1DP4"
FT STRAND 390..394
FT /evidence="ECO:0007829|PDB:1DP4"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:1DP4"
FT STRAND 404..409
FT /evidence="ECO:0007829|PDB:1DP4"
FT TURN 411..413
FT /evidence="ECO:0007829|PDB:1DP4"
FT STRAND 416..422
FT /evidence="ECO:0007829|PDB:1DP4"
FT TURN 424..426
FT /evidence="ECO:0007829|PDB:1DP4"
FT STRAND 429..432
FT /evidence="ECO:0007829|PDB:1DP4"
FT STRAND 440..443
FT /evidence="ECO:0007829|PDB:7BRI"
SQ SEQUENCE 1057 AA; 118951 MW; 9EA9AE685AC05816 CRC64;
MPGSRRVRPR LRALLLLPPL LLLRGGHASD LTVAVVLPLT NTSYPWSWAR VGPAVELALA
RVKARPDLLP GWTVRMVLGS SENAAGVCSD TAAPLAAVDL KWEHSPAVFL GPGCVYSAAP
VGRFTAHWRV PLLTAGAPAL GIGVKDEYAL TTRTGPSHVK LGDFVTALHR RLGWEHQALV
LYADRLGDDR PCFFIVEGLY MRVRERLNIT VNHQEFVEGD PDHYPKLLRA VRRKGRVIYI
CSSPDAFRNL MLLALNAGLT GEDYVFFHLD VFGQSLKSAQ GLVPQKPWER GDGQDRSARQ
AFQAAKIITY KEPDNPEYLE FLKQLKLLAD KKFNFTVEDG LKNIIPASFH DGLLLYVQAV
TETLAQGGTV TDGENITQRM WNRSFQGVTG YLKIDRNGDR DTDFSLWDMD PETGAFRVVL
NYNGTSQELM AVSEHKLYWP LGYPPPDVPK CGFDNEDPAC NQDHFSTLEV LALVGSLSLI
SFLIVSFFIY RKMQLEKELV SELWRVRWED LQPSSLERHL RSAGSRLTLS GRGSNYGSLL
TTEGQFQVFA KTAYYKGNLV AVKRVNRKRI ELTRKVLFEL KHMRDVQNEH LTRFVGACTD
PPNICILTEY CPRGSLQDIL ENESITLDWM FRYSLTNDIV KGMLFLHNGA ICSHGNLKSS
NCVVDGRFVL KITDYGLESF RDPEPEQGHT LFAKKLWTAP ELLRMASPPA RGSQAGDVYS
FGIILQEIAL RSGVFYVEGL DLSPKEIIER VTRGEQPPFR PSMDLQSHLE ELGQLMQRCW
AEDPQERPPF QQIRLALRKF NKENSSNILD NLLSRMEQYA NNLEELVEER TQAYLEEKRK
AEALLYQILP HSVAEQLKRG ETVQAEAFDS VTIYFSDIVG FTALSAESTP MQVVTLLNDL
YTCFDAVIDN FDVYKVETIG DAYMVVSGLP VRNGQLHARE VARMALALLD AVRSFRIRHR
PQEQLRLRIG IHTGPVCAGV VGLKMPRYCL FGDTVNTASR MESNGEALKI HLSSETKAVL
EEFDGFELEL RGDVEMKGKG KVRTYWLLGE RGCSTRG
