Cannabinoid receptor 1 - Rattus norvegicus (Rat)

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P20272 (CNR1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 106. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Cannabinoid receptor 1
Short name=CB-R
Short name=CB1

Alternative name(s):
Brain-type cannabinoid receptor

Gene names

Name:	Cnr1
Synonyms:	Skr6

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	473 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in cannabinoid-induced CNS effects. Acts by inhibiting adenylate cyclase. Could be a receptor for anandamide. Inhibits L-type Ca²⁺ channel current.
Subunit structure	Interacts (via C-terminus) with CNRIP1. Ref.4
Subcellular location	Cell membrane; Multi-pass membrane protein.
Post-translational modification	Palmitoylation at Cys-416 is important for recruitment at both plasma membrane and lipid rafts. Ref.5
Sequence similarities	Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Glycoprotein Lipoprotein Palmitate
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adenylate cyclase-modulating G-protein coupled receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB aging Inferred from mutant phenotype PubMed 19679649. Source: RGD maternal process involved in female pregnancy Inferred from expression pattern PubMed 19860893. Source: RGD memory Inferred from direct assay PubMed 19666083. Source: RGD negative regulation of action potential Inferred from mutant phenotype PubMed 20067581. Source: RGD negative regulation of blood pressure Inferred from mutant phenotype PubMed 19295473. Source: RGD negative regulation of dopamine secretion Inferred from mutant phenotype PubMed 19187091. Source: RGD negative regulation of fatty acid beta-oxidation Inferred from mutant phenotype PubMed 19724020. Source: RGD negative regulation of mast cell activation Inferred from direct assay PubMed 18552882. Source: RGD negative regulation of nitric-oxide synthase activity Inferred from mutant phenotype PubMed 18561998. Source: RGD positive regulation of acute inflammatory response to antigenic stimulus Inferred from mutant phenotype PubMed 19282305. Source: RGD positive regulation of apoptotic process Inferred from mutant phenotype PubMed 19560819. Source: RGD positive regulation of blood pressure Inferred from mutant phenotype PubMed 19553924. Source: RGD positive regulation of fever generation Inferred from mutant phenotype PubMed 19681872. Source: RGD positive regulation of neuron projection development Inferred from direct assay PubMed 19861414. Source: RGD regulation of feeding behavior Inferred from mutant phenotype PubMed 19575185. Source: RGD regulation of insulin secretion Inferred from mutant phenotype PubMed 19644453. Source: RGD regulation of penile erection Inferred from mutant phenotype PubMed 17850365. Source: RGD regulation of synaptic transmission, GABAergic Inferred from mutant phenotype PubMed 19725112. Source: RGD regulation of synaptic transmission, glutamatergic Inferred from mutant phenotype PubMed 19725112. Source: RGD response to cocaine Inferred from mutant phenotype PubMed 19401177. Source: RGD response to ethanol Inferred from mutant phenotype PubMed 19860799. Source: RGD response to lipopolysaccharide Inferred from mutant phenotype PubMed 19295473 PubMed 19681872. Source: RGD response to morphine Inferred from mutant phenotype PubMed 19463710 PubMed 19804815. Source: RGD response to nicotine Inferred from mutant phenotype PubMed 19463710. Source: RGD response to nutrient Inferred from expression pattern PubMed 19807847. Source: RGD response to stress Inferred from expression pattern PubMed 19460405. Source: RGD sensory perception of pain Inferred from mutant phenotype PubMed 20035773. Source: RGD spermatogenesis Inferred from expression pattern PubMed 18614700. Source: RGD
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cannabinoid receptor activity Inferred from mutant phenotype PubMed 17110038 Ref.1. Source: RGD drug binding Inferred from mutant phenotype PubMed 17110038. Source: RGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Adora2a	P30543	3	EBI-2909800,EBI-2902822

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 473

473

Cannabinoid receptor 1

PRO_0000069318

Regions

Topological domain

1 – 117

117

Extracellular Potential

Transmembrane

118 – 143

Helical; Name=1; Potential

Topological domain

144 – 155

Cytoplasmic Potential

Transmembrane

156 – 176

Helical; Name=2; Potential

Topological domain

177 – 188

Extracellular Potential

Transmembrane

189 – 213

Helical; Name=3; Potential

Topological domain

214 – 233

Cytoplasmic Potential

Transmembrane

234 – 256

Helical; Name=4; Potential

Topological domain

257 – 274

Extracellular Potential

Transmembrane

275 – 300

Helical; Name=5; Potential

Topological domain

301 – 345

Cytoplasmic Potential

Transmembrane

346 – 366

Helical; Name=6; Potential

Topological domain

367 – 378

Extracellular Potential

Transmembrane

379 – 400

Helical; Name=7; Potential

Topological domain

401 – 473

Cytoplasmic Potential

Amino acid modifications

Lipidation

416

S-palmitoyl cysteine Ref.5

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

N-linked (GlcNAc...) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

P20272 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: E59A66AFE17B646C
Show »

FASTA

473

52,845

        10         20         30         40         50         60 
MKSILDGLAD TTFRTITTDL LYVGSNDIQY EDIKGDMASK LGYFPQKFPL TSFRGSPFQE 

        70         80         90        100        110        120 
KMTAGDNSPL VPAGDTTNIT EFYNKSLSSF KENEENIQCG ENFMDMECFM ILNPSQQLAI 

       130        140        150        160        170        180 
AVLSLTLGTF TVLENLLVLC VILHSRSLRC RPSYHFIGSL AVADLLGSVI FVYSFVDFHV 

       190        200        210        220        230        240 
FHRKDSPNVF LFKLGGVTAS FTASVGSLFL TAIDRYISIH RPLAYKRIVT RPKAVVAFCL 

       250        260        270        280        290        300 
MWTIAIVIAV LPLLGWNCKK LQSVCSDIFP LIDETYLMFW IGVTSVLLLF IVYAYMYILW 

       310        320        330        340        350        360 
KAHSHAVRMI QRGTQKSIII HTSEDGKVQV TRPDQARMDI RLAKTLVLIL VVLIICWGPL 

       370        380        390        400        410        420 
LAIMVYDVFG KMNKLIKTVF AFCSMLCLLN STVNPIIYAL RSKDLRHAFR SMFPSCEGTA 

       430        440        450        460        470 
QPLDNSMGDS DCLHKHANNT ASMHRAAESC IKSTVKIAKV TMSVSTDTSA EAL

« Hide

References

[1]	"Structure of a cannabinoid receptor and functional expression of the cloned cDNA." Matsuda L.A., Lolait S.J., Brownstein M.J., Young A.C., Bonner T.I. Nature 346:561-564(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain cortex.
[2]	"Determination of the cannabinoid receptors in mouse x rat hybridoma NG108-15 cells and rat GH4C1 cells." Ho B.Y., Zhao J. Neurosci. Lett. 212:123-126(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"An amino-terminal variant of the central cannabinoid receptor resulting from alternative splicing." Shire D., Carillon C., Kaghad M., Calandra B., Rinaldi-Carmona M., Le Fur G., Caput D., Ferrara P. J. Biol. Chem. 270:3726-3731(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-107.
[4]	"CB1 cannabinoid receptor activity is modulated by the cannabinoid receptor interacting protein CRIP 1a." Niehaus J.L., Liu Y., Wallis K.T., Egertova M., Bhartur S.G., Mukhopadhyay S., Shi S., He H., Selley D.E., Howlett A.C., Elphick M.R., Lewis D.L. Mol. Pharmacol. 72:1557-1566(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CNRIP1. Tissue: Brain.
[5]	"Effects of palmitoylation of Cys(415) in helix 8 of the CB(1) cannabinoid receptor on membrane localization and signalling." Oddi S., Dainese E., Sandiford S., Fezza F., Lanuti M., Chiurchiu V., Totaro A., Catanzaro G., Barcaroli D., De Laurenzi V., Centonze D., Mukhopadhyay S., Selent J., Howlett A.C., Maccarrone M. Br. J. Pharmacol. 165:2635-2651(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PALMITOYLATION AT CYS-416.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X55812 mRNA. Translation: CAA39332.1. U40395 mRNA. Translation: AAA99067.1.
IPI	IPI00197472.
PIR	A33117.
RefSeq	NP_036916.1. NM_012784.4.
UniGene	Rn.89774.
3D structure databases
ProteinModelPortal	P20272.
ModBase	Search...
Protein-protein interaction databases
IntAct	P20272. 1 interaction.
MINT	MINT-7266592.
STRING	10116.ENSRNOP00000010850.
Protein family/group databases
GPCRDB	Search...
PTM databases
PhosphoSite	P20272.
Proteomic databases
PRIDE	P20272.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000010850; ENSRNOP00000010850; ENSRNOG00000008223.
GeneID	25248.
KEGG	rno:25248.
UCSC	RGD:2369. rat.
Organism-specific databases
CTD	1268.
RGD	2369. Cnr1.
Phylogenomic databases
eggNOG	NOG148018.
GeneTree	ENSGT00700000104088.
HOGENOM	HOG000049272.
HOVERGEN	HBG051045.
InParanoid	P20272.
KO	K04277.
OMA	ECFMILN.
OrthoDB	EOG41ZF9S.
Gene expression databases
ArrayExpress	P20272.
Genevestigator	P20272.
GermOnline	ENSRNOG00000008223. Rattus norvegicus.
Family and domain databases
InterPro	IPR002230. Cnbnoid_rcpt. IPR000810. Cnoid_rcpt_1. IPR000276. GPCR_Rhodpsn. IPR017452. GPCR_Rhodpsn_7TM. [Graphical view]
PANTHER	PTHR22750:SF10. PTHR22750:SF10. 1 hit.
Pfam	PF00001. 7tm_1. 1 hit. [Graphical view]
PIRSF	PIRSF037995. Cnoid_rcpt_1. 1 hit.
PRINTS	PR00522. CANABINOID1R. PR00362. CANNABINOIDR. PR00237. GPCRRHODOPSN.
PROSITE	PS00237. G_PROTEIN_RECEP_F1_1. 1 hit. PS50262. G_PROTEIN_RECEP_F1_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P20272.
ChEMBL	CHEMBL3571.
NextBio	605857.

Entry information

Entry name

CNR1_RAT

Accession

Primary (citable) accession number: P20272

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	April 3, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents