Cnr1
entrez
25248
canonical
uniprot
P20272
canonical
ensembl
ENSRNOG00000008223
resolver
ensembl
ENSRNOG00055016812
resolver
ensembl
ENSRNOG00060013854
resolver
ensembl
ENSRNOG00065004895
resolver
ensp
ENSRNOP00000010850
resolver
ensp
ENSRNOP00000079932
resolver
ensp
ENSRNOP00000081243
resolver
ensp
ENSRNOP00000085179
resolver
ensp
ENSRNOP00000107575
resolver
ensp
ENSRNOP00055022984
resolver
ensp
ENSRNOP00055022987
resolver
ensp
ENSRNOP00055022990
resolver
ensp
ENSRNOP00055022993
resolver
ensp
ENSRNOP00060018819
resolver
ensp
ENSRNOP00060018821
resolver
ensp
ENSRNOP00060018823
resolver
ensp
ENSRNOP00060018829
resolver
ensp
ENSRNOP00065004927
resolver
ensp
ENSRNOP00065004929
resolver
ensp
ENSRNOP00065004930
resolver
ensp
ENSRNOP00065004932
resolver
enst
ENSRNOT00000010850
resolver
enst
ENSRNOT00000099728
resolver
enst
ENSRNOT00000101534
resolver
enst
ENSRNOT00000117169
resolver
enst
ENSRNOT00000123144
resolver
enst
ENSRNOT00055028545
resolver
enst
ENSRNOT00055028548
resolver
enst
ENSRNOT00055028551
resolver
enst
ENSRNOT00055028555
resolver
enst
ENSRNOT00060023667
resolver
enst
ENSRNOT00060023669
resolver
enst
ENSRNOT00060023671
resolver
enst
ENSRNOT00060023677
resolver
enst
ENSRNOT00065007116
resolver
enst
ENSRNOT00065007118
resolver
enst
ENSRNOT00065007119
resolver
enst
ENSRNOT00065007121
resolver
genesymbol
Cnr1
resolver
genesymbol_syn
Skr6
resolver
uniprot_entry
CNR1_RAT
resolver
activity_regulation
ACTIVITY REGULATION: Hemopressin, a peptide derived from hemoglobin subunit alpha (HBA1 and/or HBA2), acts as an antagonist peptide: hemopressin-binding efficiently blocks cannabinoid receptor CNR1 and subsequent signaling. {ECO:0000269|PubMed:18077343}.
uniprot
proteins
amino_acid_sequence
MKSILDGLADTTFRTITTDLLYVGSNDIQYEDIKGDMASKLGYFPQKFPLTSFRGSPFQEKMTAGDNSPLVPAGDTTNITEFYNKSLSSFKENEENIQCGENFMDMECFMILNPSQQLAIAVLSLTLGTFTVLENLLVLCVILHSRSLRCRPSYHFIGSLAVADLLGSVIFVYSFVDFHVFHRKDSPNVFLFKLGGVTASFTASVGSLFLTAIDRYISIHRPLAYKRIVTRPKAVVAFCLMWTIAIVIAVLPLLGWNCKKLQSVCSDIFPLIDETYLMFWIGVTSVLLLFIVYAYMYILWKAHSHAVRMIQRGTQKSIIIHTSEDGKVQVTRPDQARMDIRLAKTLVLILVVLIICWGPLLAIMVYDVFGKMNKLIKTVFAFCSMLCLLNSTVNPIIYALRSKDLRHAFRSMFPSCEGTAQPLDNSMGDSDCLHKHANNTASMHRAAESCIKSTVKIAKVTMSVSTDTSAEAL
uniprot
proteins
function
FUNCTION: G protein-coupled receptor for cannabinoids, including endocannabinoids (eCBs), such as N-arachidonoylethanolamide (also called anandamide or AEA) and 2-arachidonoylglycerol (2-AG) (PubMed:2165569). Mediates many cannabinoid-induced effects, acting, among others, on food intake, memory loss, gastrointestinal motility, catalepsy, ambulatory activity, anxiety, chronic pain. Signaling typically involves reduction in cyclic AMP. In the hypothalamus, may have a dual effect on mitochondrial respiration depending upon the agonist dose and possibly upon the cell type. Increases respiration at low doses, while decreases respiration at high doses. At high doses, CNR1 signal transduction involves G protein alpha-i protein activation and subsequent inhibition of mitochondrial soluble adenylate cyclase, decrease in cyclic AMP concentration, inhibition of protein kinase A (PKA)-dependent phosphorylation of specific subunits of the mitochondrial electron transport system, including NDUFS2. In the hypothalamus, inhibits leptin-induced reactive oxygen species (ROS) formation and mediates cannabinoid-induced increase in SREBF1 and FASN gene expression. In response to cannabinoids, drives the release of orexigenic beta-endorphin, but not that of melanocyte-stimulating hormone alpha/alpha-MSH, from hypothalamic POMC neurons, hence promoting food intake. In the hippocampus, regulates cellular respiration and energy production in response to cannabinoids. Involved in cannabinoid-dependent depolarization-induced suppression of inhibition (DSI), a process in which depolarization of CA1 postsynaptic pyramidal neurons mobilizes eCBs, which retrogradely activate presynaptic CB1 receptors, transiently decreasing GABAergic inhibitory neurotransmission. Also reduces excitatory synaptic transmission (By similarity). In superior cervical ganglions and cerebral vascular smooth muscle cells, inhibits voltage-gated Ca(2+) channels in a constitutive, as well as agonist-dependent manner (By similarity). Induces leptin production in adipocytes and reduces LRP2-mediated leptin clearance in the kidney, hence participating in hyperleptinemia. In adipose tissue, CNR1 signaling leads to increased expression of SREBF1, ACACA and FASN genes. In the liver, activation by endocannabinoids leads to increased de novo lipogenesis and reduced fatty acid catabolism, associated with increased expression of SREBF1/SREBP-1, GCK, ACACA, ACACB and FASN genes. May also affect de novo cholesterol synthesis and HDL-cholesteryl ether uptake (By similarity). Peripherally modulates energy metabolism. In high carbohydrate diet-induced obesity, may decrease the expression of mitochondrial dihydrolipoyl dehydrogenase/DLD in striated muscles, as well as that of selected glucose/ pyruvate metabolic enzymes, hence affecting energy expenditure through mitochondrial metabolism (PubMed:26671069). In response to cannabinoid anandamide, elicits a pro-inflammatory response in macrophages, which involves NLRP3 inflammasome activation and IL1B and IL18 secretion. In macrophages infiltrating pancreatic islets, this process may participate in the progression of type-2 diabetes and associated loss of pancreatic beta-cells (PubMed:23955712). {ECO:0000250|UniProtKB:O02777, ECO:0000250|UniProtKB:P47746, ECO:0000269|PubMed:2165569, ECO:0000269|PubMed:23955712, ECO:0000269|PubMed:26671069}.
uniprot
proteins
mass_dalton
52845
uniprot
proteins
post_translational_modification
PTM: Palmitoylation at Cys-416 is important for recruitment at both plasma membrane and lipid rafts and association with G protein alpha subunits. {ECO:0000269|PubMed:21895628}.
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
pubmed
10362691
uniprot
proteins
pubmed
10891614
uniprot
proteins
pubmed
16033894
uniprot
proteins
pubmed
17895407
uniprot
proteins
pubmed
18077343
uniprot
proteins
pubmed
2165569
uniprot
proteins
pubmed
21895628
uniprot
proteins
pubmed
23955712
uniprot
proteins
pubmed
26671069
uniprot
proteins
pubmed
7876112
uniprot
proteins
pubmed
8832654
uniprot
proteins
sequence_length
473
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P47746}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P21554}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:P47746}. Cell projection, axon {ECO:0000269|PubMed:16033894}. Presynapse {ECO:0000269|PubMed:16033894}. Note=Unexpectedly, in the mitochondria, the C-terminus is located in the mitochondrial intermembrane space, a compartment topologically considered as extracellular. In canonical seven-transmembrane G protein-coupled receptors, the C-terminus is cytosolic (By similarity). In interneurons, found on the membrane of cytoplasmic compartments, some of which could be elements of the endosome-lysosome system and multivesicular bodies (PubMed:16033894). Found on presynaptic axon terminals in some GABAergic neurons in the somatosensory cortex (PubMed:16033894). {ECO:0000250|UniProtKB:P47746, ECO:0000269|PubMed:16033894}.
uniprot
proteins
transmembrane_region
TRANSMEM 118..143; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:P21554"; TRANSMEM 156..176; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:P21554"; TRANSMEM 189..213; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:P21554"; TRANSMEM 234..256; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:P21554"; TRANSMEM 275..300; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:P21554"; TRANSMEM 346..366; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:P21554"; TRANSMEM 379..400; /note="Helical; Name=7"; /evidence="ECO:0000250|UniProtKB:P21554
uniprot
proteins