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P2Y14_HUMAN
ID   P2Y14_HUMAN             Reviewed;         338 AA.
AC   Q15391; Q8IYT7;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 176.
DE   RecName: Full=P2Y purinoceptor 14;
DE            Short=P2Y14;
DE   AltName: Full=G-protein coupled receptor 105;
DE   AltName: Full=UDP-glucose receptor;
GN   Name=P2RY14; Synonyms=GPR105, KIAA0001;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11524702; DOI=10.1086/323610;
RA   Joensuu T., Haemaelaeinen R., Yuan B., Johnson C., Tegelberg S.,
RA   Gasparini P., Zelante L., Pirvola U., Pakarinen L., Lehesjoki A.-E.,
RA   de la Chapelle A., Sankila E.-M.;
RT   "Mutations in a novel gene with transmembrane domains underlie Usher
RT   syndrome type 3.";
RL   Am. J. Hum. Genet. 69:673-684(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Bone marrow;
RX   PubMed=7584026; DOI=10.1093/dnares/1.1.27;
RA   Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S.,
RA   Nagase T., Seki N., Ishikawa K., Tabata S.;
RT   "Prediction of the coding sequences of unidentified human genes. I. The
RT   coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of
RT   randomly sampled cDNA clones from human immature myeloid cell line KG-1.";
RL   DNA Res. 1:27-35(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION.
RX   PubMed=10753868; DOI=10.1074/jbc.275.15.10767;
RA   Chambers J.K., Macdonald L.E., Sarau H.M., Ames R.S., Freeman K.,
RA   Foley J.J., Zhu Y., McLaughlin M.M., Murdock P., McMillan L., Trill J.,
RA   Swift A., Aiyar N., Taylor P., Vawter L., Naheed S., Szekeres P.,
RA   Hervieu G., Scott C., Watson J.M., Murphy A.J., Duzic E., Klein C.,
RA   Bergsma D.J., Wilson S., Livi G.P.;
RT   "A G protein-coupled receptor for UDP-glucose.";
RL   J. Biol. Chem. 275:10767-10771(2000).
RN   [5]
RP   VARIANT [LARGE SCALE ANALYSIS] PRO-140.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Receptor for UDP-glucose and other UDP-sugar coupled to G-
CC       proteins. Not activated by ATP, ADP, UTP or ATP.
CC       {ECO:0000269|PubMed:10753868}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Highest expression in the placenta, adipose tissue,
CC       stomach and intestine, intermediate levels in the brain, spleen, lung
CC       and heart, lowest levels in the kidney.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA02791.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF456925; AAL47764.1; -; Genomic_DNA.
DR   EMBL; D13626; BAA02791.2; ALT_INIT; mRNA.
DR   EMBL; BC034989; AAH34989.1; -; mRNA.
DR   CCDS; CCDS3156.1; -.
DR   RefSeq; NP_001074924.1; NM_001081455.1.
DR   RefSeq; NP_055694.3; NM_014879.3.
DR   RefSeq; XP_005247979.1; XM_005247922.3.
DR   RefSeq; XP_005247980.1; XM_005247923.3.
DR   RefSeq; XP_011511642.1; XM_011513340.2.
DR   RefSeq; XP_016863072.1; XM_017007583.1.
DR   AlphaFoldDB; Q15391; -.
DR   SMR; Q15391; -.
DR   BioGRID; 115260; 6.
DR   IntAct; Q15391; 1.
DR   STRING; 9606.ENSP00000308361; -.
DR   BindingDB; Q15391; -.
DR   ChEMBL; CHEMBL4518; -.
DR   DrugBank; DB01069; Promethazine.
DR   GuidetoPHARMACOLOGY; 330; -.
DR   GlyGen; Q15391; 2 sites.
DR   iPTMnet; Q15391; -.
DR   PhosphoSitePlus; Q15391; -.
DR   BioMuta; P2RY14; -.
DR   DMDM; 3122322; -.
DR   jPOST; Q15391; -.
DR   MassIVE; Q15391; -.
DR   PaxDb; Q15391; -.
DR   PeptideAtlas; Q15391; -.
DR   PRIDE; Q15391; -.
DR   ProteomicsDB; 60561; -.
DR   Antibodypedia; 18296; 255 antibodies from 30 providers.
DR   DNASU; 9934; -.
DR   Ensembl; ENST00000309170.8; ENSP00000308361.3; ENSG00000174944.9.
DR   Ensembl; ENST00000424796.6; ENSP00000408733.2; ENSG00000174944.9.
DR   GeneID; 9934; -.
DR   KEGG; hsa:9934; -.
DR   MANE-Select; ENST00000309170.8; ENSP00000308361.3; NM_014879.4; NP_055694.3.
DR   UCSC; uc003eyr.2; human.
DR   CTD; 9934; -.
DR   DisGeNET; 9934; -.
DR   GeneCards; P2RY14; -.
DR   HGNC; HGNC:16442; P2RY14.
DR   HPA; ENSG00000174944; Tissue enhanced (placenta).
DR   MIM; 610116; gene.
DR   neXtProt; NX_Q15391; -.
DR   OpenTargets; ENSG00000174944; -.
DR   PharmGKB; PA28853; -.
DR   VEuPathDB; HostDB:ENSG00000174944; -.
DR   eggNOG; ENOG502R537; Eukaryota.
DR   GeneTree; ENSGT01050000244982; -.
DR   HOGENOM; CLU_009579_8_2_1; -.
DR   InParanoid; Q15391; -.
DR   OMA; VHTVNYS; -.
DR   OrthoDB; 784055at2759; -.
DR   PhylomeDB; Q15391; -.
DR   TreeFam; TF330969; -.
DR   PathwayCommons; Q15391; -.
DR   Reactome; R-HSA-417957; P2Y receptors.
DR   Reactome; R-HSA-418594; G alpha (i) signalling events.
DR   SignaLink; Q15391; -.
DR   SIGNOR; Q15391; -.
DR   BioGRID-ORCS; 9934; 13 hits in 1064 CRISPR screens.
DR   GenomeRNAi; 9934; -.
DR   Pharos; Q15391; Tchem.
DR   PRO; PR:Q15391; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q15391; protein.
DR   Bgee; ENSG00000174944; Expressed in decidua and 171 other tissues.
DR   ExpressionAtlas; Q15391; baseline and differential.
DR   Genevisible; Q15391; HS.
DR   GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0045028; F:G protein-coupled purinergic nucleotide receptor activity; IBA:GO_Central.
DR   GO; GO:0045029; F:G protein-coupled UDP receptor activity; NAS:UniProtKB.
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..338
FT                   /note="P2Y purinoceptor 14"
FT                   /id="PRO_0000070044"
FT   TOPO_DOM        1..29
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        30..50
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        51..55
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        56..76
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        77..96
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        97..117
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        118..139
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        161..188
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        210..234
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        235..255
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        256..278
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        279..299
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        300..338
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        3
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        161
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        94..172
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   VARIANT         140
FT                   /note="L -> P (in a colorectal cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035767"
FT   CONFLICT        54
FT                   /note="K -> E (in Ref. 3; AAH34989)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   338 AA;  38971 MW;  8DBE7C782CB4753D CRC64;
     MINSTSTQPP DESCSQNLLI TQQIIPVLYC MVFIAGILLN GVSGWIFFYV PSSKSFIIYL
     KNIVIADFVM SLTFPFKILG DSGLGPWQLN VFVCRVSAVL FYVNMYVSIV FFGLISFDRY
     YKIVKPLWTS FIQSVSYSKL LSVIVWMLML LLAVPNIILT NQSVREVTQI KCIELKSELG
     RKWHKASNYI FVAIFWIVFL LLIVFYTAIT KKIFKSHLKS SRNSTSVKKK SSRNIFSIVF
     VFFVCFVPYH IARIPYTKSQ TEAHYSCQSK EILRYMKEFT LLLSAANVCL DPIIYFFLCQ
     PFREILCKKL HIPLKAQNDL DISRIKRGNT TLESTDTL
 
 
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