CNR1_XENLA
ID CNR1_XENLA Reviewed; 470 AA.
AC Q801M1;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Cannabinoid receptor 1;
DE Short=CB-R;
DE Short=CB1;
GN Name=cnr1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=12900919; DOI=10.1002/cne.10808;
RA Cottone E., Salio C., Conrath M., Franzoni M.F.;
RT "Xenopus laevis CB1 cannabinoid receptor: molecular cloning and mRNA
RT distribution in the central nervous system.";
RL J. Comp. Neurol. 464:487-496(2003).
CC -!- FUNCTION: G-protein coupled receptor for cannabinoids (By similarity).
CC Mediates many cannabinoid-induced effects in the central nervous system
CC (CNS), as well as in peripheral tissue (By similarity)s. Regulates
CC cellular respiration and energy production in response to cannabinoids
CC (By similarity). Signaling typically involves reduction in cyclic AMP
CC (By similarity). {ECO:0000250|UniProtKB:P21554,
CC ECO:0000250|UniProtKB:P47746}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P47746};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P21554}.
CC Mitochondrion outer membrane {ECO:0000250|UniProtKB:P47746}. Cell
CC projection, axon {ECO:0000250|UniProtKB:P20272}. Presynapse
CC {ECO:0000250|UniProtKB:P20272}. Note=Unexpectedly, in the mitochondria,
CC the C-terminus is located in the mitochondrial intermembrane space, a
CC compartment topologically considered as extracellular. In canonical
CC seven-transmembrane G-protein coupled receptors, the C-terminus is
CC cytosolic. {ECO:0000250|UniProtKB:P47746}.
CC -!- TISSUE SPECIFICITY: Expressed in neurons, especially in the olfactory
CC bulbs, telencephalic pallium, and hypothalamus and also in the midbrain
CC and hindbrain (in the mesencephalic tegmentum and dorsolateral
CC rhombencephalon). Expressed also in the spinal cord.
CC {ECO:0000269|PubMed:12900919}.
CC -!- PTM: Palmitoylation at Cys-415 is important for recruitment at both
CC plasma membrane and lipid rafts and association with G protein alpha
CC subunits. {ECO:0000250|UniProtKB:P21554}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AY098532; AAM28314.1; -; mRNA.
DR RefSeq; NP_001079173.1; NM_001085704.1.
DR RefSeq; XP_018119706.1; XM_018264217.1.
DR AlphaFoldDB; Q801M1; -.
DR SMR; Q801M1; -.
DR GeneID; 373759; -.
DR KEGG; xla:373759; -.
DR CTD; 373759; -.
DR Xenbase; XB-GENE-962202; cnr1.S.
DR OMA; CMMWAIS; -.
DR OrthoDB; 822074at2759; -.
DR Proteomes; UP000186698; Chromosome 5S.
DR Bgee; 373759; Expressed in brain.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; IEA:UniProtKB-SubCell.
DR GO; GO:0004949; F:cannabinoid receptor activity; ISS:UniProtKB.
DR InterPro; IPR000810; Canbinoid_rcpt_1.
DR InterPro; IPR002230; Cnbnoid_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR22750:SF47; PTHR22750:SF47; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PIRSF; PIRSF037995; Cnoid_rcpt_1; 1.
DR PRINTS; PR00522; CANABINOID1R.
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 2: Evidence at transcript level;
KW Cell membrane; Cell projection; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Palmitate; Receptor; Reference proteome; Synapse; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..470
FT /note="Cannabinoid receptor 1"
FT /id="PRO_0000236811"
FT TOPO_DOM 1..121
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TRANSMEM 122..142
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TOPO_DOM 143..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TRANSMEM 155..175
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TOPO_DOM 176..187
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TRANSMEM 188..208
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TOPO_DOM 209..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TRANSMEM 233..253
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TOPO_DOM 254..277
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TRANSMEM 278..298
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TOPO_DOM 299..344
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TRANSMEM 345..365
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TOPO_DOM 366..377
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TRANSMEM 378..398
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TOPO_DOM 399..470
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT REGION 2..23
FT /note="Required for mitochondrial localization"
FT /evidence="ECO:0000250|UniProtKB:P47746"
FT LIPID 415
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 470 AA; 52778 MW; 388EA7881064C950 CRC64;
MKSILDGLAD TTFRTITTDL LYLGPNEVQY DDSKGDISSK LVYFPQKLPL SSLRGDPLHE
KMTIIDDPLL SIPLDQINAT DFYNKSIIFK DTDDNVQCGK NFMDMECFMI LTPSQQLVIA
ALSIILGTFT VLENMLVLVV IVQSRSLRCR PSYHFIGSLA VADLLGSVIF VYSFVDFHVF
HRKDSPNVFL FKLGGVTASF TASVGSLFLT AIDRYISIHR PMSYKRIVTR TKAVIAFCMM
WTIAIVIAVL PLFGWNCIKL RSVCSDIFPL IDETYLMFWI GVTSVLLLFI VYAYMYILWK
AHNHAVRMLQ RGTQKSIIVH TSEDGKVHIT RPDQTRMDIR LAKTLVLILV VLIICWGPLM
AIMVYDVFGK INKTIKTVFA FCSVLCLLNS TVNPIIYALR SKDLRNAFCS MFPSCQGTAQ
PLDNSMESDC QNRHVNNSNA HRAAESCIKS TVKIAKVTMS VSTDTSAEAV
