P2XE_DICDI
ID P2XE_DICDI Reviewed; 388 AA.
AC Q54JH4;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=P2X receptor E;
DE Short=P2XE;
GN Name=p2xE; ORFNames=DDB_G0288061;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18486207; DOI=10.1016/j.ceca.2008.04.001;
RA Ludlow M.J., Traynor D., Fisher P.R., Ennion S.J.;
RT "Purinergic-mediated Ca2+ influx in Dictyostelium discoideum.";
RL Cell Calcium 44:567-579(2008).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19833731; DOI=10.1074/jbc.m109.045674;
RA Ludlow M.J., Durai L., Ennion S.J.;
RT "Functional characterization of intracellular Dictyostelium discoideum P2X
RT receptors.";
RL J. Biol. Chem. 284:35227-35239(2009).
CC -!- FUNCTION: P2X receptors are ATP-gated ion channels that play a role in
CC intracellular calcium signaling. Not required for the purinergic
CC response to extracellular nucleotides. Not essential for
CC osmoregulation. Inward currents evoked by intracellular ATP. ATP analog
CC beta, gamma-imido-ATP is a weak partial agonist of p2xE. Exclusively
CC selective for ATP over other nucleotides. Insensitive to copper and P2
CC receptor antagonists PPADS and suramin but strongly inhibited by sodium
CC ions. More permeable to ammonium than either sodium or potassium ions
CC and less permeable to choline. Permeable to calcium ions, but not
CC chloride. {ECO:0000269|PubMed:18486207, ECO:0000269|PubMed:19833731}.
CC -!- SUBCELLULAR LOCATION: Contractile vacuole membrane
CC {ECO:0000269|PubMed:19833731}. Note=Ligand binding domain within the
CC lumen of the vacuole.
CC -!- DISRUPTION PHENOTYPE: Response to extracellular ATP remains the same in
CC p2xE null strains. Null cells are still capable of osmoregulation and
CC do not show any noticeable differences in their sensitivity to
CC hypotonic conditions. Quintuple p2xA/p2xB/p2xC/p2xD/p2xE null cells
CC displayed slight delay in their osmoregulatory response, but are still
CC capable of regulating their cell volume in water. Extracellular
CC purinergic response to ATP persists in the quintuple null cells with no
CC alteration in the kinetics of the response, but the magnitude of the
CC response is lower. Responses to the calmodulin antagonist calmidazolium
CC are reduced and intracellular calcium signaling is disrupted in
CC quintuple null cells. The presence of copper prevented both wild type
CC and quintuple null cells from undergoing an osmoregulatory decrease in
CC cell volume. No obvious morphological phenotype was apparent in the
CC p2xE or quintuple p2x null strains. The quintuple p2x null strains grow
CC slightly slower than wild type in shaking axenic cultures.
CC {ECO:0000269|PubMed:18486207, ECO:0000269|PubMed:19833731}.
CC -!- SIMILARITY: Belongs to the P2X receptor family. {ECO:0000305}.
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DR EMBL; AAFI02000107; EAL63456.2; -; Genomic_DNA.
DR RefSeq; XP_636957.2; XM_631865.2.
DR AlphaFoldDB; Q54JH4; -.
DR STRING; 44689.DDB0238352; -.
DR PaxDb; Q54JH4; -.
DR EnsemblProtists; EAL63456; EAL63456; DDB_G0288061.
DR GeneID; 8626432; -.
DR KEGG; ddi:DDB_G0288061; -.
DR dictyBase; DDB_G0288061; p2xE.
DR eggNOG; ENOG502TBEY; Eukaryota.
DR HOGENOM; CLU_060033_0_0_1; -.
DR InParanoid; Q54JH4; -.
DR OMA; QGYCPEL; -.
DR PhylomeDB; Q54JH4; -.
DR Reactome; R-DDI-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-DDI-418346; Platelet homeostasis.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-844456; The NLRP3 inflammasome.
DR PRO; PR:Q54JH4; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0031164; C:contractile vacuolar membrane; IDA:dictyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IC:dictyBase.
DR GO; GO:0035381; F:ATP-gated ion channel activity; IDA:dictyBase.
DR GO; GO:0140417; F:ATP-sensitive calcium-release channel activity; IGI:dictyBase.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IGI:dictyBase.
DR GO; GO:0071476; P:cellular hypotonic response; IGI:dictyBase.
DR GO; GO:0006811; P:ion transport; IDA:dictyBase.
DR GO; GO:0050848; P:regulation of calcium-mediated signaling; IGI:dictyBase.
DR InterPro; IPR028484; P2X_receptor_E.
DR PANTHER; PTHR10125:SF25; PTHR10125:SF25; 1.
PE 3: Inferred from homology;
KW Ion channel; Ion transport; Ligand-gated ion channel; Membrane; Receptor;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..388
FT /note="P2X receptor E"
FT /id="PRO_0000390415"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..312
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 291..304
FT /note="Pore-forming motif"
FT /evidence="ECO:0000255"
FT REGION 349..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 388 AA; 43829 MW; 8EB448F9E0A4D256 CRC64;
MNFRNIDWDS LFSYSTIKIV RIRDKRLGIL HFAFLIGIIL YIIVGTIFLQ KKYLVLESPI
GSIRTSLMAP SVKPTDLPYC LKNGTDTSYD GYPNKPCQYW DEYLVLYPPS EESSMFITTR
CTQETQSTVN GCNLSEPTCV YNTTSSSDFY IANVENFTIL LDHTLSAPSL GIQYNGAQLN
GQLLDTDGNP MSLPPPNIVG VKGSPDIMSL QGVLTAAGVE SLDSQGLANK SRTIRDDGIL
ILCFITYSNT YTYNTGNYHY TYQFKLVQNT KYKIVEPVFT KDVEDRYIFD RHGVRIIFIQ
TGQLGQFDFQ TMLLTFVSGI GLVTAASLIV DIIATRIMPQ RSRYQELKFQ DSSINNTQKT
PTNDHTPLLK DNEDTINENS YQNNSYEK
