CNR1_PELLE
ID CNR1_PELLE Reviewed; 462 AA.
AC Q333S9;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Cannabinoid receptor 1;
DE Short=CB-R;
DE Short=CB1;
GN Name=cnr1;
OS Pelophylax lessonae (Pool frog) (Rana lessonae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Pelophylax.
OX NCBI_TaxID=45623;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Brain;
RX PubMed=16485273; DOI=10.1002/mrd.20434;
RA Meccariello R., Chianese R., Cacciola G., Cobellis G., Pierantoni R.,
RA Fasano S.;
RT "Type-1 cannabinoid receptor expression in the frog, Rana esculenta,
RT tissues: a possible involvement in the regulation of testicular activity.";
RL Mol. Reprod. Dev. 73:551-558(2006).
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). May be involved in the control of reproductive
CC function (PubMed:16485273). {ECO:0000250|UniProtKB:P21554,
CC ECO:0000250|UniProtKB:P47746, ECO:0000269|PubMed:16485273}.
CC -!- ACTIVITY REGULATION: Hemopressin, a peptide derived from hemoglobin
CC subunit alpha (HBA1 and/or HBA2), acts as an antagonist peptide:
CC hemopressin-binding efficiently blocks cannabinoid receptor CNR1 and
CC subsequent signaling. {ECO:0000250|UniProtKB:P21554}.
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: Widely expressed, with high levels in the CNS and
CC lower in testis, kidney, liver, ovary, muscle, heart, spleen and
CC pituitary. {ECO:0000269|PubMed:16485273}.
CC -!- DEVELOPMENTAL STAGE: In testis, poorly expressed during the winter
CC stasis of the spermatogenesis rising during the breeding season and
CC resumption period. {ECO:0000269|PubMed:16485273}.
CC -!- PTM: Palmitoylation at Cys-407 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:0000305}.
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DR EMBL; AM113546; CAJ34534.1; -; mRNA.
DR AlphaFoldDB; Q333S9; -.
DR SMR; Q333S9; -.
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; Synapse; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..462
FT /note="Cannabinoid receptor 1"
FT /id="PRO_0000236810"
FT TOPO_DOM 1..113
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TRANSMEM 114..134
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TOPO_DOM 135..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TRANSMEM 147..167
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TOPO_DOM 168..179
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TRANSMEM 180..200
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TOPO_DOM 201..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TRANSMEM 225..245
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TOPO_DOM 246..269
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TRANSMEM 270..290
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TOPO_DOM 291..336
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TRANSMEM 337..357
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TOPO_DOM 358..369
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TRANSMEM 370..390
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TOPO_DOM 391..462
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 407
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 462 AA; 51888 MW; 505E30050F530D26 CRC64;
MKSVLDGLAD TTFRTITTDL LYMGPNEVQY EDTKSDLSKL GYYPQKLPLS SYQEKIIDGQ
STLHLDSFNA TEFYNKSITT FKDGDGNIQC GNNFMDMECF MILTPSQQLV IAALSITLGT
FTVLENMLVL CVIFQSRTLR CRPSYHFIGS LAVADLLGSV IFVYSFVDFH VFHRIDSPNV
FLFKLGGVTA SFTASVGSLF LTAIDRYISI HRPLSYKRIV TRTKAVIAFC MMWTIAIVIA
VLPLLGWNCK KLKSVCSDIF PLIDETYLMF WIGVTSVLLL FIVYAYMYIL WKAHHHAVRM
LQRGTQKSII VHTSEDGKVH ITRPDQTRMD IRLAKTLVLI LVVLIICWGP LLAIMVYDVF
GKMNKTVKTV FAFCCMLCLL NSTVNPIIYA LRSKDLRSAF CSMFPNCEGT AQPLDNSMES
DGQNRHAHNS NVHRAAESCI KSTVKIAKVT MSVSTDTSAE AV
