P2Y13_RAT
ID P2Y13_RAT Reviewed; 336 AA.
AC Q6GUG4;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=P2Y purinoceptor 13;
DE Short=P2Y13;
GN Name=P2ry13;
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 [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=15183123; DOI=10.1016/j.bcp.2004.02.038;
RA Fumagalli M., Trincavelli L., Lecca D., Martini C., Ciana P.,
RA Abbracchio M.P.;
RT "Cloning, pharmacological characterisation and distribution of the rat G-
RT protein-coupled P2Y(13) receptor.";
RL Biochem. Pharmacol. 68:113-124(2004).
CC -!- FUNCTION: Receptor for ADP. Coupled to G(i)-proteins. May play a role
CC in hematopoiesis and the immune system. {ECO:0000269|PubMed:15183123}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Highest levels in spleen, liver brain and kidney.
CC Lower but significant level are also detected in intestine, stomach,
CC skeletal muscle, testis, heart and lung. {ECO:0000269|PubMed:15183123}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AY639875; AAT57664.1; -; mRNA.
DR RefSeq; NP_001002853.1; NM_001002853.1.
DR RefSeq; XP_008759213.1; XM_008760991.2.
DR AlphaFoldDB; Q6GUG4; -.
DR SMR; Q6GUG4; -.
DR STRING; 10116.ENSRNOP00000047532; -.
DR ChEMBL; CHEMBL4524124; -.
DR GlyGen; Q6GUG4; 3 sites.
DR PhosphoSitePlus; Q6GUG4; -.
DR PaxDb; Q6GUG4; -.
DR Ensembl; ENSRNOT00000051027; ENSRNOP00000047532; ENSRNOG00000029756.
DR GeneID; 310444; -.
DR KEGG; rno:310444; -.
DR UCSC; RGD:1302941; rat.
DR CTD; 53829; -.
DR RGD; 1302941; P2ry13.
DR eggNOG; ENOG502QUS2; Eukaryota.
DR GeneTree; ENSGT01050000244845; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; Q6GUG4; -.
DR OMA; KIIRPFG; -.
DR OrthoDB; 971778at2759; -.
DR PhylomeDB; Q6GUG4; -.
DR TreeFam; TF330969; -.
DR Reactome; R-RNO-417957; P2Y receptors.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:Q6GUG4; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000029756; Expressed in spleen and 17 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045028; F:G protein-coupled purinergic nucleotide receptor activity; IDA:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; IEA:InterPro.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR008109; P2Y13_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01735; P2Y13PRNCPTR.
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; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..336
FT /note="P2Y purinoceptor 13"
FT /id="PRO_0000070043"
FT TOPO_DOM 1..32
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..100
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..193
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..281
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..336
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 14
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 99..176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 336 AA; 38823 MW; E1DA0D314DD8C1CE CRC64;
MLGTVNTTGM QGFNKSERCP RDTRMTQLLF PVLYTVVFFT GVLLNTLALW VFIHIPSNST
FIIYLKNTLV ADLIMTLMLP FKILSDSRLA PWQLRGFVCT FSSVVFYETM YVGIMMLGLI
AFDRFLKIVV PFRKTFVKKT AFAKIVSISI WLLMFLISLP NMILNKEATA STVKKCASLK
SPLGLLWHQV VSHTCQFIFW TVFILMLLFY TVIAKKVYDS YRKFKSRDSK HKRLEAKVFI
VMAVFFVCFA PFHFVRVPYT HSQTTNKTDC RLENQLFLAK ESTLFLATTN ICMDPLIYII
LCKKFTRKVP CMRWRTKTAA SSDEHHSSQT DNITLS
