P2RY1_HUMAN
ID P2RY1_HUMAN Reviewed; 373 AA.
AC P47900;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=P2Y purinoceptor 1;
DE Short=P2Y1;
DE AltName: Full=ADP receptor {ECO:0000303|PubMed:9038354};
DE AltName: Full=Purinergic receptor;
GN Name=P2RY1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=8666290; DOI=10.1016/0378-1119(96)00027-3;
RA Leon C., Vial C., Cazenave J.-P., Gachet C.;
RT "Cloning and sequencing of a human cDNA encoding endothelial P2Y1
RT purinoceptor.";
RL Gene 171:295-297(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8579591; DOI=10.1006/bbrc.1996.0139;
RA Ayyanathan K., Tania W., Harbansjit S., Raghbir A.S., Barnard E.A.,
RA Kunapuli S.P.;
RT "Cloning and chromosomal localization of the human P2Y1 purinoceptor.";
RL Biochem. Biophys. Res. Commun. 218:783-788(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8630005; DOI=10.1006/bbrc.1996.0640;
RA Janssens R., Communi D., Pirotton S., Samson M., Parmentier M.,
RA Boeynaems J.-M.;
RT "Cloning and tissue distribution of the human P2Y1 receptor.";
RL Biochem. Biophys. Res. Commun. 221:588-593(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RA Leon C., Vial C., Weber J., Cazenave J.-P., Gacher C.;
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 95-373, FUNCTION, AND ACTIVITY REGULATION.
RC TISSUE=Platelet;
RX PubMed=9442040; DOI=10.1074/jbc.273.4.2030;
RA Jin J., Daniel J.L., Kunapuli S.P.;
RT "Molecular basis for ADP-induced platelet activation. II. The P2Y1 receptor
RT mediates ADP-induced intracellular calcium mobilization and shape change in
RT platelets.";
RL J. Biol. Chem. 273:2030-2034(1998).
RN [8]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=9038354; DOI=10.1016/s0014-5793(97)00022-7;
RA Leon C., Hechler B., Vial C., Leray C., Cazenave J.P., Gachet C.;
RT "The P2Y1 receptor is an ADP receptor antagonized by ATP and expressed in
RT platelets and megakaryoblastic cells.";
RL FEBS Lett. 403:26-30(1997).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [10] {ECO:0007744|PDB:4XNV, ECO:0007744|PDB:4XNW}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-247 AND 253-373 IN COMPLEXES
RP WITH ATP ANALOG MRS2500 AND SYNTHETIC ANTAGONIST BPTU, SUBCELLULAR
RP LOCATION, TOPOLOGY, DISULFIDE BONDS, AND MUTAGENESIS OF LEU-44; TYR-110;
RP TYR-203; THR-205; ASN-283 AND TYR-306.
RX PubMed=25822790; DOI=10.1038/nature14287;
RA Zhang D., Gao Z.G., Zhang K., Kiselev E., Crane S., Wang J., Paoletta S.,
RA Yi C., Ma L., Zhang W., Han G.W., Liu H., Cherezov V., Katritch V.,
RA Jiang H., Stevens R.C., Jacobson K.A., Zhao Q., Wu B.;
RT "Two disparate ligand-binding sites in the human P2Y1 receptor.";
RL Nature 520:317-321(2015).
CC -!- FUNCTION: Receptor for extracellular adenine nucleotides such as ADP
CC (PubMed:9442040, PubMed:9038354, PubMed:25822790). In platelets,
CC binding to ADP leads to mobilization of intracellular calcium ions via
CC activation of phospholipase C, a change in platelet shape, and
CC ultimately platelet aggregation (PubMed:9442040).
CC {ECO:0000269|PubMed:25822790, ECO:0000269|PubMed:9038354,
CC ECO:0000269|PubMed:9442040}.
CC -!- ACTIVITY REGULATION: ATP functions as antagonist and inhibits ADP-
CC induced mobilization of Ca(2+) (PubMed:9038354). The P2Y1 receptor-
CC specific antagonists A3P5PS, A3P5P and A2P5P inhibit downstream
CC signaling mediated by mobilization of Ca(2+) from intracellular stores,
CC and platelet shape changes in response to extracellular ADP
CC (PubMed:9442040). {ECO:0000269|PubMed:9038354,
CC ECO:0000269|PubMed:9442040}.
CC -!- INTERACTION:
CC P47900; O14745: SLC9A3R1; NbExp=2; IntAct=EBI-8677223, EBI-349787;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25822790};
CC Multi-pass membrane protein {ECO:0000269|PubMed:25822790}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; Z49205; CAA89066.1; -; mRNA.
DR EMBL; U42030; AAA97873.1; -; mRNA.
DR EMBL; U42029; AAA97872.1; -; mRNA.
DR EMBL; S81950; AAB47091.1; -; Genomic_DNA.
DR EMBL; AJ006945; CAA07339.1; -; Genomic_DNA.
DR EMBL; AY136752; AAN01278.1; -; mRNA.
DR EMBL; BC074784; AAH74784.1; -; mRNA.
DR EMBL; BC074785; AAH74785.1; -; mRNA.
DR EMBL; AF018284; AAB94556.1; -; mRNA.
DR CCDS; CCDS3169.1; -.
DR PIR; JC4737; JC4737.
DR RefSeq; NP_002554.1; NM_002563.4.
DR PDB; 4XNV; X-ray; 2.20 A; A=2-247, A=253-373.
DR PDB; 4XNW; X-ray; 2.70 A; A/C=2-247, A/C=253-373.
DR PDBsum; 4XNV; -.
DR PDBsum; 4XNW; -.
DR AlphaFoldDB; P47900; -.
DR SMR; P47900; -.
DR BioGRID; 111067; 51.
DR IntAct; P47900; 8.
DR MINT; P47900; -.
DR STRING; 9606.ENSP00000304767; -.
DR BindingDB; P47900; -.
DR ChEMBL; CHEMBL4315; -.
DR DrugBank; DB01069; Promethazine.
DR DrugCentral; P47900; -.
DR GuidetoPHARMACOLOGY; 323; -.
DR TCDB; 9.A.14.13.22; the g-protein-coupled receptor (gpcr) family.
DR GlyGen; P47900; 4 sites.
DR iPTMnet; P47900; -.
DR PhosphoSitePlus; P47900; -.
DR BioMuta; P2RY1; -.
DR DMDM; 1352692; -.
DR MassIVE; P47900; -.
DR PaxDb; P47900; -.
DR PeptideAtlas; P47900; -.
DR PRIDE; P47900; -.
DR ProteomicsDB; 55818; -.
DR TopDownProteomics; P47900; -.
DR Antibodypedia; 2952; 400 antibodies from 36 providers.
DR DNASU; 5028; -.
DR Ensembl; ENST00000305097.6; ENSP00000304767.3; ENSG00000169860.7.
DR GeneID; 5028; -.
DR KEGG; hsa:5028; -.
DR MANE-Select; ENST00000305097.6; ENSP00000304767.3; NM_002563.5; NP_002554.1.
DR UCSC; uc003ezq.4; human.
DR CTD; 5028; -.
DR DisGeNET; 5028; -.
DR GeneCards; P2RY1; -.
DR HGNC; HGNC:8539; P2RY1.
DR HPA; ENSG00000169860; Tissue enhanced (placenta).
DR MIM; 601167; gene.
DR neXtProt; NX_P47900; -.
DR OpenTargets; ENSG00000169860; -.
DR PharmGKB; PA32868; -.
DR VEuPathDB; HostDB:ENSG00000169860; -.
DR eggNOG; ENOG502QWPV; Eukaryota.
DR GeneTree; ENSGT01030000234621; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; P47900; -.
DR OMA; FHVMKTL; -.
DR OrthoDB; 730191at2759; -.
DR PhylomeDB; P47900; -.
DR TreeFam; TF350009; -.
DR PathwayCommons; P47900; -.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR Reactome; R-HSA-417957; P2Y receptors.
DR Reactome; R-HSA-418592; ADP signalling through P2Y purinoceptor 1.
DR SignaLink; P47900; -.
DR SIGNOR; P47900; -.
DR BioGRID-ORCS; 5028; 9 hits in 1074 CRISPR screens.
DR ChiTaRS; P2RY1; human.
DR GeneWiki; P2RY1; -.
DR GenomeRNAi; 5028; -.
DR Pharos; P47900; Tchem.
DR PRO; PR:P47900; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P47900; protein.
DR Bgee; ENSG00000169860; Expressed in gingival epithelium and 158 other tissues.
DR Genevisible; P47900; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0044297; C:cell body; ISS:BHF-UCL.
DR GO; GO:0009986; C:cell surface; HDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0030425; C:dendrite; ISS:BHF-UCL.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
DR GO; GO:0014069; C:postsynaptic density; ISS:BHF-UCL.
DR GO; GO:0045211; C:postsynaptic membrane; ISS:BHF-UCL.
DR GO; GO:0031686; F:A1 adenosine receptor binding; IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IMP:UniProtKB.
DR GO; GO:0001621; F:G protein-coupled ADP receptor activity; IMP:UniProtKB.
DR GO; GO:0045031; F:G protein-coupled ATP receptor activity; ISS:BHF-UCL.
DR GO; GO:0045028; F:G protein-coupled purinergic nucleotide receptor activity; ISS:BHF-UCL.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0097110; F:scaffold protein binding; ISS:BHF-UCL.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0097746; P:blood vessel diameter maintenance; IEA:Ensembl.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0071318; P:cellular response to ATP; TAS:ARUK-UCL.
DR GO; GO:0071415; P:cellular response to purine-containing compound; IMP:UniProtKB.
DR GO; GO:0042755; P:eating behavior; IEA:Ensembl.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0001973; P:G protein-coupled adenosine receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0008347; P:glial cell migration; IEA:Ensembl.
DR GO; GO:0006811; P:ion transport; IEA:Ensembl.
DR GO; GO:0051100; P:negative regulation of binding; IEA:Ensembl.
DR GO; GO:0010700; P:negative regulation of norepinephrine secretion; IEA:Ensembl.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0030168; P:platelet activation; IEA:InterPro.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:BHF-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:BHF-UCL.
DR GO; GO:0046887; P:positive regulation of hormone secretion; IEA:Ensembl.
DR GO; GO:0032962; P:positive regulation of inositol trisphosphate biosynthetic process; IEA:Ensembl.
DR GO; GO:0043270; P:positive regulation of ion transport; IEA:Ensembl.
DR GO; GO:0060406; P:positive regulation of penile erection; IEA:Ensembl.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:BHF-UCL.
DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
DR GO; GO:0099509; P:regulation of presynaptic cytosolic calcium ion concentration; IEA:Ensembl.
DR GO; GO:0010469; P:regulation of signaling receptor activity; IEA:Ensembl.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR GO; GO:0090075; P:relaxation of muscle; IEA:InterPro.
DR GO; GO:0070848; P:response to growth factor; IEA:Ensembl.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
DR GO; GO:0023019; P:signal transduction involved in regulation of gene expression; ISS:BHF-UCL.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000142; P2Y1_rcpt.
DR PANTHER; PTHR24231:SF2; PTHR24231:SF2; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00595; P2Y1PRNOCPTR.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Blood coagulation; Cell membrane;
KW Disulfide bond; G-protein coupled receptor; Glycoprotein; Hemostasis;
KW Membrane; Nucleotide-binding; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..373
FT /note="P2Y purinoceptor 1"
FT /id="PRO_0000070006"
FT TOPO_DOM 1..51
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:25822790"
FT TRANSMEM 52..74
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:25822790"
FT TOPO_DOM 75..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25822790"
FT TRANSMEM 88..109
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:25822790"
FT TOPO_DOM 110..125
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:25822790"
FT TRANSMEM 126..147
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:25822790"
FT TOPO_DOM 148..166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25822790"
FT TRANSMEM 167..188
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:25822790"
FT TOPO_DOM 189..214
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:25822790"
FT TRANSMEM 215..237
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:25822790"
FT TOPO_DOM 238..260
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25822790"
FT TRANSMEM 261..284
FT /note="Helical; Name=6"
FT /evidence="ECO:0000269|PubMed:25822790"
FT TOPO_DOM 285..303
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:25822790"
FT TRANSMEM 304..325
FT /note="Helical; Name=7"
FT /evidence="ECO:0000269|PubMed:25822790"
FT TOPO_DOM 326..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25822790"
FT BINDING 46
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000305|PubMed:25822790,
FT ECO:0007744|PDB:4XNW"
FT BINDING 203..205
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000305|PubMed:25822790,
FT ECO:0007744|PDB:4XNW"
FT BINDING 283..287
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000305|PubMed:25822790,
FT ECO:0007744|PDB:4XNW"
FT BINDING 303..306
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000305|PubMed:25822790,
FT ECO:0007744|PDB:4XNW"
FT BINDING 310
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000305|PubMed:25822790,
FT ECO:0007744|PDB:4XNW"
FT CARBOHYD 11
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..296
FT /evidence="ECO:0000269|PubMed:25822790,
FT ECO:0007744|PDB:4XNV, ECO:0007744|PDB:4XNW"
FT DISULFID 124..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521,
FT ECO:0000269|PubMed:25822790, ECO:0007744|PDB:4XNV,
FT ECO:0007744|PDB:4XNW"
FT MUTAGEN 44
FT /note="L->A: Loss of ADP analog binding."
FT /evidence="ECO:0000269|PubMed:25822790"
FT MUTAGEN 110
FT /note="Y->F: Loss of ADP analog binding."
FT /evidence="ECO:0000269|PubMed:25822790"
FT MUTAGEN 203
FT /note="Y->A: Loss of ADP analog binding."
FT /evidence="ECO:0000269|PubMed:25822790"
FT MUTAGEN 205
FT /note="T->A: Loss of ADP analog binding."
FT /evidence="ECO:0000269|PubMed:25822790"
FT MUTAGEN 283
FT /note="N->A: Loss of ADP analog binding."
FT /evidence="ECO:0000269|PubMed:25822790"
FT MUTAGEN 306
FT /note="Y->F: Strongly decreased affinity for ADP analog."
FT /evidence="ECO:0000269|PubMed:25822790"
FT CONFLICT 138
FT /note="Missing (in Ref. 1; CAA89066)"
FT /evidence="ECO:0000305"
FT HELIX 50..78
FT /evidence="ECO:0007829|PDB:4XNV"
FT HELIX 85..112
FT /evidence="ECO:0007829|PDB:4XNV"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:4XNV"
FT HELIX 121..154
FT /evidence="ECO:0007829|PDB:4XNV"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:4XNW"
FT HELIX 161..183
FT /evidence="ECO:0007829|PDB:4XNV"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:4XNV"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:4XNV"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:4XNV"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:4XNV"
FT HELIX 211..225
FT /evidence="ECO:0007829|PDB:4XNV"
FT HELIX 227..245
FT /evidence="ECO:0007829|PDB:4XNV"
FT HELIX 253..271
FT /evidence="ECO:0007829|PDB:4XNV"
FT HELIX 273..289
FT /evidence="ECO:0007829|PDB:4XNV"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:4XNV"
FT HELIX 296..319
FT /evidence="ECO:0007829|PDB:4XNV"
FT HELIX 321..326
FT /evidence="ECO:0007829|PDB:4XNV"
SQ SEQUENCE 373 AA; 42072 MW; 4DC7C668B4145392 CRC64;
MTEVLWPAVP NGTDAAFLAG PGSSWGNSTV ASTAAVSSSF KCALTKTGFQ FYYLPAVYIL
VFIIGFLGNS VAIWMFVFHM KPWSGISVYM FNLALADFLY VLTLPALIFY YFNKTDWIFG
DAMCKLQRFI FHVNLYGSIL FLTCISAHRY SGVVYPLKSL GRLKKKNAIC ISVLVWLIVV
VAISPILFYS GTGVRKNKTI TCYDTTSDEY LRSYFIYSMC TTVAMFCVPL VLILGCYGLI
VRALIYKDLD NSPLRRKSIY LVIIVLTVFA VSYIPFHVMK TMNLRARLDF QTPAMCAFND
RVYATYQVTR GLASLNSCVD PILYFLAGDT FRRRLSRATR KASRRSEANL QSKSEDMTLN
ILPEFKQNGD TSL
