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P2RX4_BOVIN
ID   P2RX4_BOVIN             Reviewed;         388 AA.
AC   Q5E9U1;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=P2X purinoceptor 4;
DE            Short=P2X4;
DE   AltName: Full=ATP receptor;
DE   AltName: Full=Purinergic receptor;
GN   Name=P2RX4;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Brain cortex;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor for ATP that acts as a ligand-gated ion channel.
CC       This receptor is insensitive to the antagonists PPADS and suramin (By
CC       similarity). {ECO:0000250|UniProtKB:P51577,
CC       ECO:0000250|UniProtKB:Q99571}.
CC   -!- SUBUNIT: Functional P2XRs are organized as homomeric and heteromeric
CC       trimers. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q99571}; Multi-
CC       pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the P2X receptor family. {ECO:0000305}.
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DR   EMBL; BT020829; AAX08846.1; -; mRNA.
DR   EMBL; BC120340; AAI20341.1; -; mRNA.
DR   RefSeq; NP_001029221.1; NM_001034049.1.
DR   AlphaFoldDB; Q5E9U1; -.
DR   SMR; Q5E9U1; -.
DR   STRING; 9913.ENSBTAP00000014321; -.
DR   PaxDb; Q5E9U1; -.
DR   PRIDE; Q5E9U1; -.
DR   Ensembl; ENSBTAT00000014321; ENSBTAP00000014321; ENSBTAG00000010812.
DR   GeneID; 338036; -.
DR   KEGG; bta:338036; -.
DR   CTD; 5025; -.
DR   VEuPathDB; HostDB:ENSBTAG00000010812; -.
DR   VGNC; VGNC:32520; P2RX4.
DR   eggNOG; ENOG502QSUI; Eukaryota.
DR   GeneTree; ENSGT01020000230351; -.
DR   HOGENOM; CLU_034469_2_0_1; -.
DR   InParanoid; Q5E9U1; -.
DR   OMA; QGYCPEL; -.
DR   OrthoDB; 1128763at2759; -.
DR   TreeFam; TF328633; -.
DR   Reactome; R-BTA-139853; Elevation of cytosolic Ca2+ levels.
DR   Reactome; R-BTA-418346; Platelet homeostasis.
DR   Proteomes; UP000009136; Chromosome 17.
DR   Bgee; ENSBTAG00000010812; Expressed in ascending colon and 107 other tissues.
DR   GO; GO:0005639; C:integral component of nuclear inner membrane; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0098794; C:postsynapse; IEA:GOC.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0045296; F:cadherin binding; IEA:Ensembl.
DR   GO; GO:0004931; F:extracellularly ATP-gated cation channel activity; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0099604; F:ligand-gated calcium channel activity; IEA:Ensembl.
DR   GO; GO:0001614; F:purinergic nucleotide receptor activity; IEA:Ensembl.
DR   GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0071318; P:cellular response to ATP; ISS:UniProtKB.
DR   GO; GO:0071294; P:cellular response to zinc ion; ISS:UniProtKB.
DR   GO; GO:0034220; P:ion transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0051899; P:membrane depolarization; IEA:Ensembl.
DR   GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; IEA:Ensembl.
DR   GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IEA:Ensembl.
DR   GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IEA:Ensembl.
DR   GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IEA:Ensembl.
DR   GO; GO:2001028; P:positive regulation of endothelial cell chemotaxis; IEA:Ensembl.
DR   GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR   GO; GO:0055117; P:regulation of cardiac muscle contraction; IEA:Ensembl.
DR   GO; GO:0055119; P:relaxation of cardiac muscle; IEA:Ensembl.
DR   GO; GO:0034405; P:response to fluid shear stress; IEA:Ensembl.
DR   Gene3D; 2.60.490.10; -; 1.
DR   InterPro; IPR003047; P2X4_purnocptor.
DR   InterPro; IPR027309; P2X_extracellular_dom_sf.
DR   InterPro; IPR001429; P2X_purnocptor.
DR   PIRSF; PIRSF005713; P2X_purinoceptor; 1.
DR   PRINTS; PR01311; P2X4RECEPTOR.
DR   PRINTS; PR01307; P2XRECEPTOR.
DR   TIGRFAMs; TIGR00863; P2X; 1.
DR   PROSITE; PS01212; P2X_RECEPTOR; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW   Ligand-gated ion channel; Membrane; Receptor; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..388
FT                   /note="P2X purinoceptor 4"
FT                   /id="PRO_0000269193"
FT   TOPO_DOM        1..33
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        34..54
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        55..338
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        339..359
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        360..388
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        131
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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        199
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        208
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        116..165
FT                   /evidence="ECO:0000250"
FT   DISULFID        126..149
FT                   /evidence="ECO:0000250"
FT   DISULFID        132..159
FT                   /evidence="ECO:0000250"
FT   DISULFID        217..227
FT                   /evidence="ECO:0000250"
FT   DISULFID        261..270
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   388 AA;  43529 MW;  8421F3323FCFEDDC CRC64;
     MTGCCTVLGA FLFEYDTPRI VLIRSRKVGL MNRTVQLLIL AYVIGWVFVW EKGYQETDSV
     VSSVTVKAKG VTMTNTSKLG FRIWDVADYV IPAQEENSVF IMTNMVITMN QTQGLCPEIP
     GKTTVCETDA NCTAGSAGTH SSGVATGRCV SFNGTLKTCE VAAWCPVEDD TEVPKPAFLK
     AAENFTLLVK NNIWYPKFNF SKRNILPNIT TAYLKTCIYD AKTDPFCPIF RLGKIVESAG
     HSFQDIAIEG GIMGIQIKWN CNLDRAASFC LPRYSFRRLD TRDLAHNVSP GYNFRFAKYY
     SDLKGAEHRT LIKAYGIRFD IIVFGKAGKF DIIPTMINIG SGLALLGVAT VLCDVIVLYC
     MKKRYYYREK KYKYVEDYEQ GLGNQMEQ
 
 
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