ID CLTR1_PIG Reviewed; 340 AA. AC Q95N02; DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 24-JAN-2024, entry version 91. DE RecName: Full=Cysteinyl leukotriene receptor 1; DE Short=CysLTR1; GN Name=CYSLTR1; Synonyms=CYSLT1; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Takasaki J., Kamohara M., Saito T., Matsumoto M., Matsumoto S., Ohishi T., RA Soga T., Matsushime H., Furuichi K.; RT "Characterization of cloned rat and porcine cysteinyl leukotriene RT receptors."; RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Receptor for cysteinyl leukotrienes mediating constriction of CC the microvascular smooth muscle during an inflammatory response. This CC response is mediated via a G-protein that activates a CC phosphatidylinositol-calcium second messenger system (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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB052686; BAB60826.1; -; mRNA. DR RefSeq; NP_999294.1; NM_214129.1. DR STRING; 9823.ENSSSCP00000034195; -. DR GlyCosmos; Q95N02; 4 sites, No reported glycans. DR PaxDb; 9823-ENSSSCP00000013241; -. DR GeneID; 397242; -. DR KEGG; ssc:397242; -. DR CTD; 10800; -. DR eggNOG; ENOG502QUJU; Eukaryota. DR InParanoid; Q95N02; -. DR OrthoDB; 2875155at2759; -. DR Proteomes; UP000008227; Unplaced. DR Proteomes; UP000314985; Unplaced. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; Unplaced. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0004974; F:leukotriene receptor activity; IEA:InterPro. DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR013310; CLT1_recept. DR InterPro; IPR004071; Cyst_leuk_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR PANTHER; PTHR24231:SF45; CYSTEINYL LEUKOTRIENE RECEPTOR 1; 1. DR PANTHER; PTHR24231; PURINOCEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR01902; CYSLT1RECPTR. DR PRINTS; PR01533; CYSLTRECPTR. DR PRINTS; PR00237; GPCRRHODOPSN. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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..340 FT /note="Cysteinyl leukotriene receptor 1" FT /id="PRO_0000069301" FT TOPO_DOM 1..31 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 32..52 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 53..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..109 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 110..130 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 131..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..196 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 197..217 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 218..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..279 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 280..300 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 301..340 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT CARBOHYD 6 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 18 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 172 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 265 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 99..176 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" SQ SEQUENCE 340 AA; 38989 MW; 54F9372A121CE413 CRC64; MDGVRNLTVS CASSNTCNDT IDDFRNQVYS TLYSMITVVG FFGNGFVLYV LIKTYHEKSA YQVYMINLAV ADLLCVCTLP LRVVYYVHKG IWLFGDFLCR LSTYALYVNL YCSIFFMTAM SFFRCIAIVF PVQNINLITH KKAKIVCIAI WIFVILTSSP FLMSTSYKDE KNNTKCFEPP QXNQAKYHVL VLHYVSLFVG FIIPFVIIIV CYTMIILTLL KNSMKKNISS RKKAIGMIIV VTAAFLISFM PYHIQRTIHL HFLHNDTKHC DSVLRMQKSV XITLSLAASN CCFDPLLYFF SGGNFREGLS TFRKHSLSTM TYVPKKKTSL PEKAQEIYKE //