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P2RY4_RAT
ID   P2RY4_RAT               Reviewed;         361 AA.
AC   O35811;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=P2Y purinoceptor 4;
DE            Short=P2Y4;
GN   Name=P2ry4; Synonyms=P2y4;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RA   Bogdanov Y.D., Wildman S., King B.F., Burntock G.;
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RX   PubMed=9751165; DOI=10.1046/j.1471-4159.1998.71041348.x;
RA   Webb T.E., Henderson D., Roberts J.A., Barnard E.A.;
RT   "Molecular cloning and characterization of the rat P2Y4 receptor.";
RL   J. Neurochem. 71:1348-1357(1998).
CC   -!- FUNCTION: Receptor for ATP and UTP coupled to G-proteins that activate
CC       a phosphatidylinositol-calcium second messenger system. Not activated
CC       by ADP or UDP.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Widely expressed at low levels. In brain, higher
CC       expression in the pineal gland and ventricular system.
CC   -!- PTM: Phosphorylation of Ser-329 and Ser-330 is a key step in agonist-
CC       dependent desensitization and loss of surface P2RY4. This
CC       phosphorylation does not involve PKC, nor other calcium-activated
CC       kinases (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; Y14705; CAA75007.1; -; Genomic_DNA.
DR   EMBL; Y11433; CAA72241.1; -; mRNA.
DR   RefSeq; NP_113868.1; NM_031680.1.
DR   RefSeq; XP_006257155.1; XM_006257093.3.
DR   RefSeq; XP_006257156.1; XM_006257094.3.
DR   RefSeq; XP_006257157.1; XM_006257095.3.
DR   RefSeq; XP_017457635.1; XM_017602146.1.
DR   RefSeq; XP_017457636.1; XM_017602147.1.
DR   AlphaFoldDB; O35811; -.
DR   SMR; O35811; -.
DR   STRING; 10116.ENSRNOP00000039027; -.
DR   BindingDB; O35811; -.
DR   ChEMBL; CHEMBL2124; -.
DR   DrugCentral; O35811; -.
DR   GuidetoPHARMACOLOGY; 325; -.
DR   GlyGen; O35811; 1 site.
DR   PhosphoSitePlus; O35811; -.
DR   PaxDb; O35811; -.
DR   PRIDE; O35811; -.
DR   Ensembl; ENSRNOT00000045907; ENSRNOP00000039027; ENSRNOG00000070777.
DR   Ensembl; ENSRNOT00000096316; ENSRNOP00000094459; ENSRNOG00000070777.
DR   Ensembl; ENSRNOT00000099755; ENSRNOP00000085052; ENSRNOG00000070777.
DR   Ensembl; ENSRNOT00000112073; ENSRNOP00000082634; ENSRNOG00000070777.
DR   GeneID; 63843; -.
DR   KEGG; rno:63843; -.
DR   UCSC; RGD:61798; rat.
DR   CTD; 5030; -.
DR   RGD; 61798; P2ry4.
DR   eggNOG; ENOG502QSTF; Eukaryota.
DR   GeneTree; ENSGT01030000234621; -.
DR   HOGENOM; CLU_009579_8_2_1; -.
DR   InParanoid; O35811; -.
DR   OMA; HWPFGTG; -.
DR   OrthoDB; 1077455at2759; -.
DR   PhylomeDB; O35811; -.
DR   TreeFam; TF350009; -.
DR   Reactome; R-RNO-417957; P2Y receptors.
DR   Reactome; R-RNO-418594; G alpha (i) signalling events.
DR   PRO; PR:O35811; -.
DR   Proteomes; UP000002494; Chromosome X.
DR   Bgee; ENSRNOG00000002953; Expressed in esophagus and 17 other tissues.
DR   Genevisible; O35811; RN.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0099059; C:integral component of presynaptic active zone membrane; IDA:SynGO.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IDA:RGD.
DR   GO; GO:0045028; F:G protein-coupled purinergic nucleotide receptor activity; IEA:InterPro.
DR   GO; GO:0045030; F:G protein-coupled UTP receptor activity; ISO:RGD.
DR   GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0071380; P:cellular response to prostaglandin E stimulus; ISO:RGD.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0099509; P:regulation of presynaptic cytosolic calcium ion concentration; IDA:SynGO.
DR   GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR   GO; GO:0030321; P:transepithelial chloride transport; ISO:RGD.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR000018; P2Y4.
DR   PANTHER; PTHR24231:SF21; PTHR24231:SF21; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01066; P2Y4PRNOCPTR.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Phosphoprotein; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..361
FT                   /note="P2Y purinoceptor 4"
FT                   /id="PRO_0000070023"
FT   TOPO_DOM        1..30
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        31..58
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        59..68
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        69..91
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        92..108
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..127
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        128..149
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        150..170
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        171..192
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        193..218
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        219..242
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        243..265
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        266..283
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        284..305
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        306..361
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        175
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        104..181
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   361 AA;  40894 MW;  0377F96E54B449A3 CRC64;
     MTSAESLLFT SLGPSPSSGD GDCRFNEEFK FILLPMSYAV VFVLGLALNA PTLWLFLFRL
     RPWDATATYM FHLALSDTLY VLSLPTLVYY YAARNHWPFG TGLCKFVRFL FYWNLYCSVL
     FLTCISVHRY LGICHPLRAI RWGRPRFASL LCLGVWLVVA GCLVPNLFFV TTNANGTTIL
     CHDTTLPEEF DHYVYFSSAV MVLLFGLPFL ITLVCYGLMA RRLYRPLPGA GQSSSRLRSL
     RTIAVVLTVF AVCFVPFHIT RTIYYQARLL QADCHVLNIV NVVYKVTRPL ASANSCLDPV
     LYLFTGDKYR NQLQQLCRGS KPKPRTAASS LALVTLHEES ISRWADTHQD STFSAYEGDR
     L
 
 
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