ID LT4R1_HUMAN Reviewed; 352 AA. AC Q15722; Q13305; Q53XV5; Q92641; Q9BSU5; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 27-MAR-2024, entry version 202. DE RecName: Full=Leukotriene B4 receptor 1; DE Short=LTB4-R 1; DE Short=LTB4-R1; DE AltName: Full=Chemoattractant receptor-like 1; DE AltName: Full=G-protein coupled receptor 16; DE AltName: Full=P2Y purinoceptor 7; DE Short=P2Y7; GN Name=LTB4R; Synonyms=BLT, BLT1, BLTR, CMKRL1, GPR16, P2RY7; 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 [MRNA]. RX PubMed=8702478; DOI=10.1074/jbc.271.31.18363; RA Akbar G.K.M., Dasari V.R., Webb T., Ayyanathan K., Pillarisetti K., RA Sandhu A.K., Athwal R.S., Daniel J.L., Ashby B., Barnard E.A., RA Kunapuli S.P.; RT "Molecular cloning of a novel P2 purinoceptor from human erythroleukemia RT cells."; RL J. Biol. Chem. 271:18363-18367(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9177352; DOI=10.1038/42506; RA Yokomizo T., Izumi T., Chang K., Takuwa Y., Shimizu T.; RT "A G-protein-coupled receptor for leukotriene B4 that mediates RT chemotaxis."; RL Nature 387:620-624(1997). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8921391; DOI=10.1006/geno.1996.0541; RA Owman C.S.O., Nilsson C., Lolait S.J.; RT "Cloning of cDNA encoding a putative chemoattractant receptor."; RL Genomics 37:187-194(1996). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10934229; DOI=10.1084/jem.192.3.413; RA Kato K., Yokomizo T., Izumi T., Shimizu T.; RT "Cell-specific transcriptional regulation of human leukotriene B(4) RT receptor gene."; RL J. Exp. Med. 192:413-420(2000). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Kopatz S.A., Aronstam R.S., Sharma S.V.; RT "Isolation of complete coding sequence for leukotriene B4 receptor RT (LTB4R)."; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-346. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-346. RC TISSUE=Lung; 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 [9] RP PHOSPHORYLATION, AND MUTAGENESIS OF THR-308 AND SER-310. RX PubMed=12077128; DOI=10.1074/jbc.m202723200; RA Gaudreau R., Le Gouill C., Venne M.-H., Stankova J., Rola-Pleszczynski M.; RT "Threonine 308 within a putative casein kinase 2 site of the cytoplasmic RT tail of leukotriene B(4) receptor (BLT1) is crucial for ligand-induced, G- RT protein-coupled receptor-specific kinase 6-mediated desensitization."; RL J. Biol. Chem. 277:31567-31576(2002). CC -!- FUNCTION: Receptor for extracellular ATP > UTP and ADP. The activity of CC this receptor is mediated by G proteins which activate a CC phosphatidylinositol-calcium second messenger system. May be the CC cardiac P2Y receptor involved in the regulation of cardiac muscle CC contraction through modulation of L-type calcium currents. Is a CC receptor for leukotriene B4, a potent chemoattractant involved in CC inflammation and immune response. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Expressed at highest levels in heart, skeletal CC muscle and at lower levels in brain and liver. High level of expression CC in lymphoid tissues. CC -!- PTM: Phosphorylated by GRK6 upon leukotriene B4 binding; which promotes CC desensitization. {ECO:0000269|PubMed:12077128}. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC {ECO:0000255|PROSITE-ProRule:PRU00521}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB16747.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; U41070; AAC50628.1; -; mRNA. DR EMBL; U33448; AAB16747.1; ALT_INIT; Genomic_DNA. DR EMBL; D89079; BAA20424.1; -; mRNA. DR EMBL; D89078; BAA20423.1; -; mRNA. DR EMBL; X98356; CAA67001.1; -; mRNA. DR EMBL; AB008193; BAB00611.1; -; Genomic_DNA. DR EMBL; AY322535; AAP84348.1; -; Genomic_DNA. DR EMBL; BT007267; AAP35931.1; -; mRNA. DR EMBL; BC004545; AAH04545.1; -; mRNA. DR CCDS; CCDS9626.1; -. DR RefSeq; NP_001137391.1; NM_001143919.2. DR RefSeq; NP_858043.1; NM_181657.3. DR PDB; 7K15; X-ray; 2.88 A; A=5-310. DR PDB; 7VKT; EM; 2.90 A; A=1-352. DR PDBsum; 7K15; -. DR PDBsum; 7VKT; -. DR AlphaFoldDB; Q15722; -. DR EMDB; EMD-32018; -. DR SMR; Q15722; -. DR BioGRID; 107645; 10. DR IntAct; Q15722; 1. DR STRING; 9606.ENSP00000380008; -. DR BindingDB; Q15722; -. DR ChEMBL; CHEMBL3911; -. DR DrugBank; DB06248; Amelubant. DR DrugBank; DB12961; Leukotriene B4. DR DrugBank; DB09285; Morniflumate. DR DrugCentral; Q15722; -. DR GuidetoPHARMACOLOGY; 267; -. DR SwissLipids; SLP:000001555; -. DR TCDB; 9.A.14.13.5; the g-protein-coupled receptor (gpcr) family. DR GlyCosmos; Q15722; 2 sites, No reported glycans. DR GlyGen; Q15722; 2 sites. DR iPTMnet; Q15722; -. DR PhosphoSitePlus; Q15722; -. DR BioMuta; LTB4R; -. DR DMDM; 3041713; -. DR EPD; Q15722; -. DR jPOST; Q15722; -. DR MassIVE; Q15722; -. DR PaxDb; 9606-ENSP00000380008; -. DR PeptideAtlas; Q15722; -. DR ProteomicsDB; 60717; -. DR Antibodypedia; 193; 563 antibodies from 33 providers. DR DNASU; 1241; -. DR Ensembl; ENST00000345363.8; ENSP00000307445.3; ENSG00000213903.9. DR Ensembl; ENST00000396782.2; ENSP00000380002.2; ENSG00000213903.9. DR Ensembl; ENST00000396789.4; ENSP00000380008.4; ENSG00000213903.9. DR Ensembl; ENST00000646659.1; ENSP00000495785.1; ENSG00000285456.2. DR Ensembl; ENST00000646739.1; ENSP00000494730.1; ENSG00000285456.2. DR Ensembl; ENST00000647085.2; ENSP00000495466.1; ENSG00000285456.2. DR GeneID; 1241; -. DR KEGG; hsa:1241; -. DR MANE-Select; ENST00000345363.8; ENSP00000307445.3; NM_001143919.3; NP_001137391.1. DR UCSC; uc001wos.4; human. DR AGR; HGNC:6713; -. DR CTD; 1241; -. DR DisGeNET; 1241; -. DR GeneCards; LTB4R; -. DR HGNC; HGNC:6713; LTB4R. DR HPA; ENSG00000213903; Tissue enhanced (esophagus, skin). DR MIM; 601531; gene. DR neXtProt; NX_Q15722; -. DR OpenTargets; ENSG00000213903; -. DR PharmGKB; PA30476; -. DR VEuPathDB; HostDB:ENSG00000213903; -. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT00950000182966; -. DR HOGENOM; CLU_009579_8_0_1; -. DR InParanoid; Q15722; -. DR OMA; QRMRTKR; -. DR OrthoDB; 4266448at2759; -. DR PhylomeDB; Q15722; -. DR TreeFam; TF330976; -. DR PathwayCommons; Q15722; -. DR Reactome; R-HSA-391906; Leukotriene receptors. DR Reactome; R-HSA-416476; G alpha (q) signalling events. DR SignaLink; Q15722; -. DR SIGNOR; Q15722; -. DR BioGRID-ORCS; 1241; 27 hits in 1160 CRISPR screens. DR ChiTaRS; LTB4R; human. DR GeneWiki; Leukotriene_B4_receptor; -. DR GenomeRNAi; 1241; -. DR Pharos; Q15722; Tchem. DR PRO; PR:Q15722; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q15722; Protein. DR Bgee; ENSG00000213903; Expressed in lower esophagus mucosa and 99 other cell types or tissues. DR ExpressionAtlas; Q15722; baseline and differential. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central. DR GO; GO:0001632; F:leukotriene B4 receptor activity; IBA:GO_Central. DR GO; GO:0004974; F:leukotriene receptor activity; TAS:ProtInc. DR GO; GO:0000166; F:nucleotide binding; TAS:ProtInc. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc. DR GO; GO:0006955; P:immune response; TAS:ProtInc. DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc. DR GO; GO:0006936; P:muscle contraction; TAS:ProtInc. DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central. DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; TAS:ProtInc. DR CDD; cd15121; 7tmA_LTB4R1; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR000826; Formyl_rcpt-rel. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR InterPro; IPR003981; Leukotriene_B4_rcpt. DR InterPro; IPR003983; Leukotriene_B4_typ-1_rcpt. DR PANTHER; PTHR24225; CHEMOTACTIC RECEPTOR; 1. DR PANTHER; PTHR24225:SF62; G_PROTEIN_RECEP_F1_2 DOMAIN-CONTAINING PROTEIN-RELATED; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR01477; LTB1RECEPTOR. DR PRINTS; PR01476; LTBRECEPTOR. 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. DR Genevisible; Q15722; HS. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; G-protein coupled receptor; Glycoprotein; KW Membrane; Phosphoprotein; Receptor; Reference proteome; Transducer; KW Transmembrane; Transmembrane helix. FT CHAIN 1..352 FT /note="Leukotriene B4 receptor 1" FT /id="PRO_0000069708" FT TOPO_DOM 1..19 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 20..42 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 43..54 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 55..75 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 76..91 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 92..113 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 114..138 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 139..159 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 160..178 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 179..199 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 200..221 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 222..242 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 243..268 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 269..289 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 290..352 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 310..352 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 337..352 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 2 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 164 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VARIANT 346 FT /note="L -> F (in dbSNP:rs17849864)" FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.7" FT /id="VAR_060679" FT MUTAGEN 308 FT /note="T->P,A: No effect on affinity for leukotriene B4, FT induces resistance to desensitization by GRK6, but minor FT effect on phosphorylation by GRK6." FT /evidence="ECO:0000269|PubMed:12077128" FT MUTAGEN 310 FT /note="S->A: No effect on affinity for leukotriene B4 or on FT desensitization by GRK6." FT /evidence="ECO:0000269|PubMed:12077128" FT CONFLICT 246 FT /note="G -> R (in Ref. 4; CAA67001)" FT /evidence="ECO:0000305" FT CONFLICT 272 FT /note="A -> V (in Ref. 1; AAC50628)" FT /evidence="ECO:0000305" FT CONFLICT 293 FT /note="L -> V (in Ref. 1; AAC50628)" FT /evidence="ECO:0000305" FT HELIX 14..44 FT /evidence="ECO:0007829|PDB:7K15" FT HELIX 52..68 FT /evidence="ECO:0007829|PDB:7K15" FT HELIX 71..80 FT /evidence="ECO:0007829|PDB:7K15" FT HELIX 86..120 FT /evidence="ECO:0007829|PDB:7K15" FT HELIX 122..128 FT /evidence="ECO:0007829|PDB:7K15" FT HELIX 131..148 FT /evidence="ECO:0007829|PDB:7K15" FT HELIX 152..155 FT /evidence="ECO:0007829|PDB:7K15" FT STRAND 156..160 FT /evidence="ECO:0007829|PDB:7K15" FT STRAND 166..170 FT /evidence="ECO:0007829|PDB:7K15" FT HELIX 175..189 FT /evidence="ECO:0007829|PDB:7K15" FT HELIX 191..208 FT /evidence="ECO:0007829|PDB:7K15" FT HELIX 221..249 FT /evidence="ECO:0007829|PDB:7K15" FT STRAND 257..259 FT /evidence="ECO:0007829|PDB:7K15" FT HELIX 260..277 FT /evidence="ECO:0007829|PDB:7K15" FT HELIX 280..292 FT /evidence="ECO:0007829|PDB:7K15" FT HELIX 294..296 FT /evidence="ECO:0007829|PDB:7K15" FT HELIX 298..305 FT /evidence="ECO:0007829|PDB:7K15" FT STRAND 307..309 FT /evidence="ECO:0007829|PDB:7K15" SQ SEQUENCE 352 AA; 37557 MW; 5A7BFC0A659AC81C CRC64; MNTTSSAAPP SLGVEFISLL AIILLSVALA VGLPGNSFVV WSILKRMQKR SVTALMVLNL ALADLAVLLT APFFLHFLAQ GTWSFGLAGC RLCHYVCGVS MYASVLLITA MSLDRSLAVA RPFVSQKLRT KAMARRVLAG IWVLSFLLAT PVLAYRTVVP WKTNMSLCFP RYPSEGHRAF HLIFEAVTGF LLPFLAVVAS YSDIGRRLQA RRFRRSRRTG RLVVLIILTF AAFWLPYHVV NLAEAGRALA GQAAGLGLVG KRLSLARNVL IALAFLSSSV NPVLYACAGG GLLRSAGVGF VAKLLEGTGS EASSTRRGGS LGQTARSGPA ALEPGPSESL TASSPLKLNE LN //