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Cannabinoid receptor 2 (CB-2) (CB2) (hCB2) (CX5)

 CNR2_HUMAN              Reviewed;         360 AA.
P34972; C6ES44; Q4VBK8; Q5JRH7; Q6B0G7; Q6NSY0;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
12-SEP-2018, entry version 164.
RecName: Full=Cannabinoid receptor 2;
Short=CB-2;
Short=CB2;
Short=hCB2;
AltName: Full=CX5;
Name=CNR2; Synonyms=CB2A, CB2B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7689702; DOI=10.1038/365061a0;
Munro S., Thomas K.L., Abu-Shaar M.;
"Molecular characterization of a peripheral receptor for
cannabinoids.";
Nature 365:61-65(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Spleen;
PubMed=19496827; DOI=10.1111/j.1601-183X.2009.00498.x;
Liu Q.-R., Pan C.H., Hishimoto A., Li C.Y., Xi Z.X.,
Llorente-Berzal A., Viveros M.P., Ishiguro H., Arinami T.,
Onaivi E.S., Uhl G.R.;
"Species differences in cannabinoid receptor 2 (CNR2 gene):
identification of novel human and rodent CB2 isoforms, differential
tissue expression and regulation by cannabinoid receptor ligands.";
Genes Brain Behav. 8:519-530(2009).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Blood;
Bruess M., Boenisch H.;
"Cannabinoid receptors and their genes.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Warren C.N., Aronstam R.S., Sharma S.V.;
"Isolation of complete coding sequence for cannabinoid receptor 2
(CNR2).";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT TYR-316.
TISSUE=Blood;
Saravanan T., Chugh A., Kant R.;
"Amplification and cloning of human cannabinoid receptor 2 gene from
Asiatic origin.";
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-63 AND
TYR-316.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
TISSUE SPECIFICITY.
PubMed=7556170; DOI=10.1111/j.1432-1033.1995.tb20780.x;
Galiegue S., Mary S., Marchand J., Dussossoy D., Carriere D.,
Carayon P., Bouaboula M., Shire D., Le Fur G., Casellas P.;
"Expression of central and peripheral cannabinoid receptors in human
immune tissues and leukocyte subpopulations.";
Eur. J. Biochem. 232:54-61(1995).
[10]
PHOSPHORYLATION AT SER-352, AND SUBCELLULAR LOCATION.
PubMed=10400664; DOI=10.1074/jbc.274.29.20397;
Bouaboula M., Dussossoy D., Casellas P.;
"Regulation of peripheral cannabinoid receptor CB2 phosphorylation by
the inverse agonist SR 144528. Implications for receptor biological
responses.";
J. Biol. Chem. 274:20397-20405(1999).
[11]
FUNCTION, AND MUTAGENESIS OF LYS-109 AND SER-112.
PubMed=10051546;
Tao Q., McAllister S.D., Andreassi J., Nowell K.W., Cabral G.A.,
Hurst D.P., Bachtel K., Ekman M.C., Reggio P.H., Abood M.E.;
"Role of a conserved lysine residue in the peripheral cannabinoid
receptor (CB2): evidence for subtype specificity.";
Mol. Pharmacol. 55:605-613(1999).
[12]
IDENTIFICATION OF 2-ARACHIDONOYLGLYCEROL AS AN ENDOGENOUS LIGAND.
PubMed=10617657; DOI=10.1074/jbc.275.1.605;
Sugiura T., Kondo S., Kishimoto S., Miyashita T., Nakane S.,
Kodaka T., Suhara Y., Takayama H., Waku K.;
"Evidence that 2-arachidonoylglycerol but not N-palmitoylethanolamine
or anandamide is the physiological ligand for the cannabinoid CB2
receptor. Comparison of the agonistic activities of various
cannabinoid receptor ligands in HL-60 cells.";
J. Biol. Chem. 275:605-612(2000).
[13]
TISSUE SPECIFICITY.
PubMed=12153574; DOI=10.1046/j.1432-1033.2002.03078.x;
Matias I., Pochard P., Orlando P., Salzet M., Pestel J., Di Marzo V.;
"Presence and regulation of the endocannabinoid system in human
dendritic cells.";
Eur. J. Biochem. 269:3771-3778(2002).
[14]
MUTAGENESIS OF LEU-201 AND TYR-207.
PubMed=12417328; DOI=10.1016/S0014-5793(02)03537-8;
Song Z.H., Feng W.;
"Absence of a conserved proline and presence of a conserved tyrosine
in the CB2 cannabinoid receptor are crucial for its function.";
FEBS Lett. 531:290-294(2002).
[15]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-130; ARG-131
AND ALA-244.
PubMed=12663043; DOI=10.1016/S0006-2952(03)00005-4;
Feng W., Song Z.H.;
"Effects of D3.49A, R3.50A, and A6.34E mutations on ligand binding and
activation of the cannabinoid-2 (CB2) receptor.";
Biochem. Pharmacol. 65:1077-1085(2003).
[16]
FUNCTION.
PubMed=12711605; DOI=10.1074/jbc.M301359200;
Kishimoto S., Gokoh M., Oka S., Muramatsu M., Kajiwara T., Waku K.,
Sugiura T.;
"2-arachidonoylglycerol induces the migration of HL-60 cells
differentiated into macrophage-like cells and human peripheral blood
monocytes through the cannabinoid CB2 receptor-dependent mechanism.";
J. Biol. Chem. 278:24469-24475(2003).
[17]
TISSUE SPECIFICITY.
PubMed=12511587; DOI=10.1172/JCI200316116;
Casanova M.L., Blazquez C., Martinez-Palacio J., Villanueva C.,
Fernandez-Acenero M.J., Huffman J.W., Jorcano J.L., Guzman M.;
"Inhibition of skin tumor growth and angiogenesis in vivo by
activation of cannabinoid receptors.";
J. Clin. Invest. 111:43-50(2003).
[18]
TISSUE SPECIFICITY.
PubMed=14657172;
Benito C., Nunez E., Tolon R.M., Carrier E.J., Rabano A.,
Hillard C.J., Romero J.;
"Cannabinoid CB2 receptors and fatty acid amide hydrolase are
selectively overexpressed in neuritic plaque-associated glia in
Alzheimer's disease brains.";
J. Neurosci. 23:11136-11141(2003).
[19]
TISSUE SPECIFICITY.
PubMed=15266552; DOI=10.1002/syn.20050;
Nunez E., Benito C., Pazos M.R., Barbachano A., Fajardo O.,
Gonzalez S., Tolon R.M., Romero J.;
"Cannabinoid CB2 receptors are expressed by perivascular microglial
cells in the human brain: an immunohistochemical study.";
Synapse 53:208-213(2004).
[20]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=18692962; DOI=10.1016/j.pain.2008.06.007;
Anand U., Otto W.R., Sanchez-Herrera D., Facer P., Yiangou Y.,
Korchev Y., Birch R., Benham C., Bountra C., Chessell I.P., Anand P.;
"Cannabinoid receptor CB2 localisation and agonist-mediated inhibition
of capsaicin responses in human sensory neurons.";
Pain 138:667-680(2008).
[21]
INDUCTION BY ENDOCANNABINOID ANANDAMIDE.
PubMed=23955712; DOI=10.1038/nm.3265;
Jourdan T., Godlewski G., Cinar R., Bertola A., Szanda G., Liu J.,
Tam J., Han T., Mukhopadhyay B., Skarulis M.C., Ju C., Aouadi M.,
Czech M.P., Kunos G.;
"Activation of the Nlrp3 inflammasome in infiltrating macrophages by
endocannabinoids mediates beta cell loss in type 2 diabetes.";
Nat. Med. 19:1132-1140(2013).
[22]
STRUCTURE BY NMR OF 240-272.
PubMed=19397896; DOI=10.1016/j.bbrc.2009.04.099;
Tiburu E.K., Tyukhtenko S., Deshmukh L., Vinogradova O., Janero D.R.,
Makriyannis A.;
"Structural biology of human cannabinoid receptor-2 helix 6 in
membrane-mimetic environments.";
Biochem. Biophys. Res. Commun. 384:243-248(2009).
[23]
VARIANTS ARG-63 AND TYR-316.
PubMed=18286196; DOI=10.1371/journal.pone.0001640;
Onaivi E.S., Ishiguro H., Gong J.-P., Patel S., Meozzi P.A., Myers L.,
Perchuk A., Mora Z., Tagliaferro P.A., Gardner E., Brusco A.,
Akinshola B.E., Hope B., Lujilde J., Inada T., Iwasaki S.,
Macharia D., Teasenfitz L., Arinami T., Uhl G.R.;
"Brain neuronal CB2 cannabinoid receptors in drug abuse and
depression: from mice to human subjects.";
PLoS ONE 3:E1640-E1640(2008).
-!- FUNCTION: Heterotrimeric G protein-coupled receptor for
endocannabinoid 2-arachidonoylglycerol mediating inhibition of
adenylate cyclase. May function in inflammatory response,
nociceptive transmission and bone homeostasis.
{ECO:0000269|PubMed:10051546, ECO:0000269|PubMed:12663043,
ECO:0000269|PubMed:12711605, ECO:0000269|PubMed:18692962}.
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
Cell projection, dendrite {ECO:0000250}. Perikaryon {ECO:0000250}.
Note=Localizes to apical dendrite of pyramidal neurons.
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Preferentially expressed in cells of the
immune system with higher expression in B-cells and NK cells (at
protein level). Expressed in skin in suprabasal layers and hair
follicles (at protein level). Highly expressed in tonsil and to a
lower extent in spleen, peripheral blood mononuclear cells, and
thymus. PubMed:14657172 could not detect expression in normal
brain. Expressed in brain by perivascular microglial cells and
dorsal root ganglion sensory neurons (at protein level). Two
isoforms are produced by alternative promoter usage and differ
only in the 5' UTR: isoform CB2A is observed predominantly in
testis with some expression in brain, while isoform CB2B is
predominant in spleen and leukocytes.
{ECO:0000269|PubMed:12153574, ECO:0000269|PubMed:12511587,
ECO:0000269|PubMed:14657172, ECO:0000269|PubMed:15266552,
ECO:0000269|PubMed:18692962, ECO:0000269|PubMed:19496827,
ECO:0000269|PubMed:7556170}.
-!- INDUCTION: In macrophages, down-regulated by endocannabinoid
anandamide/AEA. {ECO:0000269|PubMed:23955712}.
-!- PTM: Constitutively phosphorylated on Ser-352; phosphorylation
increases cell internalization and desensitizes the receptor.
{ECO:0000269|PubMed:10400664}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
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EMBL; X74328; CAA52376.1; -; mRNA.
EMBL; EU517121; ACD31539.1; -; mRNA.
EMBL; AJ430063; CAD22548.1; -; mRNA.
EMBL; AJ430064; CAD22549.1; -; Genomic_DNA.
EMBL; AY242132; AAO92299.1; -; Genomic_DNA.
EMBL; AM156854; CAJ42137.1; -; mRNA.
EMBL; AM156855; CAJ42138.1; -; mRNA.
EMBL; AM156856; CAJ42139.1; -; mRNA.
EMBL; AL590609; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471134; EAW95099.1; -; Genomic_DNA.
EMBL; BC069722; AAH69722.1; -; mRNA.
EMBL; BC074767; AAH74767.1; -; mRNA.
EMBL; BC095545; AAH95545.1; -; mRNA.
CCDS; CCDS245.1; -.
PIR; S36750; S36750.
RefSeq; NP_001832.1; NM_001841.2.
RefSeq; XP_011538931.1; XM_011540629.2.
RefSeq; XP_016855750.1; XM_017000261.1.
UniGene; Hs.73037; -.
PDB; 2KI9; NMR; -; A=240-272.
PDBsum; 2KI9; -.
ProteinModelPortal; P34972; -.
SMR; P34972; -.
IntAct; P34972; 23.
STRING; 9606.ENSP00000363596; -.
BindingDB; P34972; -.
ChEMBL; CHEMBL253; -.
DrugBank; DB00470; Dronabinol.
DrugBank; DB00486; Nabilone.
GuidetoPHARMACOLOGY; 57; -.
SwissLipids; SLP:000001608; -.
TCDB; 9.A.14.2.6; the g-protein-coupled receptor (gpcr) family.
iPTMnet; P34972; -.
PhosphoSitePlus; P34972; -.
BioMuta; CNR2; -.
DMDM; 461697; -.
EPD; P34972; -.
MaxQB; P34972; -.
PaxDb; P34972; -.
PeptideAtlas; P34972; -.
PRIDE; P34972; -.
ProteomicsDB; 54964; -.
DNASU; 1269; -.
Ensembl; ENST00000374472; ENSP00000363596; ENSG00000188822.
GeneID; 1269; -.
KEGG; hsa:1269; -.
UCSC; uc001bif.4; human.
CTD; 1269; -.
DisGeNET; 1269; -.
EuPathDB; HostDB:ENSG00000188822.7; -.
GeneCards; CNR2; -.
H-InvDB; HIX0160038; -.
HGNC; HGNC:2160; CNR2.
HPA; CAB009719; -.
MIM; 605051; gene.
neXtProt; NX_P34972; -.
OpenTargets; ENSG00000188822; -.
PharmGKB; PA26682; -.
eggNOG; KOG3656; Eukaryota.
eggNOG; ENOG410XRW9; LUCA.
GeneTree; ENSGT00760000118804; -.
HOGENOM; HOG000049272; -.
HOVERGEN; HBG051045; -.
InParanoid; P34972; -.
KO; K04278; -.
OMA; VNFHVFH; -.
OrthoDB; EOG091G05O3; -.
PhylomeDB; P34972; -.
TreeFam; TF330052; -.
Reactome; R-HSA-373076; Class A/1 (Rhodopsin-like receptors).
Reactome; R-HSA-418594; G alpha (i) signalling events.
EvolutionaryTrace; P34972; -.
GeneWiki; Cannabinoid_receptor_type_2; -.
GenomeRNAi; 1269; -.
PRO; PR:P34972; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000188822; Expressed in 36 organ(s), highest expression level in spleen.
CleanEx; HS_CNR2; -.
ExpressionAtlas; P34972; baseline and differential.
Genevisible; P34972; HS.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0004949; F:cannabinoid receptor activity; TAS:ProtInc.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0007187; P:G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; TAS:ProtInc.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0030595; P:leukocyte chemotaxis; IEA:Ensembl.
GO; GO:0045759; P:negative regulation of action potential; IEA:Ensembl.
GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
GO; GO:0033004; P:negative regulation of mast cell activation; IEA:Ensembl.
GO; GO:0051001; P:negative regulation of nitric-oxide synthase activity; IEA:Ensembl.
GO; GO:0032229; P:negative regulation of synaptic transmission, GABAergic; IEA:Ensembl.
GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
CDD; cd15341; 7tmA_CB2; 1.
InterPro; IPR001551; Canbinoid_rcpt_2.
InterPro; IPR002230; Cnbnoid_rcpt.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
PANTHER; PTHR22750:SF10; PTHR22750:SF10; 1.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00523; CANABINOID2R.
PRINTS; PR00362; CANNABINOIDR.
PRINTS; PR00237; GPCRRHODOPSN.
SMART; SM01381; 7TM_GPCR_Srsx; 1.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Cell projection; Complete proteome;
G-protein coupled receptor; Glycoprotein; Inflammatory response;
Membrane; Phosphoprotein; Polymorphism; Receptor; Reference proteome;
Transducer; Transmembrane; Transmembrane helix.
CHAIN 1 360 Cannabinoid receptor 2.
/FTId=PRO_0000069323.
TOPO_DOM 1 33 Extracellular. {ECO:0000255}.
TRANSMEM 34 59 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 60 71 Cytoplasmic. {ECO:0000255}.
TRANSMEM 72 92 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 93 104 Extracellular. {ECO:0000255}.
TRANSMEM 105 129 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 130 149 Cytoplasmic. {ECO:0000255}.
TRANSMEM 150 172 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 173 188 Extracellular. {ECO:0000255}.
TRANSMEM 189 214 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 215 246 Cytoplasmic. {ECO:0000255}.
TRANSMEM 247 267 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 268 279 Extracellular. {ECO:0000255}.
TRANSMEM 280 301 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 302 360 Cytoplasmic. {ECO:0000255}.
MOD_RES 335 335 Phosphoserine.
{ECO:0000250|UniProtKB:P47936}.
MOD_RES 336 336 Phosphoserine.
{ECO:0000250|UniProtKB:P47936}.
MOD_RES 338 338 Phosphothreonine.
{ECO:0000250|UniProtKB:P47936}.
MOD_RES 352 352 Phosphoserine.
{ECO:0000269|PubMed:10400664}.
CARBOHYD 11 11 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 63 63 Q -> R (high incidence in Japanese
depressed subjects; dbSNP:rs2501432).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:18286196}.
/FTId=VAR_054310.
VARIANT 316 316 H -> Y (in dbSNP:rs2229579).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:18286196,
ECO:0000269|Ref.5}.
/FTId=VAR_029209.
MUTAGEN 109 109 K->A: No effect on agonist binding.
Affects cannabinoid agonist binding; when
associated with G-112.
{ECO:0000269|PubMed:10051546}.
MUTAGEN 109 109 K->R: No effect on agonist binding.
{ECO:0000269|PubMed:10051546}.
MUTAGEN 112 112 S->G: Affects cannabinoid agonist
binding; when associated with A-109.
{ECO:0000269|PubMed:10051546}.
MUTAGEN 130 130 D->A: Loss of ligand binding. Alters
agonist-induced inhibitory effect on
adenylate cyclase.
{ECO:0000269|PubMed:12663043}.
MUTAGEN 131 131 R->A: No effect on ligand binding. Alters
agonist-induced inhibitory effect on
adenylate cyclase.
{ECO:0000269|PubMed:12663043}.
MUTAGEN 201 201 L->P: Abolishes ligand binding and
agonist-induced inhibitory effect on
adenylate cyclase.
{ECO:0000269|PubMed:12417328}.
MUTAGEN 207 207 Y->A: Abolishes agonist-induced
inhibitory effect on adenylate cyclase.
No effect on ligand binding.
{ECO:0000269|PubMed:12417328}.
MUTAGEN 244 244 A->E: Loss of ligand binding. Alters
agonist-induced inhibitory effect on
adenylate cyclase.
{ECO:0000269|PubMed:12663043}.
CONFLICT 173 173 T -> A (in Ref. 8; AAH95545).
{ECO:0000305}.
CONFLICT 307 307 R -> H (in Ref. 8; AAH69722).
{ECO:0000305}.
STRAND 242 245 {ECO:0000244|PDB:2KI9}.
HELIX 246 254 {ECO:0000244|PDB:2KI9}.
TURN 255 257 {ECO:0000244|PDB:2KI9}.
STRAND 258 260 {ECO:0000244|PDB:2KI9}.
HELIX 261 265 {ECO:0000244|PDB:2KI9}.
TURN 266 269 {ECO:0000244|PDB:2KI9}.
SEQUENCE 360 AA; 39681 MW; A7ECF68C16E7514B CRC64;
MEECWVTEIA NGSKDGLDSN PMKDYMILSG PQKTAVAVLC TLLGLLSALE NVAVLYLILS
SHQLRRKPSY LFIGSLAGAD FLASVVFACS FVNFHVFHGV DSKAVFLLKI GSVTMTFTAS
VGSLLLTAID RYLCLRYPPS YKALLTRGRA LVTLGIMWVL SALVSYLPLM GWTCCPRPCS
ELFPLIPNDY LLSWLLFIAF LFSGIIYTYG HVLWKAHQHV ASLSGHQDRQ VPGMARMRLD
VRLAKTLGLV LAVLLICWFP VLALMAHSLA TTLSDQVKKA FAFCSMLCLI NSMVNPVIYA
LRSGEIRSSA HHCLAHWKKC VRGLGSEAKE EAPRSSVTET EADGKITPWP DSRDLDLSDC


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