ID   GPR17_HUMAN             Reviewed;         367 AA.
AC   Q13304; A8K9L0; B2R9X0; Q8N5S7; Q9UDZ6; Q9UE21;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   13-SEP-2023, entry version 177.
DE   RecName: Full=Uracil nucleotide/cysteinyl leukotriene receptor;
DE            Short=UDP/CysLT receptor;
DE   AltName: Full=G-protein coupled receptor 17;
DE   AltName: Full=P2Y-like receptor;
DE   AltName: Full=R12;
GN   Name=GPR17;
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] (ISOFORM 2).
RX   PubMed=8558062; DOI=10.1002/jlb.59.1.18;
RA   Raport C.J., Schweickart V.L., Chantry D., Eddy R.L. Jr., Shows T.B.,
RA   Godiska R., Gray P.W.;
RT   "New members of the chemokine receptor gene family.";
RL   J. Leukoc. Biol. 59:18-23(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Hippocampus;
RX   PubMed=9523551; DOI=10.1046/j.1471-4159.1998.70041357.x;
RA   Blaesius R.H., Weber R.G., Lichter P., Ogilvie A.;
RT   "A novel orphan G protein-coupled receptor primarily expressed in the brain
RT   is localized on human chromosomal band 2q21.";
RL   J. Neurochem. 70:1357-1365(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Kidney;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain;
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   [6]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=16990797; DOI=10.1038/sj.emboj.7601341;
RA   Ciana P., Fumagalli M., Trincavelli M.L., Verderio C., Rosa P., Lecca D.,
RA   Ferrario S., Parravicini C., Capra V., Gelosa P., Guerrini U.,
RA   Belcredito S., Cimino M., Sironi L., Tremoli E., Rovati G.E., Martini C.,
RA   Abbracchio M.P.;
RT   "The orphan receptor GPR17 identified as a new dual uracil
RT   nucleotides/cysteinyl-leukotrienes receptor.";
RL   EMBO J. 25:4615-4627(2006).
CC   -!- FUNCTION: Dual specificity receptor for uracil nucleotides and
CC       cysteinyl leukotrienes (CysLTs). Signals through G(i) and inhibition of
CC       adenylyl cyclase. May mediate brain damage by nucleotides and CysLTs
CC       following ischemia. {ECO:0000269|PubMed:16990797}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q13304-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q13304-2; Sequence=VSP_001987;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, kidney, heart and umbilical
CC       vein endothelial cells. Highest level in brain.
CC       {ECO:0000269|PubMed:16990797}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; U33447; AAB16746.1; -; Genomic_DNA.
DR   EMBL; Y12546; CAA73144.1; -; mRNA.
DR   EMBL; Z94154; CAB08107.1; -; mRNA.
DR   EMBL; Z94155; CAB08108.1; -; mRNA.
DR   EMBL; AK292725; BAF85414.1; -; mRNA.
DR   EMBL; AK313949; BAG36667.1; -; mRNA.
DR   EMBL; CH471103; EAW95337.1; -; Genomic_DNA.
DR   EMBL; BC031653; AAH31653.1; -; mRNA.
DR   EMBL; BC039595; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS2148.1; -. [Q13304-1]
DR   CCDS; CCDS92862.1; -. [Q13304-2]
DR   RefSeq; NP_001154887.1; NM_001161415.1. [Q13304-1]
DR   RefSeq; NP_001154888.1; NM_001161416.1. [Q13304-2]
DR   RefSeq; NP_001154889.1; NM_001161417.1. [Q13304-2]
DR   RefSeq; NP_005282.1; NM_005291.2. [Q13304-1]
DR   RefSeq; XP_016859322.1; XM_017003833.1.
DR   PDB; 7Y89; EM; 3.02 A; A=50-342.
DR   PDBsum; 7Y89; -.
DR   AlphaFoldDB; Q13304; -.
DR   SMR; Q13304; -.
DR   BioGRID; 109099; 288.
DR   IntAct; Q13304; 2.
DR   MINT; Q13304; -.
DR   STRING; 9606.ENSP00000442982; -.
DR   BindingDB; Q13304; -.
DR   ChEMBL; CHEMBL1075162; -.
DR   DrugBank; DB03501; Galactose-uridine-5'-diphosphate.
DR   DrugBank; DB01861; Uridine diphosphate glucose.
DR   DrugBank; DB03435; Uridine-5'-Diphosphate.
DR   DrugCentral; Q13304; -.
DR   GuidetoPHARMACOLOGY; 88; -.
DR   GlyCosmos; Q13304; 3 sites, No reported glycans.
DR   GlyGen; Q13304; 3 sites.
DR   iPTMnet; Q13304; -.
DR   PhosphoSitePlus; Q13304; -.
DR   BioMuta; GPR17; -.
DR   DMDM; 21264435; -.
DR   MassIVE; Q13304; -.
DR   PaxDb; Q13304; -.
DR   PeptideAtlas; Q13304; -.
DR   ProteomicsDB; 59291; -. [Q13304-1]
DR   ProteomicsDB; 59292; -. [Q13304-2]
DR   Antibodypedia; 18483; 479 antibodies from 36 providers.
DR   DNASU; 2840; -.
DR   Ensembl; ENST00000272644.7; ENSP00000272644.3; ENSG00000144230.17. [Q13304-1]
DR   Ensembl; ENST00000393018.3; ENSP00000376741.3; ENSG00000144230.17. [Q13304-1]
DR   Ensembl; ENST00000486700.2; ENSP00000508383.1; ENSG00000144230.17. [Q13304-2]
DR   Ensembl; ENST00000544369.5; ENSP00000442982.1; ENSG00000144230.17. [Q13304-1]
DR   GeneID; 2840; -.
DR   KEGG; hsa:2840; -.
DR   MANE-Select; ENST00000486700.2; ENSP00000508383.1; NM_001161417.2; NP_001154889.1. [Q13304-2]
DR   UCSC; uc002tpc.4; human. [Q13304-1]
DR   AGR; HGNC:4471; -.
DR   CTD; 2840; -.
DR   DisGeNET; 2840; -.
DR   GeneCards; GPR17; -.
DR   HGNC; HGNC:4471; GPR17.
DR   HPA; ENSG00000144230; Tissue enhanced (heart muscle, intestine).
DR   MIM; 603071; gene.
DR   neXtProt; NX_Q13304; -.
DR   OpenTargets; ENSG00000144230; -.
DR   PharmGKB; PA28859; -.
DR   VEuPathDB; HostDB:ENSG00000144230; -.
DR   eggNOG; ENOG502QW6S; Eukaryota.
DR   GeneTree; ENSGT01090000260026; -.
DR   HOGENOM; CLU_009579_8_2_1; -.
DR   InParanoid; Q13304; -.
DR   OMA; TCLNGAM; -.
DR   OrthoDB; 5383533at2759; -.
DR   PhylomeDB; Q13304; -.
DR   TreeFam; TF330775; -.
DR   PathwayCommons; Q13304; -.
DR   Reactome; R-HSA-391906; Leukotriene receptors.
DR   Reactome; R-HSA-416476; G alpha (q) signalling events.
DR   Reactome; R-HSA-417957; P2Y receptors.
DR   Reactome; R-HSA-418594; G alpha (i) signalling events.
DR   SignaLink; Q13304; -.
DR   SIGNOR; Q13304; -.
DR   BioGRID-ORCS; 2840; 94 hits in 1142 CRISPR screens.
DR   GeneWiki; GPR17; -.
DR   GenomeRNAi; 2840; -.
DR   Pharos; Q13304; Tchem.
DR   PRO; PR:Q13304; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q13304; Protein.
DR   Bgee; ENSG00000144230; Expressed in apex of heart and 111 other tissues.
DR   ExpressionAtlas; Q13304; baseline and differential.
DR   Genevisible; Q13304; HS.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0004950; F:chemokine receptor activity; TAS:ProtInc.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0033612; F:receptor serine/threonine kinase binding; IEA:Ensembl.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR   GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IEA:Ensembl.
DR   GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IBA:GO_Central.
DR   GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IBA:GO_Central.
DR   CDD; cd15161; 7tmA_GPR17; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24232; G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR24232:SF44; URACIL NUCLEOTIDE/CYSTEINYL LEUKOTRIENE RECEPTOR; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01157; P2YPURNOCPTR.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW   Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN           1..367
FT                   /note="Uracil nucleotide/cysteinyl leukotriene receptor"
FT                   /id="PRO_0000069536"
FT   TOPO_DOM        1..64
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        65..85
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        86..92
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..113
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        114..133
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..154
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        155..175
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        197..223
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        224..244
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        245..260
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        261..281
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        282..308
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        309..329
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        330..367
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        42
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        204
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        282
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        132..209
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   VAR_SEQ         1..28
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9523551"
FT                   /id="VSP_001987"
FT   CONFLICT        83
FT                   /note="L -> F (in Ref. 5; AAH31653)"
FT                   /evidence="ECO:0000305"
FT   HELIX           56..86
FT                   /evidence="ECO:0007829|PDB:7Y89"
FT   HELIX           93..109
FT                   /evidence="ECO:0007829|PDB:7Y89"
FT   HELIX           112..120
FT                   /evidence="ECO:0007829|PDB:7Y89"
FT   HELIX           129..161
FT                   /evidence="ECO:0007829|PDB:7Y89"
FT   HELIX           166..169
FT                   /evidence="ECO:0007829|PDB:7Y89"
FT   HELIX           173..189
FT                   /evidence="ECO:0007829|PDB:7Y89"
FT   HELIX           192..196
FT                   /evidence="ECO:0007829|PDB:7Y89"
FT   STRAND          210..213
FT                   /evidence="ECO:0007829|PDB:7Y89"
FT   HELIX           219..248
FT                   /evidence="ECO:0007829|PDB:7Y89"
FT   STRAND          254..258
FT                   /evidence="ECO:0007829|PDB:7Y89"
FT   HELIX           261..275
FT                   /evidence="ECO:0007829|PDB:7Y89"
FT   HELIX           277..288
FT                   /evidence="ECO:0007829|PDB:7Y89"
FT   TURN            289..292
FT                   /evidence="ECO:0007829|PDB:7Y89"
FT   HELIX           297..320
FT                   /evidence="ECO:0007829|PDB:7Y89"
FT   HELIX           321..323
FT                   /evidence="ECO:0007829|PDB:7Y89"
FT   HELIX           326..328
FT                   /evidence="ECO:0007829|PDB:7Y89"
FT   TURN            330..333
FT                   /evidence="ECO:0007829|PDB:7Y89"
FT   HELIX           334..341
FT                   /evidence="ECO:0007829|PDB:7Y89"
SQ   SEQUENCE   367 AA;  40989 MW;  132FBE97BE83C60C CRC64;
     MSKRSWWAGS RKPPREMLKL SGSDSSQSMN GLEVAPPGLI TNFSLATAEQ CGQETPLENM
     LFASFYLLDF ILALVGNTLA LWLFIRDHKS GTPANVFLMH LAVADLSCVL VLPTRLVYHF
     SGNHWPFGEI ACRLTGFLFY LNMYASIYFL TCISADRFLA IVHPVKSLKL RRPLYAHLAC
     AFLWVVVAVA MAPLLVSPQT VQTNHTVVCL QLYREKASHH ALVSLAVAFT FPFITTVTCY
     LLIIRSLRQG LRVEKRLKTK AVRMIAIVLA IFLVCFVPYH VNRSVYVLHY RSHGASCATQ
     RILALANRIT SCLTSLNGAL DPIMYFFVAE KFRHALCNLL CGKRLKGPPP SFEGKTNESS
     LSAKSEL
//