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   03-AUG-2022, entry version 85.
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.ENSSSCP00000013241; -.
DR   PaxDb; Q95N02; -.
DR   PRIDE; Q95N02; -.
DR   GeneID; 397242; -.
DR   KEGG; ssc:397242; -.
DR   CTD; 10800; -.
DR   eggNOG; ENOG502QUJU; Eukaryota.
DR   InParanoid; Q95N02; -.
DR   OrthoDB; 791328at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   InterPro; IPR013310; CLT1_recept.
DR   InterPro; IPR004071; Cyst_leuk_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01902; CYSLT1RECPTR.
DR   PRINTS; PR01533; CYSLTRECPTR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
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