ID CLTR1_MOUSE Reviewed; 352 AA.
AC Q99JA4; Q544P1; Q9JJ71; Q9JK47;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 163.
DE RecName: Full=Cysteinyl leukotriene receptor 1;
DE Short=CysLTR1;
DE AltName: Full=Cysteinyl leukotriene D4 receptor;
DE Short=LTD4 receptor;
GN Name=Cysltr1; Synonyms=Cyslt1, Cyslt1r;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RC STRAIN=129/Sv;
RX PubMed=11226226; DOI=10.1073/pnas.041624398;
RA Maekawa A., Kanaoka Y., Lam B.K., Austen K.F.;
RT "Identification in mice of two isoforms of the cysteinyl leukotriene 1
RT receptor that result from alternative splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:2256-2261(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Trachea;
RX PubMed=11705452; DOI=10.1016/s0006-2952(01)00774-2;
RA Martin V., Sawyer N., Stocco R., Unett D., Lerner M.R., Abramovitz M.,
RA Funk C.D.;
RT "Molecular cloning and functional characterization of murine cysteinyl-
RT leukotriene 1 (CysLT1) receptors.";
RL Biochem. Pharmacol. 62:1193-1200(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Blood;
RX PubMed=11342226; DOI=10.1016/s0167-4781(00)00271-2;
RA Mollerup J., Jorgensen S.T., Hougaard C., Hoffmann E.K.;
RT "Identification of a murine cysteinyl leukotriene receptor by expression in
RT Xenopus laevis oocytes.";
RL Biochim. Biophys. Acta 1517:455-459(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=T-cell;
RA Ogasawara H., Izumi T., Shimizu T.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Colon;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary gland;
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).
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. The rank order of
CC affinities for the leukotrienes is LTD4 >> LTE4 = LTC4 >> LTB4.
CC -!- INTERACTION:
CC Q99JA4; Q6NS65: Gpr17; NbExp=2; IntAct=EBI-15791392, EBI-15791369;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Long;
CC IsoId=Q99JA4-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=Q99JA4-2; Sequence=VSP_001921;
CC -!- TISSUE SPECIFICITY: Widely expressed, with higher expression in the
CC lung and skin, intermediate levels in the heart, kidney and stomach and
CC lower levels in several other tissues. Isoform 1 is the most abundant
CC form in all tested tissues.
CC -!- MISCELLANEOUS: MK-571, a selective antagonist, was shown to inhibit
CC eosinophilia, bronchial hyperreactivity and microvascular leakage.
CC Zafirlukast (Accolate) and pranlukast (Onon) were also shown to be
CC selective antagonists.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF329272; AAK16715.1; -; Genomic_DNA.
DR EMBL; AF329272; AAK16716.1; -; Genomic_DNA.
DR EMBL; AF205830; AAK15433.1; -; mRNA.
DR EMBL; AF263370; AAF73047.1; -; mRNA.
DR EMBL; AB044087; BAA96809.1; -; mRNA.
DR EMBL; AK033476; BAC28308.1; -; mRNA.
DR EMBL; AL732460; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027102; AAH27102.1; -; mRNA.
DR CCDS; CCDS41098.1; -. [Q99JA4-1]
DR RefSeq; NP_001268788.1; NM_001281859.1. [Q99JA4-1]
DR RefSeq; NP_001268791.1; NM_001281862.1. [Q99JA4-2]
DR RefSeq; NP_067451.2; NM_021476.5. [Q99JA4-1]
DR AlphaFoldDB; Q99JA4; -.
DR SMR; Q99JA4; -.
DR BioGRID; 208449; 1.
DR DIP; DIP-48916N; -.
DR IntAct; Q99JA4; 1.
DR STRING; 10090.ENSMUSP00000109108; -.
DR BindingDB; Q99JA4; -.
DR ChEMBL; CHEMBL3808269; -.
DR GlyCosmos; Q99JA4; 4 sites, No reported glycans.
DR GlyGen; Q99JA4; 4 sites.
DR iPTMnet; Q99JA4; -.
DR PhosphoSitePlus; Q99JA4; -.
DR jPOST; Q99JA4; -.
DR PaxDb; 10090-ENSMUSP00000109108; -.
DR Antibodypedia; 548; 350 antibodies from 31 providers.
DR DNASU; 58861; -.
DR Ensembl; ENSMUST00000064892.4; ENSMUSP00000063520.4; ENSMUSG00000052821.4. [Q99JA4-1]
DR Ensembl; ENSMUST00000113480.2; ENSMUSP00000109108.2; ENSMUSG00000052821.4. [Q99JA4-1]
DR GeneID; 58861; -.
DR KEGG; mmu:58861; -.
DR UCSC; uc009ubt.2; mouse. [Q99JA4-1]
DR AGR; MGI:1926218; -.
DR CTD; 10800; -.
DR MGI; MGI:1926218; Cysltr1.
DR VEuPathDB; HostDB:ENSMUSG00000052821; -.
DR eggNOG; ENOG502QUJU; Eukaryota.
DR GeneTree; ENSGT01100000263536; -.
DR HOGENOM; CLU_009579_8_2_1; -.
DR InParanoid; Q99JA4; -.
DR OMA; FMPYHVQ; -.
DR OrthoDB; 2875155at2759; -.
DR PhylomeDB; Q99JA4; -.
DR TreeFam; TF350009; -.
DR Reactome; R-MMU-391906; Leukotriene receptors.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 58861; 2 hits in 76 CRISPR screens.
DR PRO; PR:Q99JA4; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q99JA4; Protein.
DR Bgee; ENSMUSG00000052821; Expressed in epiblast cell in embryo and 96 other cell types or tissues.
DR Genevisible; Q99JA4; MM.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0001631; F:cysteinyl leukotriene receptor activity; IBA:GO_Central.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0004974; F:leukotriene receptor activity; IDA:MGI.
DR GO; GO:0006816; P:calcium ion transport; IDA:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:MGI.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0006935; P:chemotaxis; IDA:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IDA:MGI.
DR GO; GO:0002437; P:inflammatory response to antigenic stimulus; IMP:MGI.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; ISO:MGI.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; ISO:MGI.
DR CDD; cd15158; 7tmA_CysLTR1; 1.
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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..352
FT /note="Cysteinyl leukotriene receptor 1"
FT /id="PRO_0000069300"
FT TOPO_DOM 1..43
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..121
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..208
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..291
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 111..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 1..13
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_001921"
FT CONFLICT 176
FT /note="Y -> D (in Ref. 3; AAF73047)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 352 AA; 40715 MW; 5BDC94B3F1CD0CAB CRC64;
MYLQGTKQTF LENMNGTENL TTSLINNTCH DTIDEFRNQV YSTMYSVISV VGFFGNSFVL
YVLIKTYHEK SAFQVYMINL AIADLLCVCT LPLRVVYYVH KGKWLFGDFL CRLTTYALYV
NLYCSIFFMT AMSFFRCVAI VFPVQNINLV TQKKARFVCI GIWIFVILTS SPFLMYKSYQ
DEKNNTKCFE PPQNNQAKKY VLILHYVSLF FGFIIPFVTI IVCYTMIILT LLKNTMKKNM
PSRRKAIGMI IVVTAAFLVS FMPYHIQRTI HLHLLHSETR PCDSVLRMQK SVVITLSLAA
SNCCFDPLLY FFSGGNFRRR LSTFRKHSLS SMTYVPKKKA SLPEKGEEIC NE
//
