Q9QZN9 · CNR2_RAT
- ProteinCannabinoid receptor 2
- GeneCnr2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids360 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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 (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCannabinoid receptor 2
- Short namesCB-2; CB2; rCB2
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ9QZN9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Note: Localizes to apical dendrite of pyramidal neurons.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-33 | Extracellular | ||||
Sequence: MAGCRELELTNGSNGGLEFNPMKEYMILSDAQQ | ||||||
Transmembrane | 34-59 | Helical; Name=1 | ||||
Sequence: IAVAVLCTLMGLLSALENVAVLYLIL | ||||||
Topological domain | 60-71 | Cytoplasmic | ||||
Sequence: SSQRLRRKPSYL | ||||||
Transmembrane | 72-92 | Helical; Name=2 | ||||
Sequence: FIGSLAGADFLASVIFACNFV | ||||||
Topological domain | 93-104 | Extracellular | ||||
Sequence: IFHVFHGVDSRN | ||||||
Transmembrane | 105-129 | Helical; Name=3 | ||||
Sequence: IFLLKIGSVTMTFTASVGSLLLTAV | ||||||
Topological domain | 130-149 | Cytoplasmic | ||||
Sequence: DRYLCLCYPPTYKALVTRGR | ||||||
Transmembrane | 150-172 | Helical; Name=4 | ||||
Sequence: ALVALGVMWVLSALISYLPLMGW | ||||||
Topological domain | 173-188 | Extracellular | ||||
Sequence: TCCPSPCSELFPLIPN | ||||||
Transmembrane | 189-214 | Helical; Name=5 | ||||
Sequence: DYLLGWLLFIAILFSGIIYTYGYVLW | ||||||
Topological domain | 215-246 | Cytoplasmic | ||||
Sequence: KAHQHVASLAEHQDRQVPGIARMRLDVRLAKT | ||||||
Transmembrane | 247-267 | Helical; Name=6 | ||||
Sequence: LGLVMAVLLICWFPALALMGH | ||||||
Topological domain | 268-279 | Extracellular | ||||
Sequence: SLVTTLSDKVKE | ||||||
Transmembrane | 280-301 | Helical; Name=7 | ||||
Sequence: AFAFCSMLCLVNSMINPIIYAL | ||||||
Topological domain | 302-360 | Cytoplasmic | ||||
Sequence: RSGEIRSAAQHCLTGWKKYLQGLGSEGKEEAPKSSVTETEAEVKTTTGPGSRTPGCSNC |
Keywords
- Cellular component
Phenotypes & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for chain, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000069325 | 1-360 | Cannabinoid receptor 2 | |||
Sequence: MAGCRELELTNGSNGGLEFNPMKEYMILSDAQQIAVAVLCTLMGLLSALENVAVLYLILSSQRLRRKPSYLFIGSLAGADFLASVIFACNFVIFHVFHGVDSRNIFLLKIGSVTMTFTASVGSLLLTAVDRYLCLCYPPTYKALVTRGRALVALGVMWVLSALISYLPLMGWTCCPSPCSELFPLIPNDYLLGWLLFIAILFSGIIYTYGYVLWKAHQHVASLAEHQDRQVPGIARMRLDVRLAKTLGLVMAVLLICWFPALALMGHSLVTTLSDKVKEAFAFCSMLCLVNSMINPIIYALRSGEIRSAAQHCLTGWKKYLQGLGSEGKEEAPKSSVTETEAEVKTTTGPGSRTPGCSNC | ||||||
Glycosylation | 11 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 335 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 336 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 338 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 352 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Constitutively phosphorylated on Ser-352; phosphorylation increases cell internalization and desensitizes the receptor.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in spleen and brain by neurons and glial cells (at protein level). Expressed in lung, testis and thymus but not in heart, liver or kidney. Expressed in cerebellum, cortex and brainstem.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 327-360 | Disordered | ||||
Sequence: EGKEEAPKSSVTETEAEVKTTTGPGSRTPGCSNC | ||||||
Compositional bias | 339-360 | Polar residues | ||||
Sequence: ETEAEVKTTTGPGSRTPGCSNC |
Sequence similarities
Belongs to the G-protein coupled receptor 1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Protein family/group databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9QZN9-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length360
- Mass (Da)39,359
- Last updated2009-02-10 v3
- ChecksumE523C77055B24BE0
Q9QZN9-2
- Name2
- Differences from canonical
- 344-360: VKTTTGPGSRTPGCSNC → TLVLKDKQELGGDCLLRTSSIHSPMLSLADSANRQDVRPHCPEELTWWCSVRRPISLPNKAGQSTLL
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 224 | in Ref. 2; AAG09710/AAG22010/AAG22011 | ||||
Sequence: A → T | ||||||
Compositional bias | 339-360 | Polar residues | ||||
Sequence: ETEAEVKTTTGPGSRTPGCSNC | ||||||
Alternative sequence | VSP_036231 | 344-360 | in isoform 2 | |||
Sequence: VKTTTGPGSRTPGCSNC → TLVLKDKQELGGDCLLRTSSIHSPMLSLADSANRQDVRPHCPEELTWWCSVRRPISLPNKAGQSTLL |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF176350 EMBL· GenBank· DDBJ | AAF08535.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF218846 EMBL· GenBank· DDBJ | AAG09710.1 EMBL· GenBank· DDBJ | mRNA | ||
AF286721 EMBL· GenBank· DDBJ | AAG22010.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF286722 EMBL· GenBank· DDBJ | AAG22011.1 EMBL· GenBank· DDBJ | Genomic DNA |