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   27-MAR-2024, entry version 202.
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: NHERF1; 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   PDB; 7XXH; EM; 2.90 A; R=2-373.
DR   PDBsum; 4XNV; -.
DR   PDBsum; 4XNW; -.
DR   PDBsum; 7XXH; -.
DR   AlphaFoldDB; P47900; -.
DR   EMDB; EMD-33503; -.
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   GlyCosmos; P47900; 4 sites, No reported glycans.
DR   GlyGen; P47900; 4 sites.
DR   iPTMnet; P47900; -.
DR   PhosphoSitePlus; P47900; -.
DR   BioMuta; P2RY1; -.
DR   DMDM; 1352692; -.
DR   MassIVE; P47900; -.
DR   PaxDb; 9606-ENSP00000304767; -.
DR   PeptideAtlas; P47900; -.
DR   ProteomicsDB; 55818; -.
DR   TopDownProteomics; P47900; -.
DR   Antibodypedia; 2952; 453 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   AGR; HGNC:8539; -.
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; GFCVPFI; -.
DR   OrthoDB; 5347340at2759; -.
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 1145 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 160 other cell types or tissues.
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:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0014069; C:postsynaptic density; ISS:BHF-UCL.
DR   GO; GO:0045211; C:postsynaptic membrane; ISS:BHF-UCL.
DR   GO; GO:0048787; C:presynaptic active zone membrane; IEA:Ensembl.
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; TAS:ProtInc.
DR   GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; 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:monoatomic ion transport; 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 monoatomic 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: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:0023019; P:signal transduction involved in regulation of gene expression; ISS:BHF-UCL.
DR   CDD; cd15377; 7tmA_P2Y1; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR000142; P2Y1_rcpt.
DR   PANTHER; PTHR24231:SF2; P2Y PURINOCEPTOR 1; 1.
DR   PANTHER; PTHR24231; PURINOCEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00595; P2Y1PRNOCPTR.
DR   PRINTS; PR01157; P2YPURNOCPTR.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   Genevisible; P47900; HS.
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"
FT   STRAND          329..331
FT                   /evidence="ECO:0007829|PDB:7XXH"
FT   HELIX           332..339
FT                   /evidence="ECO:0007829|PDB:7XXH"
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
//