GenomeNet

Database: UniProt
Entry: F1RNN5_PIG
LinkDB: F1RNN5_PIG
Original site: F1RNN5_PIG 
ID   F1RNN5_PIG              Unreviewed;       595 AA.
AC   F1RNN5; A0A4X1U1B8;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 2.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=P2X purinoceptor {ECO:0000256|RuleBase:RU000681};
GN   Name=P2RX7 {ECO:0000313|Ensembl:ENSSSCP00000010480.2,
GN   ECO:0000313|VGNC:VGNC:111758};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000010480.2, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000010480.2, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000010480.2,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:HDA47020.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30723633; DOI=.7717/peerj.6374;
RA   Gilbert D.G.;
RT   "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL   PeerJ 7:E6374-E6374(2019).
RN   [3] {ECO:0000313|Ensembl:ENSSSCP00000010480.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Receptor for ATP that acts as a ligand-gated ion channel.
CC       {ECO:0000256|RuleBase:RU000681}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU000681}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU000681}.
CC   -!- SIMILARITY: Belongs to the P2X receptor family.
CC       {ECO:0000256|ARBA:ARBA00009848, ECO:0000256|RuleBase:RU000681}.
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DR   EMBL; DQIR01091544; HDA47020.1; -; Transcribed_RNA.
DR   EMBL; DQIR01106960; HDA62436.1; -; Transcribed_RNA.
DR   EMBL; DQIR01179213; HDB34690.1; -; Transcribed_RNA.
DR   RefSeq; XP_001926839.2; XM_001926804.4.
DR   IntAct; F1RNN5; 1.
DR   STRING; 9823.ENSSSCP00000010480; -.
DR   PaxDb; 9823-ENSSSCP00000010480; -.
DR   Ensembl; ENSSSCT00000010760.6; ENSSSCP00000010480.2; ENSSSCG00000009817.6.
DR   Ensembl; ENSSSCT00005032492.1; ENSSSCP00005019778.1; ENSSSCG00005020430.1.
DR   GeneID; 497623; -.
DR   KEGG; ssc:497623; -.
DR   CTD; 5027; -.
DR   VGNC; VGNC:111758; P2RX7.
DR   eggNOG; ENOG502QSBN; Eukaryota.
DR   GeneTree; ENSGT01020000230351; -.
DR   OrthoDB; 5312692at2759; -.
DR   TreeFam; TF328633; -.
DR   Reactome; R-SSC-139853; Elevation of cytosolic Ca2+ levels.
DR   Reactome; R-SSC-418346; Platelet homeostasis.
DR   Reactome; R-SSC-844456; The NLRP3 inflammasome.
DR   Proteomes; UP000008227; Chromosome 14.
DR   Bgee; ENSSSCG00000009817; Expressed in omentum and 40 other cell types or tissues.
DR   Genevisible; F1RNN5; SS.
DR   GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR   GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR   GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0098794; C:postsynapse; IEA:GOC.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0005524; F:ATP binding; IEA:Ensembl.
DR   GO; GO:0004931; F:extracellularly ATP-gated monoatomic cation channel activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0001530; F:lipopolysaccharide binding; IEA:Ensembl.
DR   GO; GO:0001614; F:purinergic nucleotide receptor activity; IEA:Ensembl.
DR   GO; GO:0032060; P:bleb assembly; IEA:Ensembl.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0071359; P:cellular response to dsRNA; IEA:Ensembl.
DR   GO; GO:0031668; P:cellular response to extracellular stimulus; IEA:Ensembl.
DR   GO; GO:0046513; P:ceramide biosynthetic process; IEA:Ensembl.
DR   GO; GO:0032963; P:collagen metabolic process; IEA:Ensembl.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
DR   GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0014051; P:gamma-aminobutyric acid secretion; IEA:Ensembl.
DR   GO; GO:0014047; P:glutamate secretion; IEA:Ensembl.
DR   GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl.
DR   GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR   GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR   GO; GO:0006509; P:membrane protein ectodomain proteolysis; IEA:Ensembl.
DR   GO; GO:0051882; P:mitochondrial depolarization; IEA:Ensembl.
DR   GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl.
DR   GO; GO:0043132; P:NAD transport; IEA:Ensembl.
DR   GO; GO:0045779; P:negative regulation of bone resorption; IEA:Ensembl.
DR   GO; GO:0045794; P:negative regulation of cell volume; IEA:Ensembl.
DR   GO; GO:0043409; P:negative regulation of MAPK cascade; IEA:Ensembl.
DR   GO; GO:0001845; P:phagolysosome assembly; IEA:Ensembl.
DR   GO; GO:0006649; P:phospholipid transfer to membrane; IEA:Ensembl.
DR   GO; GO:0017121; P:plasma membrane phospholipid scrambling; IEA:Ensembl.
DR   GO; GO:0046931; P:pore complex assembly; IEA:Ensembl.
DR   GO; GO:1904172; P:positive regulation of bleb assembly; IEA:Ensembl.
DR   GO; GO:0030501; P:positive regulation of bone mineralization; IEA:Ensembl.
DR   GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IEA:Ensembl.
DR   GO; GO:0014054; P:positive regulation of gamma-aminobutyric acid secretion; IEA:Ensembl.
DR   GO; GO:0014049; P:positive regulation of glutamate secretion; IEA:Ensembl.
DR   GO; GO:0045821; P:positive regulation of glycolytic process; IEA:Ensembl.
DR   GO; GO:0032730; P:positive regulation of interleukin-1 alpha production; IEA:Ensembl.
DR   GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IEA:Ensembl.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
DR   GO; GO:0060907; P:positive regulation of macrophage cytokine production; IEA:Ensembl.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR   GO; GO:0051901; P:positive regulation of mitochondrial depolarization; IEA:Ensembl.
DR   GO; GO:0032308; P:positive regulation of prostaglandin secretion; IEA:Ensembl.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0050714; P:positive regulation of protein secretion; IEA:Ensembl.
DR   GO; GO:0070234; P:positive regulation of T cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IEA:Ensembl.
DR   GO; GO:0032310; P:prostaglandin secretion; IEA:Ensembl.
DR   GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
DR   GO; GO:0016485; P:protein processing; IEA:Ensembl.
DR   GO; GO:0009306; P:protein secretion; IEA:Ensembl.
DR   GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:Ensembl.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IEA:Ensembl.
DR   GO; GO:0033198; P:response to ATP; IEA:Ensembl.
DR   GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR   GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
DR   GO; GO:0034405; P:response to fluid shear stress; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR   GO; GO:0010043; P:response to zinc ion; IEA:Ensembl.
DR   GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
DR   GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl.
DR   GO; GO:0016079; P:synaptic vesicle exocytosis; IEA:Ensembl.
DR   GO; GO:0070231; P:T cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0043029; P:T cell homeostasis; IEA:Ensembl.
DR   GO; GO:0001913; P:T cell mediated cytotoxicity; IEA:Ensembl.
DR   GO; GO:0042098; P:T cell proliferation; IEA:Ensembl.
DR   GO; GO:0006900; P:vesicle budding from membrane; IEA:Ensembl.
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; IPR046815; P2RX7_C.
DR   InterPro; IPR003050; P2X7_purinoceptor.
DR   InterPro; IPR027309; P2X_extracellular_dom_sf.
DR   InterPro; IPR001429; P2X_purnocptor.
DR   NCBIfam; TIGR00863; P2X; 1.
DR   PANTHER; PTHR10125; P2X PURINOCEPTOR; 1.
DR   PANTHER; PTHR10125:SF13; P2X PURINOCEPTOR 7; 1.
DR   Pfam; PF20478; P2RX7_C; 1.
DR   Pfam; PF00864; P2X_receptor; 1.
DR   PRINTS; PR01314; P2X7RECEPTOR.
DR   PRINTS; PR01307; P2XRECEPTOR.
DR   PROSITE; PS01212; P2X_RECEPTOR; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Ion channel {ECO:0000256|RuleBase:RU000681};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU000681};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000681};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:F1RNN5};
KW   Receptor {ECO:0000256|RuleBase:RU000681};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU000681};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU000681};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000681}.
FT   TRANSMEM        29..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000681"
FT   TRANSMEM        333..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000681"
FT   DOMAIN          400..592
FT                   /note="P2X purinoreceptor 7 intracellular"
FT                   /evidence="ECO:0000259|Pfam:PF20478"
SQ   SEQUENCE   595 AA;  68348 MW;  8F1A1A65A31D9FA3 CRC64;
     MPAWCSWNDV FQYETNKVTR IQSMNYGTIK WFFHVLVFSY VSFALVSDKR YQRKESVISS
     VHTKVKGIAE VTQEIVENGL KKVVPSVLDT ADYTFPLQGN SFFVMTNFLK TEGQEQGLCP
     EYPTRRTLCS SNQGCKKGWM DPQSKGIQTG RCVEYKGKQK TCEVSAWCPI EAVEEAPQPA
     LLRSAENFTV LIKNNIDFPG HNYTTRNILP GLNITCTFHK TQNPLCPIFR LGDIFRETGD
     NFSDVAIQGG IMGIEIYWDC NLDRWFHHCR PKYSFRRLDD KTAKESSYPG YNFRYAKYYK
     ENNVEKRTLI KVFGIRFDIL VFGTGGKFDI IQLIVYIGST LSYFGLATVF IDFLINTYSN
     NCCRSHVYPC CKCCEPCAVN EYYYRKKCES IMEPKPTLKY VSFVDEPHIR MVDQRLLGRS
     LQDVKGEEVP RPPMDFTDLS RLPLSLHDPP FIPGQPEAIQ LLSEEAAPKS SDCPDWCQCG
     NCLPSQLPDS HKCLEELCCR KKLGACITTS ELFQKLVLSR GVLQFLLHYQ EPLLVLDADS
     ANSQLRHCAY RCYTIWRFGS QDLADFAILP SCCRWKIRRE FPKSEGQYSG FQSPY
//
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