CNR2_RAT
ID CNR2_RAT Reviewed; 360 AA.
AC Q9QZN9; Q9EP74;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Cannabinoid receptor 2;
DE Short=CB-2;
DE Short=CB2;
DE Short=rCB2;
GN Name=Cnr2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC STRAIN=Sprague-Dawley;
RX PubMed=10688601;
RA Griffin G., Tao Q., Abood M.E.;
RT "Cloning and pharmacological characterization of the rat CB2 cannabinoid
RT receptor.";
RL J. Pharmacol. Exp. Ther. 292:886-894(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), AND TISSUE
RP SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=12084572; DOI=10.1016/s0167-4781(02)00341-x;
RA Brown S.M., Wager-Miller J., Mackie K.;
RT "Cloning and molecular characterization of the rat CB2 cannabinoid
RT receptor.";
RL Biochim. Biophys. Acta 1576:255-264(2002).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=12153574; DOI=10.1046/j.1432-1033.2002.03078.x;
RA Matias I., Pochard P., Orlando P., Salzet M., Pestel J., Di Marzo V.;
RT "Presence and regulation of the endocannabinoid system in human dendritic
RT cells.";
RL Eur. J. Biochem. 269:3771-3778(2002).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=16224028; DOI=10.1126/science.1115740;
RA Van Sickle M.D., Duncan M., Kingsley P.J., Mouihate A., Urbani P.,
RA Mackie K., Stella N., Makriyannis A., Piomelli D., Davison J.S.,
RA Marnett L.J., Di Marzo V., Pittman Q.J., Patel K.D., Sharkey K.A.;
RT "Identification and functional characterization of brainstem cannabinoid
RT CB2 receptors.";
RL Science 310:329-332(2005).
RN [5]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=18286196; DOI=10.1371/journal.pone.0001640;
RA Onaivi E.S., Ishiguro H., Gong J.-P., Patel S., Meozzi P.A., Myers L.,
RA Perchuk A., Mora Z., Tagliaferro P.A., Gardner E., Brusco A.,
RA Akinshola B.E., Hope B., Lujilde J., Inada T., Iwasaki S., Macharia D.,
RA Teasenfitz L., Arinami T., Uhl G.R.;
RT "Brain neuronal CB2 cannabinoid receptors in drug abuse and depression:
RT from mice to human subjects.";
RL PLoS ONE 3:E1640-E1640(2008).
CC -!- FUNCTION: Heterotrimeric G protein-coupled receptor for endocannabinoid
CC 2-arachidonoylglycerol mediating inhibition of adenylate cyclase. May
CC function in inflammatory response, nociceptive transmission and bone
CC homeostasis (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18286196};
CC Multi-pass membrane protein {ECO:0000269|PubMed:18286196}. Cell
CC projection, dendrite {ECO:0000269|PubMed:18286196}. Perikaryon
CC {ECO:0000269|PubMed:18286196}. Note=Localizes to apical dendrite of
CC pyramidal neurons.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9QZN9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QZN9-2; Sequence=VSP_036231;
CC -!- TISSUE SPECIFICITY: Expressed in spleen and brain by neurons and glial
CC cells (at protein level). Expressed in lung, testis and thymus but not
CC in heart, liver or kidney. Expressed in cerebellum, cortex and
CC brainstem. {ECO:0000269|PubMed:12084572, ECO:0000269|PubMed:12153574,
CC ECO:0000269|PubMed:16224028, ECO:0000269|PubMed:18286196}.
CC -!- PTM: Constitutively phosphorylated on Ser-352; phosphorylation
CC increases cell internalization and desensitizes the receptor.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF176350; AAF08535.1; -; Genomic_DNA.
DR EMBL; AF218846; AAG09710.1; -; mRNA.
DR EMBL; AF286721; AAG22010.1; -; Genomic_DNA.
DR EMBL; AF286722; AAG22011.1; -; Genomic_DNA.
DR RefSeq; NP_001157614.1; NM_001164142.3. [Q9QZN9-1]
DR RefSeq; NP_001157615.1; NM_001164143.3. [Q9QZN9-1]
DR RefSeq; NP_065418.3; NM_020543.4. [Q9QZN9-2]
DR RefSeq; XP_017449092.1; XM_017593603.1. [Q9QZN9-2]
DR AlphaFoldDB; Q9QZN9; -.
DR SMR; Q9QZN9; -.
DR IntAct; Q9QZN9; 1.
DR STRING; 10116.ENSRNOP00000012342; -.
DR BindingDB; Q9QZN9; -.
DR ChEMBL; CHEMBL2470; -.
DR DrugCentral; Q9QZN9; -.
DR GuidetoPHARMACOLOGY; 57; -.
DR GlyGen; Q9QZN9; 1 site.
DR PhosphoSitePlus; Q9QZN9; -.
DR PaxDb; Q9QZN9; -.
DR Ensembl; ENSRNOT00000012342; ENSRNOP00000012342; ENSRNOG00000009260. [Q9QZN9-2]
DR Ensembl; ENSRNOT00000074998; ENSRNOP00000066697; ENSRNOG00000009260. [Q9QZN9-1]
DR Ensembl; ENSRNOT00000114527; ENSRNOP00000078684; ENSRNOG00000009260. [Q9QZN9-1]
DR Ensembl; ENSRNOT00000119033; ENSRNOP00000088855; ENSRNOG00000009260. [Q9QZN9-1]
DR GeneID; 57302; -.
DR KEGG; rno:57302; -.
DR UCSC; RGD:619713; rat. [Q9QZN9-1]
DR CTD; 1269; -.
DR RGD; 619713; Cnr2.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234510; -.
DR HOGENOM; CLU_009579_7_0_1; -.
DR InParanoid; Q9QZN9; -.
DR OMA; CNFVNFH; -.
DR OrthoDB; 822074at2759; -.
DR PhylomeDB; Q9QZN9; -.
DR TreeFam; TF330052; -.
DR Reactome; R-RNO-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:Q9QZN9; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000009260; Expressed in spleen and 16 other tissues.
DR ExpressionAtlas; Q9QZN9; baseline and differential.
DR Genevisible; Q9QZN9; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; TAS:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004949; F:cannabinoid receptor activity; IDA:RGD.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IDA:RGD.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0038171; P:cannabinoid signaling pathway; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:RGD.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0030595; P:leukocyte chemotaxis; ISO:RGD.
DR GO; GO:0045759; P:negative regulation of action potential; IMP:RGD.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IDA:RGD.
DR GO; GO:0033004; P:negative regulation of mast cell activation; IDA:RGD.
DR GO; GO:0051001; P:negative regulation of nitric-oxide synthase activity; IMP:RGD.
DR GO; GO:0032229; P:negative regulation of synaptic transmission, GABAergic; IMP:RGD.
DR GO; GO:0019222; P:regulation of metabolic process; IBA:GO_Central.
DR GO; GO:0001975; P:response to amphetamine; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:RGD.
DR GO; GO:0019233; P:sensory perception of pain; IMP:RGD.
DR InterPro; IPR001551; Canbinoid_rcpt_2.
DR InterPro; IPR002230; Cnbnoid_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR22750:SF10; PTHR22750:SF10; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00523; CANABINOID2R.
DR PRINTS; PR00362; CANNABINOIDR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
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 Alternative splicing; Cell membrane; Cell projection;
KW G-protein coupled receptor; Glycoprotein; Inflammatory response; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..360
FT /note="Cannabinoid receptor 2"
FT /id="PRO_0000069325"
FT TOPO_DOM 1..33
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..59
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..104
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..129
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..172
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..188
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..214
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..279
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..301
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..360
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 327..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47936"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47936"
FT MOD_RES 338
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P47936"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34972"
FT CARBOHYD 11
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 344..360
FT /note="VKTTTGPGSRTPGCSNC -> TLVLKDKQELGGDCLLRTSSIHSPMLSLADS
FT ANRQDVRPHCPEELTWWCSVRRPISLPNKAGQSTLL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12084572"
FT /id="VSP_036231"
FT CONFLICT 224
FT /note="A -> T (in Ref. 2; AAG09710/AAG22010/AAG22011)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 39359 MW; E523C77055B24BE0 CRC64;
MAGCRELELT NGSNGGLEFN PMKEYMILSD AQQIAVAVLC TLMGLLSALE NVAVLYLILS
SQRLRRKPSY LFIGSLAGAD FLASVIFACN FVIFHVFHGV DSRNIFLLKI GSVTMTFTAS
VGSLLLTAVD RYLCLCYPPT YKALVTRGRA LVALGVMWVL SALISYLPLM GWTCCPSPCS
ELFPLIPNDY LLGWLLFIAI LFSGIIYTYG YVLWKAHQHV ASLAEHQDRQ VPGIARMRLD
VRLAKTLGLV MAVLLICWFP ALALMGHSLV TTLSDKVKEA FAFCSMLCLV NSMINPIIYA
LRSGEIRSAA QHCLTGWKKY LQGLGSEGKE EAPKSSVTET EAEVKTTTGP GSRTPGCSNC
