P2Y14_BOVIN
ID P2Y14_BOVIN Reviewed; 337 AA.
AC Q3SX17;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=P2Y purinoceptor 14;
DE Short=P2Y14;
DE AltName: Full=UDP-glucose receptor;
GN Name=P2RY14;
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=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for UDP-glucose and other UDP-sugar coupled to G-
CC proteins. Not activated by ATP, ADP, UTP or ATP (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; BT030704; ABS45020.1; -; mRNA.
DR EMBL; BC104556; AAI04557.1; -; mRNA.
DR RefSeq; NP_001070477.1; NM_001077009.1.
DR RefSeq; XP_005201886.1; XM_005201829.3.
DR RefSeq; XP_005201887.1; XM_005201830.3.
DR RefSeq; XP_010799800.1; XM_010801498.2.
DR RefSeq; XP_010799801.1; XM_010801499.2.
DR RefSeq; XP_010799802.1; XM_010801500.2.
DR RefSeq; XP_015328558.1; XM_015473072.1.
DR RefSeq; XP_015328559.1; XM_015473073.1.
DR RefSeq; XP_015328560.1; XM_015473074.1.
DR AlphaFoldDB; Q3SX17; -.
DR SMR; Q3SX17; -.
DR STRING; 9913.ENSBTAP00000027950; -.
DR PaxDb; Q3SX17; -.
DR PRIDE; Q3SX17; -.
DR Ensembl; ENSBTAT00000027950; ENSBTAP00000027950; ENSBTAG00000020990.
DR GeneID; 767936; -.
DR KEGG; bta:767936; -.
DR CTD; 9934; -.
DR VEuPathDB; HostDB:ENSBTAG00000020990; -.
DR VGNC; VGNC:32527; P2RY14.
DR eggNOG; ENOG502R537; Eukaryota.
DR GeneTree; ENSGT01050000244982; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; Q3SX17; -.
DR OMA; VHTVNYS; -.
DR OrthoDB; 784055at2759; -.
DR TreeFam; TF330969; -.
DR Reactome; R-BTA-417957; P2Y receptors.
DR Reactome; R-BTA-418594; G alpha (i) signalling events.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000020990; Expressed in thyroid gland and 95 other tissues.
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; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR005466; P2Y14_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01655; UDPGLUCOSER.
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..337
FT /note="P2Y purinoceptor 14"
FT /id="PRO_0000310278"
FT TOPO_DOM 1..28
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..95
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..187
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..277
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 93..171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 337 AA; 38697 MW; 16F44B1A4C8F5117 CRC64;
MNATSVPPAE GSCPSNALIT KQIIPMLYFV VFVAGILLNG MSGWVFFYVP SSKSFIVYLK
NIVIADFLMS LTFPFKILGD LGLGLWQVKV FVCRVSAVLF YINMYVSIVF FGLIGFDRYY
KIVKPLLTSF IQSISYSKLL SVLVWSLTLL IALPNMILTN RNVTEATRVK CMDLKSDLGL
KWHKASSYIF VGIFWIVFLS LIIFYTAITK KIFKSHFKSR KNSVSVKKKS SRNIFSIMFV
FFICFVPYHI ARIPYTQSQT EAHYSCQSKQ ILFYVKEFSL LLSAANVCLD PIIYFFLCQP
FREVLCKKLH IQLKTQHDSE TSKIKRENII QESTDTL
