P2RX2_CAVPO
ID P2RX2_CAVPO Reviewed; 474 AA.
AC O70397; O70398; O70399;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=P2X purinoceptor 2;
DE Short=P2X2;
DE AltName: Full=ATP receptor;
DE AltName: Full=Purinergic receptor;
GN Name=P2RX2;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS P2X2-1; P2X2-2 AND P2X2-3).
RC STRAIN=NIH 2; TISSUE=Organ of Corti;
RX PubMed=9682808; DOI=10.1016/s0378-5955(98)00065-3;
RA Parker M.S., Larroque M.L., Campbell J.M., Bobbin R.P., Deininger P.L.;
RT "Novel variant of the P2X2 ATP receptor from the guinea pig organ of
RT Corti.";
RL Hear. Res. 121:62-70(1998).
CC -!- FUNCTION: Ion channel gated by extracellular ATP involved in a variety
CC of cellular responses, such as excitatory postsynaptic responses in
CC sensory neurons, neuromuscular junctions (NMJ) formation, hearing,
CC perception of taste and peristalsis. In the inner ear, regulates sound
CC transduction and auditory neurotransmission, outer hair cell
CC electromotility, inner ear gap junctions, and K(+) recycling. Mediates
CC synaptic transmission between neurons and from neurons to smooth muscle
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer and heterotrimer; functional P2XRs are organized as
CC homomeric and heteromeric trimers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=P2X2-1;
CC IsoId=O70397-1; Sequence=Displayed;
CC Name=P2X2-2;
CC IsoId=O70397-2; Sequence=VSP_004494;
CC Name=P2X2-3;
CC IsoId=O70397-3; Sequence=VSP_014134;
CC -!- SIMILARITY: Belongs to the P2X receptor family. {ECO:0000305}.
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; AF053327; AAC08992.1; -; mRNA.
DR EMBL; AF053328; AAC08993.1; -; mRNA.
DR EMBL; AF053329; AAC08994.1; -; mRNA.
DR RefSeq; NP_001166180.1; NM_001172709.1. [O70397-1]
DR AlphaFoldDB; O70397; -.
DR SMR; O70397; -.
DR STRING; 10141.ENSCPOP00000012286; -.
DR GeneID; 100135591; -.
DR KEGG; cpoc:100135591; -.
DR CTD; 22953; -.
DR eggNOG; ENOG502QVP9; Eukaryota.
DR InParanoid; O70397; -.
DR OrthoDB; 1128763at2759; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0004931; F:extracellularly ATP-gated cation channel activity; ISS:UniProtKB.
DR GO; GO:0001614; F:purinergic nucleotide receptor activity; IEA:InterPro.
DR GO; GO:0033198; P:response to ATP; IEA:InterPro.
DR GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
DR Gene3D; 2.60.490.10; -; 1.
DR InterPro; IPR003045; P2X2_purnocptor.
DR InterPro; IPR027309; P2X_extracellular_dom_sf.
DR InterPro; IPR001429; P2X_purnocptor.
DR PRINTS; PR01309; P2X2RECEPTOR.
DR PRINTS; PR01307; P2XRECEPTOR.
DR TIGRFAMs; TIGR00863; P2X; 1.
DR PROSITE; PS01212; P2X_RECEPTOR; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Ligand-gated ion channel; Membrane; Receptor;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..474
FT /note="P2X purinoceptor 2"
FT /id="PRO_0000161548"
FT TOPO_DOM 1..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..60
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..333
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 355..474
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 316..329
FT /note="Pore-forming motif"
FT /evidence="ECO:0000255"
FT REGION 445..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 121..172
FT /evidence="ECO:0000250"
FT DISULFID 132..155
FT /evidence="ECO:0000250"
FT DISULFID 138..166
FT /evidence="ECO:0000250"
FT DISULFID 222..232
FT /evidence="ECO:0000250"
FT DISULFID 266..275
FT /evidence="ECO:0000250"
FT VAR_SEQ 298
FT /note="R -> RYLPRVPSRGKMGQWALHSAGQRSLHPR (in isoform P2X2-
FT 3)"
FT /evidence="ECO:0000303|PubMed:9682808"
FT /id="VSP_014134"
FT VAR_SEQ 377..441
FT /note="VCAPSRPSSSWPVTLALILGQAPPPPRHCSSPWHLAHQAVGPQGAEQAKLLG
FT LQNPTPYRLSEQI -> I (in isoform P2X2-2)"
FT /evidence="ECO:0000303|PubMed:9682808"
FT /id="VSP_004494"
SQ SEQUENCE 474 AA; 52702 MW; F02495B340E3CF16 CRC64;
MAATHPKAPT AQRLRQGWSA FWDYETPKVI VVRNRPLGVV YRAVQLLILL YFVWYVFIVQ
KSYQDSETGP ESSIITKVKG ITQSEHKVWD VEEYVKPPEG GSVFSIITRI EVTPFQTLGA
CPESIRVPNT TCHLDADCTA GELDMLGNGL RTGRCVPYYH GEAKTCEVSG WCPVEDGAAV
SHFLGKMAPN FTILIKNSIH YPKFQFSKGN IAHRDMTYLR RCTFDQGFDP YCPIFRLGFI
VEQAGENFTE LAHRGGVIGV IINWDCDLDL PSSHCNPKYS FRRLDPKHVP ASSGYNFRFA
KYYRVNSTTT RTLIKAYGIR IDVIVHGQAG KFSLIPTIIN LATALTSIGV GSFLCDWILL
TFMNKNKVYS HKKFDKVCAP SRPSSSWPVT LALILGQAPP PPRHCSSPWH LAHQAVGPQG
AEQAKLLGLQ NPTPYRLSEQ IADTPDRCVG QGLPSSESPL QDSTPTDPKG LAQL
