ID P2RX1_HUMAN Reviewed; 399 AA. AC P51575; Q9UK84; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 02-SEP-2026, entry version 208. DE RecName: Full=P2X purinoceptor 1; DE Short=P2X1; DE AltName: Full=ATP receptor; DE AltName: Full=Purinergic receptor; GN Name=P2RX1; Synonyms=P2X1; 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], FUNCTION, ACTIVITY REGULATION, AND TISSUE RP SPECIFICITY. RC TISSUE=Urinary bladder smooth muscle; RX PubMed=8834001; RA Valera S., Talabot F., Evans R.J., Gos A., Antonarakis S.E., Morris M.A., RA Buell G.N.; RT "Characterization and chromosomal localization of a human P2X receptor from RT the urinary bladder."; RL Recept. Channels 3:283-289(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Urinary bladder; RX PubMed=8809107; DOI=10.1016/0167-4781(96)00112-1; RA Longhurst P.A., Schwegel T., Folander K., Swanson R.; RT "The human P2x1 receptor: molecular cloning, tissue distribution, and RT localization to chromosome 17."; RL Biochim. Biophys. Acta 1308:185-188(1996). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Platelet; RX PubMed=9565569; DOI=10.1074/jbc.273.19.11544; RA Sun B., Li J., Okahara K., Kambayashi J.; RT "P2X1 purinoceptor in human platelets. Molecular cloning and functional RT characterization after heterologous expression."; RL J. Biol. Chem. 273:11544-11547(1998). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Blood; 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8. RC TISSUE=Placenta; RA Dhulipala P.D., Kotlikoff M.I.; RT "Regulation of human P2X1 promoter by bHLH factors in smooth muscle RT cells."; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. RN [7] RP FUNCTION, AND TRANSPORTER ACTIVITY. RX PubMed=8961184; DOI=10.1113/jphysiol.1996.sp021777; RA Evans R.J., Lewis C., Virginio C., Lundstrom K., Buell G., Surprenant A., RA North R.A.; RT "Ionic permeability of, and divalent cation effects on, two ATP-gated RT cation channels (P2X receptors) expressed in mammalian cells."; RL J. Physiol. (Lond.) 497:413-422(1996). RN [8] RP FUNCTION, TRANSPORTER ACTIVITY, AND ACTIVITY REGULATION. RX PubMed=10440098; DOI=10.1016/s0014-2999(99)00350-7; RA Bianchi B.R., Lynch K.J., Touma E., Niforatos W., Burgard E.C., RA Alexander K.M., Park H.S., Yu H., Metzger R., Kowaluk E., Jarvis M.F., RA van Biesen T.; RT "Pharmacological characterization of recombinant human and rat P2X receptor RT subtypes."; RL Eur. J. Pharmacol. 376:127-138(1999). RN [9] RP DISULFIDE BONDS, AND SUBCELLULAR LOCATION. RX PubMed=11809854; DOI=10.1124/mol.61.2.303; RA Ennion S.J., Evans R.J.; RT "Conserved cysteine residues in the extracellular loop of the human P2X(1) RT receptor form disulfide bonds and are involved in receptor trafficking to RT the cell surface."; RL Mol. Pharmacol. 61:303-311(2002). RN [10] RP FUNCTION. RX PubMed=14699168; DOI=10.1074/jbc.m308964200; RA Roberts J.A., Evans R.J.; RT "ATP binding at human P2X1 receptors. Contribution of aromatic and basic RT amino acids revealed using mutagenesis and partial agonists."; RL J. Biol. Chem. 279:9043-9055(2004). RN [11] RP FUNCTION, AND TRANSPORTER ACTIVITY. RX PubMed=15056721; DOI=10.1523/jneurosci.5429-03.2004; RA Egan T.M., Khakh B.S.; RT "Contribution of calcium ions to P2X channel responses."; RL J. Neurosci. 24:3413-3420(2004). RN [12] RP FUNCTION, ACTIVITY REGULATION, AND TISSUE SPECIFICITY. RX PubMed=19635923; DOI=10.4049/jimmunol.0804007; RA Lecut C., Frederix K., Johnson D.M., Deroanne C., Thiry M., Faccinetto C., RA Maree R., Evans R.J., Volders P.G., Bours V., Oury C.; RT "P2X1 ion channels promote neutrophil chemotaxis through Rho kinase RT activation."; RL J. Immunol. 183:2801-2809(2009). RN [13] RP FUNCTION, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION. RX PubMed=20699225; DOI=10.1074/jbc.m110.148940; RA Allsopp R.C., Lalo U., Evans R.J.; RT "Lipid raft association and cholesterol sensitivity of P2X1-4 receptors for RT ATP: chimeras and point mutants identify intracellular amino-terminal RT residues involved in lipid regulation of P2X1 receptors."; RL J. Biol. Chem. 285:32770-32777(2010). RN [14] RP PHOSPHORYLATION AT SER-387; SER-388 AND THR-389. RX PubMed=22971236; DOI=10.1111/jnc.12012; RA Roberts J.A., Bottrill A.R., Mistry S., Evans R.J.; RT "Mass spectrometry analysis of human P2X1 receptors; insight into RT phosphorylation, modelling and conformational changes."; RL J. Neurochem. 123:725-735(2012). RN [15] RP VARIANT LEU-351 DEL, CHARACTERIZATION OF VARIANT LEU-351 DEL, AND RP SUBCELLULAR LOCATION. RX PubMed=10816552; DOI=10.1074/jbc.c000305200; RA Oury C., Toth-Zsamboki E., Van Geet C., Thys C., Wei L., Nilius B., RA Vermylen J., Hoylaerts M.F.; RT "A natural dominant negative P2X1 receptor due to deletion of a single RT amino acid residue."; RL J. Biol. Chem. 275:22611-22614(2000). CC -!- FUNCTION: ATP-gated nonselective transmembrane cation channel permeable CC to potassium, sodium and with relatively high calcium permeability CC (PubMed:10440098, PubMed:15056721, PubMed:20699225, PubMed:8834001, CC PubMed:8961184). Furthermore, CTP functions as a weak affinity agonist CC for P2RX1 (PubMed:14699168). Plays a role a role in urogenital, immune CC and cardiovascular function (By similarity). Specifically, plays an CC important role in neurogenic contraction of smooth muscle of the vas CC deferens, and therefore is essential for normal male reproductive CC function (By similarity). In addition, contributes to smooth muscle CC contractions of the urinary bladder (By similarity). On platelets, CC contributes to platelet activation and aggregation and thereby, also to CC thrombosis (By similarity). On neutrophils, it is involved in CC chemotaxis and in mitigating the activation of circulating cells CC (PubMed:19635923). {ECO:0000250|UniProtKB:P51576, CC ECO:0000269|PubMed:10440098, ECO:0000269|PubMed:14699168, CC ECO:0000269|PubMed:15056721, ECO:0000269|PubMed:19635923, CC ECO:0000269|PubMed:20699225, ECO:0000269|PubMed:8834001, CC ECO:0000269|PubMed:8961184}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, CC ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:10440098, CC ECO:0000269|PubMed:15056721, ECO:0000269|PubMed:8961184}; CC -!- CATALYTIC ACTIVITY: CC Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; CC Evidence={ECO:0000269|PubMed:8961184}; CC -!- CATALYTIC ACTIVITY: CC Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, CC ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:8961184}; CC -!- ACTIVITY REGULATION: Activated by low concentrations of ATP (<1 uM) CC (PubMed:10440098, PubMed:8834001). Undergoes rapid desensitization CC (PubMed:10440098). Sensitive to the ATP agonist:alpha/beta-methylene- CC ATP (PubMed:19635923, PubMed:8834001). Modulated by cholesterol CC (PubMed:20699225). {ECO:0000269|PubMed:10440098, CC ECO:0000269|PubMed:19635923, ECO:0000269|PubMed:20699225, CC ECO:0000269|PubMed:8834001}. CC -!- SUBUNIT: Functional P2XRs are organized as homomeric and heteromeric CC trimers. Forms heterodimer with P2RX2. Forms heterodimer with P2RX4. CC Forms heterodimer with P2RX5. {ECO:0000250|UniProtKB:P47824}. CC -!- INTERACTION: CC P51575; Q9BQA9: CYBC1; NbExp=5; IntAct=EBI-11599725, EBI-2680384; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10816552, CC ECO:0000269|PubMed:11809854}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:P56373}. Note=Detected at plasma membrane lipid CC rafts. {ECO:0000269|PubMed:20699225}. CC -!- TISSUE SPECIFICITY: Expressed on neutrophils and platelets CC (PubMed:19635923). Expressed on urinary bladder smooth muscle CC (PubMed:8834001). {ECO:0000269|PubMed:19635923, CC ECO:0000269|PubMed:8834001}. CC -!- DOMAIN: The N-terminal 20 to 23 and 27 to 29 residues seem to play a CC role in the cholesterol-dependent gating of this receptor. CC {ECO:0000269|PubMed:20699225}. CC -!- SIMILARITY: Belongs to the P2X receptor family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=P2X receptor entry; CC URL="https://en.wikipedia.org/wiki/P2X_receptor"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=P2RX1 entry; CC URL="https://en.wikipedia.org/wiki/P2RX1"; 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; X83688; CAA58657.1; -; mRNA. DR EMBL; U45448; AAC50698.1; -; mRNA. DR EMBL; AF020498; AAC24494.1; -; mRNA. DR EMBL; AC005940; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC044657; AAH44657.1; -; mRNA. DR EMBL; AF177472; AAD55395.1; -; Genomic_DNA. DR CCDS; CCDS11040.1; -. DR PIR; S71927; S71927. DR RefSeq; NP_002549.1; NM_002558.4. DR PDB; 9B73; EM; 1.96 A; A/B/C=1-399. DR PDB; 9B95; EM; 2.61 A; A/B/C=1-399. DR PDB; 9C2A; EM; 2.74 A; A/B/C=1-399. DR PDB; 9C2B; EM; 2.42 A; A/B/C=1-399. DR PDB; 9C2C; EM; 2.90 A; A/B/C=1-399. DR PDB; 9LX5; EM; 3.60 A; A/B/C=28-357. DR PDB; 9LXC; EM; 3.10 A; A/B/C=29-354. DR AlphaFoldDB; P51575; -. DR EMDB; EMD-44299; -. DR EMDB; EMD-44370; -. DR EMDB; EMD-45152; -. DR EMDB; EMD-45153; -. DR EMDB; EMD-45154; -. DR EMDB; EMD-63466; -. DR EMDB; EMD-63473; -. DR SMR; P51575; -. DR BioGRID; 111062; 36. DR FunCoup; P51575; 648. DR IntAct; P51575; 24. DR NDEx; IQUERY-CP-P2RX1; 2 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000225538; -. DR BindingDB; P51575; -. DR ChEMBL; CHEMBL2094; -. DR DrugBank; DB01069; Promethazine. DR DrugCentral; P51575; -. DR GuidetoPHARMACOLOGY; 478; -. DR GlyCosmos; P51575; 4 sites, No reported glycans. DR GlyGen; P51575; 4 sites, 2 N-linked glycans (1 site). DR iPTMnet; P51575; -. DR PhosphoSitePlus; P51575; -. DR BioMuta; P2RX1; -. DR DMDM; 1709519; -. DR MassIVE; P51575; -. DR PaxDb; 9606-ENSP00000225538; -. DR PeptideAtlas; P51575; -. DR ProteomicsDB; 56337; -. DR Antibodypedia; 3473; 197 antibodies from 28 providers. DR DNASU; 5023; -. DR Ensembl; ENST00000225538.4; ENSP00000225538.3; ENSG00000108405.5. DR GeneID; 5023; -. DR KEGG; hsa:5023; -. DR MANE-Select; ENST00000225538.4; ENSP00000225538.3; NM_002558.4; NP_002549.1. DR UCSC; uc002fww.4; human. DR AGR; HGNC:8533; -. DR ClinPGx; PA32861; -. DR CTD; 5023; -. DR DisGeNET; 5023; -. DR GeneCards; P2RX1; -. DR HGNC; HGNC:8533; P2RX1. DR HPA; ENSG00000108405; Tissue enhanced (blood vessel, pancreas, urinary bladder). DR MalaCards; P2RX1; -. DR MIM; 600845; gene+phenotype. DR OpenTargets; ENSG00000108405; -. DR VEuPathDB; HostDB:ENSG00000108405; -. DR eggNOG; ENOG502QSUI; Eukaryota. DR GeneTree; ENSGT01020000230351; -. DR HOGENOM; CLU_034469_2_0_1; -. DR InParanoid; P51575; -. DR OMA; DCDLDWS; -. DR OrthoDB; 494673at2759; -. DR PAN-GO; P51575; 3 GO annotations based on evolutionary models. DR PhylomeDB; P51575; -. DR PathwayCommons; P51575; -. DR Reactome; R-HSA-139853; Elevation of cytosolic Ca2+ levels. DR Reactome; R-HSA-418346; Platelet homeostasis. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR SignaLink; P51575; -. DR Agora; ENSG00000108405; -. DR BioGRID-ORCS; 5023; 19 hits in 1160 CRISPR screens. DR ChiTaRS; P2RX1; human. DR GeneWiki; P2RX1; -. DR GenomeRNAi; 5023; -. DR Pharos; P51575; Tchem. DR PRO; PR:P51575; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P51575; protein. DR Bgee; ENSG00000108405; Expressed in popliteal artery and 110 other cell types or tissues. DR ExpressionAtlas; P51575; baseline and differential. DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl. DR GO; GO:0048787; C:presynaptic active zone membrane; IEA:Ensembl. DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl. DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome. DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome. DR GO; GO:0005524; F:ATP binding; IEA:Ensembl. DR GO; GO:0004931; F:extracellularly ATP-gated monoatomic cation channel activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl. DR GO; GO:0099604; F:ligand-gated calcium channel activity; IDA:UniProtKB. DR GO; GO:0005261; F:monoatomic cation channel activity; IDA:MGI. DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl. DR GO; GO:0001614; F:purinergic nucleotide receptor activity; IDA:MGI. DR GO; GO:0043924; F:suramin binding; IEA:Ensembl. DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central. DR GO; GO:0006811; P:monoatomic ion transport; IDA:MGI. DR GO; GO:0019228; P:neuronal action potential; IEA:Ensembl. DR GO; GO:1905665; P:positive regulation of calcium ion import across plasma membrane; IEA:Ensembl. DR GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl. 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:0033198; P:response to ATP; IEA:InterPro. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IEA:Ensembl. DR FunFam; 2.60.490.10:FF:000001; P2X purinoceptor; 1. DR Gene3D; 1.10.287.940; atp-gated p2x4 ion channel; 1. DR Gene3D; 2.60.490.10; atp-gated p2x4 ion channel domain; 1. DR InterPro; IPR003044; P2X1_purnocptor. DR InterPro; IPR027309; P2X_extracellular_dom_sf. DR InterPro; IPR001429; P2X_purnocptor. DR InterPro; IPR059116; P2X_receptor. DR InterPro; IPR053792; P2X_RECEPTOR_CS. DR NCBIfam; TIGR00863; P2X; 1. DR PANTHER; PTHR10125; P2X PURINOCEPTOR; 1. DR PANTHER; PTHR10125:SF9; P2X PURINOCEPTOR 1; 1. DR Pfam; PF00864; P2X_receptor; 1. DR PIRSF; PIRSF005713; P2X_purinoceptor; 1. DR PRINTS; PR01308; P2X1RECEPTOR. DR PRINTS; PR01307; P2XRECEPTOR. DR PROSITE; PS01212; P2X_RECEPTOR; 1. DR PDBsum; 9B73; -. DR PDBsum; 9B95; -. DR PDBsum; 9C2A; -. DR PDBsum; 9C2B; -. DR PDBsum; 9C2C; -. DR PDBsum; 9LX5; -. DR PDBsum; 9LXC; -. PE 1: Evidence at protein level; KW 3D-structure; Apoptosis; ATP-binding; Cell membrane; Disulfide bond; KW Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel; KW Membrane; Nucleotide-binding; Phosphoprotein; Proteomics identification; KW Receptor; Reference proteome; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1..399 FT /note="P2X purinoceptor 1" FT /id="PRO_0000161545" FT TOPO_DOM 1..28 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P56373" FT TRANSMEM 29..50 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 51..338 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:P56373" FT TRANSMEM 339..358 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 359..399 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P56373" FT REGION 331..338 FT /note="Pore-forming motif" FT /evidence="ECO:0000255" FT BINDING 68 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P56373" FT BINDING 68 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0000250|UniProtKB:F8W463" FT BINDING 70 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P56373" FT BINDING 70 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0000250|UniProtKB:F8W463" FT BINDING 140 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0000250|UniProtKB:F8W463" FT BINDING 186 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P56373" FT BINDING 186 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0000250|UniProtKB:F8W463" FT BINDING 286 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P56373" FT BINDING 290 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P56373" FT BINDING 290 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0000250|UniProtKB:F8W463" FT BINDING 292 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P56373" FT BINDING 292 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0000250|UniProtKB:F8W463" FT BINDING 309 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P56373" FT BINDING 309 FT /ligand="CTP" FT /ligand_id="ChEBI:CHEBI:37563" FT /evidence="ECO:0000250|UniProtKB:F8W463" FT MOD_RES 387 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:22971236" FT MOD_RES 388 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:22971236" FT MOD_RES 389 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:22971236" FT CARBOHYD 153 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 184 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 242 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 300 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 117..165 FT /evidence="ECO:0000269|PubMed:11809854" FT DISULFID 126..149 FT /evidence="ECO:0000269|PubMed:11809854" FT DISULFID 132..159 FT /evidence="ECO:0000269|PubMed:11809854" FT DISULFID 217..227 FT /evidence="ECO:0000269|PubMed:11809854" FT DISULFID 261..270 FT /evidence="ECO:0000269|PubMed:11809854" FT VARIANT 351 FT /note="Missing (in a patient presenting with severe FT bleeding; uncertain significance; somatic variant; results FT in a non-functional channel; dbSNP:rs587776702)" FT /evidence="ECO:0000269|PubMed:10816552" FT /id="VAR_025382" FT VARIANT 396 FT /note="M -> V (in dbSNP:rs34617528)" FT /id="VAR_053552" FT HELIX 32..42 FT /evidence="ECO:0007829|PDB:9B73" FT HELIX 43..51 FT /evidence="ECO:0007829|PDB:9B73" FT TURN 52..55 FT /evidence="ECO:0007829|PDB:9LXC" FT STRAND 56..60 FT /evidence="ECO:0007829|PDB:9B73" FT STRAND 62..70 FT /evidence="ECO:0007829|PDB:9B73" FT STRAND 73..75 FT /evidence="ECO:0007829|PDB:9B73" FT TURN 78..80 FT /evidence="ECO:0007829|PDB:9B95" FT STRAND 83..85 FT /evidence="ECO:0007829|PDB:9B73" FT HELIX 87..90 FT /evidence="ECO:0007829|PDB:9B73" FT STRAND 91..93 FT /evidence="ECO:0007829|PDB:9B73" FT STRAND 98..118 FT /evidence="ECO:0007829|PDB:9B73" FT HELIX 121..123 FT /evidence="ECO:0007829|PDB:9B73" FT STRAND 125..128 FT /evidence="ECO:0007829|PDB:9C2C" FT TURN 129..131 FT /evidence="ECO:0007829|PDB:9B73" FT STRAND 134..136 FT /evidence="ECO:0007829|PDB:9B73" FT STRAND 138..140 FT /evidence="ECO:0007829|PDB:9B73" FT STRAND 143..155 FT /evidence="ECO:0007829|PDB:9B73" FT STRAND 157..166 FT /evidence="ECO:0007829|PDB:9B73" FT HELIX 167..171 FT /evidence="ECO:0007829|PDB:9C2C" FT HELIX 180..184 FT /evidence="ECO:0007829|PDB:9B73" FT STRAND 186..195 FT /evidence="ECO:0007829|PDB:9B73" FT TURN 196..199 FT /evidence="ECO:0007829|PDB:9B73" FT STRAND 200..205 FT /evidence="ECO:0007829|PDB:9B73" FT HELIX 211..216 FT /evidence="ECO:0007829|PDB:9B73" FT STRAND 221..224 FT /evidence="ECO:0007829|PDB:9B73" FT STRAND 229..231 FT /evidence="ECO:0007829|PDB:9B73" FT HELIX 232..238 FT /evidence="ECO:0007829|PDB:9B73" FT HELIX 243..249 FT /evidence="ECO:0007829|PDB:9B73" FT STRAND 251..262 FT /evidence="ECO:0007829|PDB:9B73" FT HELIX 267..269 FT /evidence="ECO:0007829|PDB:9B73" FT STRAND 273..277 FT /evidence="ECO:0007829|PDB:9B73" FT STRAND 282..286 FT /evidence="ECO:0007829|PDB:9B73" FT STRAND 290..299 FT /evidence="ECO:0007829|PDB:9B73" FT STRAND 302..326 FT /evidence="ECO:0007829|PDB:9B73" FT HELIX 328..355 FT /evidence="ECO:0007829|PDB:9B73" SQ SEQUENCE 399 AA; 44980 MW; 8365466665522BF8 CRC64; MARRFQEELA AFLFEYDTPR MVLVRNKKVG VIFRLIQLVV LVYVIGWVFL YEKGYQTSSG LISSVSVKLK GLAVTQLPGL GPQVWDVADY VFPAQGDNSF VVMTNFIVTP KQTQGYCAEH PEGGICKEDS GCTPGKAKRK AQGIRTGKCV AFNDTVKTCE IFGWCPVEVD DDIPRPALLR EAENFTLFIK NSISFPRFKV NRRNLVEEVN AAHMKTCLFH KTLHPLCPVF QLGYVVQESG QNFSTLAEKG GVVGITIDWH CDLDWHVRHC RPIYEFHGLY EEKNLSPGFN FRFARHFVEN GTNYRHLFKV FGIRFDILVD GKAGKFDIIP TMTTIGSGIG IFGVATVLCD LLLLHILPKR HYYKQKKFKY AEDMGPGAAE RDLAATSSTL GLQENMRTS //