CNR1_TARGR
ID CNR1_TARGR Reviewed; 473 AA.
AC Q9PUI7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Cannabinoid receptor 1;
DE Short=CB-R;
DE Short=CB1;
GN Name=CNR1;
OS Taricha granulosa (Roughskin newt).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Caudata; Salamandroidea; Salamandridae; Pleurodelinae; Taricha.
OX NCBI_TaxID=8321;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10854287; DOI=10.1046/j.1471-4159.2000.0750413.x;
RA Soderstrom K., Leid M., Moore F.L., Murray T.F.;
RT "Behavorial, pharmacological, and molecular characterization of an
RT amphibian cannabinoid receptor.";
RL J. Neurochem. 75:413-423(2000).
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 -!- 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 -!- PTM: Palmitoylation at Cys-417 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; AF181894; AAD56029.1; -; mRNA.
DR AlphaFoldDB; Q9PUI7; -.
DR SMR; Q9PUI7; -.
DR BindingDB; Q9PUI7; -.
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; IEA:InterPro.
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..473
FT /note="Cannabinoid receptor 1"
FT /id="PRO_0000069322"
FT TOPO_DOM 1..118
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TRANSMEM 119..144
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TOPO_DOM 145..156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TRANSMEM 157..177
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TOPO_DOM 178..189
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TRANSMEM 190..214
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TOPO_DOM 215..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TRANSMEM 235..257
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TOPO_DOM 258..275
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TRANSMEM 276..301
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TOPO_DOM 302..346
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TRANSMEM 347..367
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TOPO_DOM 368..379
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TRANSMEM 380..401
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT TOPO_DOM 402..473
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 417
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P21554"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 473 AA; 53325 MW; F17C016516ED4724 CRC64;
MKSILDGLAD TTFRTITTDL LYMGSNDVQY EDTKGEMASK LGYFPQKLPL SSFRRDHSPD
KMTIGDDNLL SFYPLDQFNV TEFFNRSVST FKENDDNLKC GENFMDMECF MILTASQQLI
IAVLSLTLGT FTVLENFLVL CVILQSRTLR CRPSYHFIGS LAVADLLGSV IFVYSFLDFH
VFHRKDSSNV FLFKLGGVTA SFTASVGSLF LTAIDRYISI HRPLAYKRIV TRTKAVIAFC
VMWTIAIIIA VLPLLGWNCK KLKSVCSDIF PLIDENYLMF WIGVTSILLL FIVYAYVYIL
WKAHSHAVRM LQRGTQKSII IHTSEDGKVQ ITRPEQTRMD IRLAKTLVLI LVVLIICWGP
LLAIMVYDVF GKMNNPIKTV FAFCSMLCLM DSTVNPIIYA LRSQDLRHAF LEQCPPCEGT
SQPLDNSMES DCQHRHGNNA GNVHRAAENC IKSTVKIAKV TMSVSTETSG EAV
