P2RX3_HUMAN
ID P2RX3_HUMAN Reviewed; 397 AA.
AC P56373; Q6DK37; Q9UQB6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=P2X purinoceptor 3;
DE Short=P2X3;
DE AltName: Full=ATP receptor;
DE AltName: Full=Purinergic receptor;
GN Name=P2RX3;
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=Heart;
RX PubMed=9016352; DOI=10.1124/mol.51.1.109;
RA Garcia-Guzman M., Soto F., Gomez-Hernandez J.M., Lund P.E., Stuhmer W.;
RT "Characterization of recombinant human P2X4 receptor reveals
RT pharmacological differences to the rat homologue.";
RL Mol. Pharmacol. 51:109-118(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-383.
RC TISSUE=Heart;
RA Funatsuki K., Tanaka R., Inagaki S., Kawamura Y., Hashimoto Y., Yukioka H.,
RA Okuda U., Katoh K.;
RT "Cloning of a cDNA for human P2X3 purinoceptor variant.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
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 [5] {ECO:0007744|PDB:5SVJ, ECO:0007744|PDB:5SVK, ECO:0007744|PDB:5SVL, ECO:0007744|PDB:5SVM, ECO:0007744|PDB:5SVP, ECO:0007744|PDB:5SVQ, ECO:0007744|PDB:5SVR, ECO:0007744|PDB:5SVS, ECO:0007744|PDB:5SVT}
RP X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF 6-364 IN COMPLEXES WITH ATP AND
RP ATP ANALOG, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT,
RP GLYCOSYLATION AT ASN-139; ASN-170; ASN-194 AND ASN-290, AND DISULFIDE
RP BONDS.
RX PubMed=27626375; DOI=10.1038/nature19367;
RA Mansoor S.E., Lu W., Oosterheert W., Shekhar M., Tajkhorshid E., Gouaux E.;
RT "X-ray structures define human P2X(3) receptor gating cycle and antagonist
RT action.";
RL Nature 538:66-71(2016).
CC -!- FUNCTION: Receptor for ATP that acts as a ligand-gated cation channel
CC (PubMed:27626375). Plays a role in sensory perception. Required for
CC normal perception of pain. Required for normal taste perception (By
CC similarity). {ECO:0000250|UniProtKB:Q3UR32,
CC ECO:0000269|PubMed:27626375}.
CC -!- SUBUNIT: Homotrimer (PubMed:27626375). Functional P2XRs are organized
CC as homomeric and heteromeric trimers (By similarity).
CC {ECO:0000250|UniProtKB:P49654, ECO:0000269|PubMed:27626375}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27626375};
CC Multi-pass membrane protein {ECO:0000269|PubMed:27626375}.
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";
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DR EMBL; Y07683; CAA68947.1; -; mRNA.
DR EMBL; AB016608; BAA76515.1; -; mRNA.
DR EMBL; AP000781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC074792; AAH74792.1; -; mRNA.
DR EMBL; BC074793; AAH74793.1; -; mRNA.
DR EMBL; BC109287; AAI09288.1; -; mRNA.
DR CCDS; CCDS7953.1; -.
DR RefSeq; NP_002550.2; NM_002559.3.
DR RefSeq; XP_011543371.1; XM_011545069.2.
DR RefSeq; XP_011543372.1; XM_011545070.2.
DR PDB; 5SVJ; X-ray; 2.98 A; A=6-364.
DR PDB; 5SVK; X-ray; 2.77 A; A/B=6-364.
DR PDB; 5SVL; X-ray; 2.90 A; A/B=6-364.
DR PDB; 5SVM; X-ray; 3.09 A; A/B=6-364.
DR PDB; 5SVP; X-ray; 3.30 A; A/B=6-364.
DR PDB; 5SVQ; X-ray; 3.25 A; A=6-364.
DR PDB; 5SVR; X-ray; 3.13 A; A=6-364.
DR PDB; 5SVS; X-ray; 4.03 A; A=6-364.
DR PDB; 5SVT; X-ray; 3.79 A; A=6-364.
DR PDB; 5YVE; X-ray; 3.40 A; A=6-364.
DR PDB; 6AH4; X-ray; 3.30 A; A/B/C=17-363.
DR PDB; 6AH5; X-ray; 3.82 A; A/B/C=17-363.
DR PDBsum; 5SVJ; -.
DR PDBsum; 5SVK; -.
DR PDBsum; 5SVL; -.
DR PDBsum; 5SVM; -.
DR PDBsum; 5SVP; -.
DR PDBsum; 5SVQ; -.
DR PDBsum; 5SVR; -.
DR PDBsum; 5SVS; -.
DR PDBsum; 5SVT; -.
DR PDBsum; 5YVE; -.
DR PDBsum; 6AH4; -.
DR PDBsum; 6AH5; -.
DR AlphaFoldDB; P56373; -.
DR SMR; P56373; -.
DR BioGRID; 111063; 1.
DR STRING; 9606.ENSP00000263314; -.
DR BindingDB; P56373; -.
DR ChEMBL; CHEMBL2998; -.
DR DrugBank; DB01069; Promethazine.
DR DrugCentral; P56373; -.
DR GuidetoPHARMACOLOGY; 480; -.
DR TCDB; 1.A.7.1.6; the atp-gated p2x receptor cation channel (p2x receptor) family.
DR GlyGen; P56373; 4 sites.
DR iPTMnet; P56373; -.
DR PhosphoSitePlus; P56373; -.
DR BioMuta; P2RX3; -.
DR DMDM; 259016295; -.
DR MassIVE; P56373; -.
DR PaxDb; P56373; -.
DR PeptideAtlas; P56373; -.
DR PRIDE; P56373; -.
DR Antibodypedia; 14096; 253 antibodies from 31 providers.
DR DNASU; 5024; -.
DR Ensembl; ENST00000263314.3; ENSP00000263314.2; ENSG00000109991.10.
DR GeneID; 5024; -.
DR KEGG; hsa:5024; -.
DR MANE-Select; ENST00000263314.3; ENSP00000263314.2; NM_002559.5; NP_002550.2.
DR UCSC; uc001nju.4; human.
DR CTD; 5024; -.
DR DisGeNET; 5024; -.
DR GeneCards; P2RX3; -.
DR HGNC; HGNC:8534; P2RX3.
DR HPA; ENSG00000109991; Tissue enhanced (heart muscle, liver, testis).
DR MIM; 600843; gene.
DR neXtProt; NX_P56373; -.
DR OpenTargets; ENSG00000109991; -.
DR PharmGKB; PA32863; -.
DR VEuPathDB; HostDB:ENSG00000109991; -.
DR eggNOG; ENOG502QUDE; Eukaryota.
DR GeneTree; ENSGT01020000230351; -.
DR HOGENOM; CLU_034469_8_0_1; -.
DR InParanoid; P56373; -.
DR OMA; CPAEIDD; -.
DR OrthoDB; 1128763at2759; -.
DR PhylomeDB; P56373; -.
DR TreeFam; TF328633; -.
DR PathwayCommons; P56373; -.
DR Reactome; R-HSA-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-HSA-418346; Platelet homeostasis.
DR BioGRID-ORCS; 5024; 17 hits in 1065 CRISPR screens.
DR ChiTaRS; P2RX3; human.
DR GeneWiki; P2RX3; -.
DR GenomeRNAi; 5024; -.
DR Pharos; P56373; Tchem.
DR PRO; PR:P56373; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P56373; protein.
DR Bgee; ENSG00000109991; Expressed in apex of heart and 58 other tissues.
DR ExpressionAtlas; P56373; baseline and differential.
DR Genevisible; P56373; HS.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0043195; C:terminal bouton; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0004931; F:extracellularly ATP-gated cation channel activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0001614; F:purinergic nucleotide receptor activity; IDA:UniProtKB.
DR GO; GO:0061368; P:behavioral response to formalin induced pain; IEA:Ensembl.
DR GO; GO:0071318; P:cellular response to ATP; IDA:UniProtKB.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0098662; P:inorganic cation transmembrane transport; IDA:UniProtKB.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IEA:Ensembl.
DR GO; GO:0019228; P:neuronal action potential; IEA:Ensembl.
DR GO; GO:0030432; P:peristalsis; IEA:Ensembl.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; NAS:BHF-UCL.
DR GO; GO:0050850; P:positive regulation of calcium-mediated signaling; NAS:BHF-UCL.
DR GO; GO:1904058; P:positive regulation of sensory perception of pain; IEA:Ensembl.
DR GO; GO:0070207; P:protein homotrimerization; IDA:UniProtKB.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IEA:Ensembl.
DR GO; GO:0009743; P:response to carbohydrate; IEA:Ensembl.
DR GO; GO:0009409; P:response to cold; IEA:Ensembl.
DR GO; GO:0009408; P:response to heat; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0050909; P:sensory perception of taste; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0014832; P:urinary bladder smooth muscle contraction; IEA:Ensembl.
DR Gene3D; 2.60.490.10; -; 1.
DR InterPro; IPR003046; P2X3_purnocptor.
DR InterPro; IPR027309; P2X_extracellular_dom_sf.
DR InterPro; IPR001429; P2X_purnocptor.
DR PANTHER; PTHR10125:SF8; PTHR10125:SF8; 1.
DR PIRSF; PIRSF005713; P2X_purinoceptor; 1.
DR PRINTS; PR01310; P2X3RECEPTOR.
DR PRINTS; PR01307; P2XRECEPTOR.
DR TIGRFAMs; TIGR00863; P2X; 1.
DR PROSITE; PS01212; P2X_RECEPTOR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW Nucleotide-binding; Receptor; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..397
FT /note="P2X purinoceptor 3"
FT /id="PRO_0000161551"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27626375"
FT TRANSMEM 21..43
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:27626375"
FT TOPO_DOM 44..322
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:27626375"
FT TRANSMEM 323..341
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:27626375"
FT TOPO_DOM 342..397
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27626375"
FT REGION 378..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 63..65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27626375,
FT ECO:0007744|PDB:5SVK, ECO:0007744|PDB:5SVL,
FT ECO:0007744|PDB:5SVM, ECO:0007744|PDB:5SVP"
FT BINDING 172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27626375,
FT ECO:0007744|PDB:5SVK, ECO:0007744|PDB:5SVL,
FT ECO:0007744|PDB:5SVM, ECO:0007744|PDB:5SVP"
FT BINDING 275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27626375,
FT ECO:0007744|PDB:5SVK, ECO:0007744|PDB:5SVL,
FT ECO:0007744|PDB:5SVM, ECO:0007744|PDB:5SVP"
FT BINDING 279..281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27626375,
FT ECO:0007744|PDB:5SVK, ECO:0007744|PDB:5SVL,
FT ECO:0007744|PDB:5SVM, ECO:0007744|PDB:5SVP"
FT BINDING 299
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27626375,
FT ECO:0007744|PDB:5SVK, ECO:0007744|PDB:5SVL,
FT ECO:0007744|PDB:5SVM, ECO:0007744|PDB:5SVP"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27626375,
FT ECO:0007744|PDB:5SVK"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27626375,
FT ECO:0007744|PDB:5SVJ, ECO:0007744|PDB:5SVK,
FT ECO:0007744|PDB:5SVL, ECO:0007744|PDB:5SVM,
FT ECO:0007744|PDB:5SVP, ECO:0007744|PDB:5SVQ,
FT ECO:0007744|PDB:5SVR, ECO:0007744|PDB:5SVS,
FT ECO:0007744|PDB:5SVT"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27626375,
FT ECO:0007744|PDB:5SVJ, ECO:0007744|PDB:5SVK,
FT ECO:0007744|PDB:5SVL, ECO:0007744|PDB:5SVM,
FT ECO:0007744|PDB:5SVP, ECO:0007744|PDB:5SVQ,
FT ECO:0007744|PDB:5SVS, ECO:0007744|PDB:5SVT"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27626375,
FT ECO:0007744|PDB:5SVJ, ECO:0007744|PDB:5SVK,
FT ECO:0007744|PDB:5SVL, ECO:0007744|PDB:5SVM,
FT ECO:0007744|PDB:5SVP, ECO:0007744|PDB:5SVQ,
FT ECO:0007744|PDB:5SVR, ECO:0007744|PDB:5SVS,
FT ECO:0007744|PDB:5SVT"
FT DISULFID 107..153
FT /evidence="ECO:0000269|PubMed:27626375,
FT ECO:0007744|PDB:5SVJ, ECO:0007744|PDB:5SVK,
FT ECO:0007744|PDB:5SVL, ECO:0007744|PDB:5SVM,
FT ECO:0007744|PDB:5SVP, ECO:0007744|PDB:5SVQ,
FT ECO:0007744|PDB:5SVR, ECO:0007744|PDB:5SVS,
FT ECO:0007744|PDB:5SVT"
FT DISULFID 116..137
FT /evidence="ECO:0000269|PubMed:27626375,
FT ECO:0007744|PDB:5SVJ, ECO:0007744|PDB:5SVK,
FT ECO:0007744|PDB:5SVL, ECO:0007744|PDB:5SVM,
FT ECO:0007744|PDB:5SVP, ECO:0007744|PDB:5SVQ,
FT ECO:0007744|PDB:5SVR, ECO:0007744|PDB:5SVS,
FT ECO:0007744|PDB:5SVT"
FT DISULFID 122..147
FT /evidence="ECO:0000269|PubMed:27626375,
FT ECO:0007744|PDB:5SVJ, ECO:0007744|PDB:5SVK,
FT ECO:0007744|PDB:5SVL, ECO:0007744|PDB:5SVM,
FT ECO:0007744|PDB:5SVP, ECO:0007744|PDB:5SVQ,
FT ECO:0007744|PDB:5SVR, ECO:0007744|PDB:5SVS,
FT ECO:0007744|PDB:5SVT"
FT DISULFID 203..213
FT /evidence="ECO:0000269|PubMed:27626375,
FT ECO:0007744|PDB:5SVJ, ECO:0007744|PDB:5SVK,
FT ECO:0007744|PDB:5SVL, ECO:0007744|PDB:5SVM,
FT ECO:0007744|PDB:5SVP, ECO:0007744|PDB:5SVQ,
FT ECO:0007744|PDB:5SVR, ECO:0007744|PDB:5SVS,
FT ECO:0007744|PDB:5SVT"
FT DISULFID 247..256
FT /evidence="ECO:0000269|PubMed:27626375,
FT ECO:0007744|PDB:5SVJ, ECO:0007744|PDB:5SVK,
FT ECO:0007744|PDB:5SVL, ECO:0007744|PDB:5SVM,
FT ECO:0007744|PDB:5SVP, ECO:0007744|PDB:5SVQ,
FT ECO:0007744|PDB:5SVR, ECO:0007744|PDB:5SVS,
FT ECO:0007744|PDB:5SVT"
FT VARIANT 383
FT /note="A -> V (in dbSNP:rs2276038)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_034674"
FT CONFLICT 126
FT /note="R -> P (in Ref. 1; CAA68947)"
FT /evidence="ECO:0000305"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:5SVL"
FT HELIX 21..40
FT /evidence="ECO:0007829|PDB:5SVK"
FT HELIX 41..45
FT /evidence="ECO:0007829|PDB:5SVK"
FT TURN 46..49
FT /evidence="ECO:0007829|PDB:5SVL"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:5SVK"
FT STRAND 57..65
FT /evidence="ECO:0007829|PDB:5SVK"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:5SVK"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:5SVK"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:5SVK"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:5SVK"
FT STRAND 88..108
FT /evidence="ECO:0007829|PDB:5SVK"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:5SVK"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:5SVK"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:5SVK"
FT STRAND 128..143
FT /evidence="ECO:0007829|PDB:5SVK"
FT STRAND 145..154
FT /evidence="ECO:0007829|PDB:5SVK"
FT HELIX 166..170
FT /evidence="ECO:0007829|PDB:5SVK"
FT STRAND 172..181
FT /evidence="ECO:0007829|PDB:5SVK"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:5SVK"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:5SVK"
FT TURN 193..195
FT /evidence="ECO:0007829|PDB:5SVJ"
FT HELIX 197..202
FT /evidence="ECO:0007829|PDB:5SVK"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:5SVK"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:5SVK"
FT HELIX 218..224
FT /evidence="ECO:0007829|PDB:5SVK"
FT HELIX 229..235
FT /evidence="ECO:0007829|PDB:5SVK"
FT STRAND 237..248
FT /evidence="ECO:0007829|PDB:5SVK"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:5SVK"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:5SVK"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:5SVK"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:6AH4"
FT STRAND 279..287
FT /evidence="ECO:0007829|PDB:5SVK"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:5SVK"
FT STRAND 293..316
FT /evidence="ECO:0007829|PDB:5SVK"
FT HELIX 318..332
FT /evidence="ECO:0007829|PDB:5SVK"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:5SVK"
FT HELIX 336..345
FT /evidence="ECO:0007829|PDB:5SVK"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:5SVK"
FT HELIX 350..357
FT /evidence="ECO:0007829|PDB:5SVK"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:6AH4"
SQ SEQUENCE 397 AA; 44289 MW; 3CB0081E65748EED CRC64;
MNCISDFFTY ETTKSVVVKS WTIGIINRVV QLLIISYFVG WVFLHEKAYQ VRDTAIESSV
VTKVKGSGLY ANRVMDVSDY VTPPQGTSVF VIITKMIVTE NQMQGFCPES EEKYRCVSDS
QCGPERLPGG GILTGRCVNY SSVLRTCEIQ GWCPTEVDTV ETPIMMEAEN FTIFIKNSIR
FPLFNFEKGN LLPNLTARDM KTCRFHPDKD PFCPILRVGD VVKFAGQDFA KLARTGGVLG
IKIGWVCDLD KAWDQCIPKY SFTRLDSVSE KSSVSPGYNF RFAKYYKMEN GSEYRTLLKA
FGIRFDVLVY GNAGKFNIIP TIISSVAAFT SVGVGTVLCD IILLNFLKGA DQYKAKKFEE
VNETTLKIAA LTNPVYPSDQ TTAEKQSTDS GAFSIGH
