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LT4R1_HUMAN
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   03-AUG-2022, entry version 193.
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};
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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   SMR; Q15722; -.
DR   BioGRID; 107645; 10.
DR   IntAct; Q15722; 2.
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   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; Q15722; -.
DR   PeptideAtlas; Q15722; -.
DR   PRIDE; Q15722; -.
DR   ProteomicsDB; 60717; -.
DR   Antibodypedia; 193; 533 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   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; CRLRSAM; -.
DR   OrthoDB; 978296at2759; -.
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 1080 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 97 other tissues.
DR   ExpressionAtlas; Q15722; baseline and differential.
DR   Genevisible; Q15722; HS.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
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   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; PTHR24230:SF51; PTHR24230:SF51; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01477; LTB1RECEPTOR.
DR   PRINTS; PR01476; LTBRECEPTOR.
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; 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
 
 
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