CNR1_TAEGU
ID CNR1_TAEGU Reviewed; 473 AA.
AC P56971;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Cannabinoid receptor 1;
DE Short=CB-R;
DE Short=CB1;
GN Name=CNR1;
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Soderstrom K., Johnson F.;
RT "Behavioral, pharmacologic and molecular characterization of a Zebra finch
RT CB1 cannabinoid receptor.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). Found on presynaptic axon terminals in some
CC GABAergic neurons in the somatosensory cortex (By similarity).
CC {ECO:0000250|UniProtKB:P20272, 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; AF255388; AAF78049.1; -; mRNA.
DR RefSeq; NP_001041727.1; NM_001048262.1.
DR AlphaFoldDB; P56971; -.
DR SMR; P56971; -.
DR STRING; 59729.ENSTGUP00000028918; -.
DR BindingDB; P56971; -.
DR Ensembl; ENSTGUT00000031468; ENSTGUP00000021444; ENSTGUG00000020322.
DR Ensembl; ENSTGUT00000036566; ENSTGUP00000031767; ENSTGUG00000020322.
DR Ensembl; ENSTGUT00000037149; ENSTGUP00000025330; ENSTGUG00000020322.
DR GeneID; 751607; -.
DR KEGG; tgu:751607; -.
DR CTD; 1268; -.
DR GeneTree; ENSGT01030000234510; -.
DR HOGENOM; CLU_009579_7_0_1; -.
DR InParanoid; P56971; -.
DR OMA; CMMWAIS; -.
DR OrthoDB; 822074at2759; -.
DR TreeFam; TF330052; -.
DR Proteomes; UP000007754; Chromosome 3.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0044297; C:cell body; IDA:AgBase.
DR GO; GO:0030175; C:filopodium; IDA:AgBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:AgBase.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:AgBase.
DR GO; GO:0098793; C:presynapse; IEA:UniProtKB-SubCell.
DR GO; GO:0004949; F:cannabinoid receptor activity; IMP:AgBase.
DR GO; GO:1904483; F:synthetic cannabinoid binding; IDA:AgBase.
DR GO; GO:0016049; P:cell growth; IMP:AgBase.
DR GO; GO:0060997; P:dendritic spine morphogenesis; IMP:AgBase.
DR GO; GO:0046847; P:filopodium assembly; IMP:AgBase.
DR GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; IMP:AgBase.
DR GO; GO:1903295; P:negative regulation of glutamate secretion, neurotransmission; IMP:AgBase.
DR GO; GO:1900454; P:positive regulation of long-term synaptic depression; IMP:AgBase.
DR GO; GO:0031915; P:positive regulation of synaptic plasticity; IMP:AgBase.
DR GO; GO:0031623; P:receptor internalization; IMP:AgBase.
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..473
FT /note="Cannabinoid receptor 1"
FT /id="PRO_0000069319"
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; 53094 MW; 96ECC6D1BD25461E CRC64;
MKSILDGLAD TTFRTITTDL LYVGSNDIQY EDMKGDMASK LGYYPQKFPL SSFRGDPFQE
KMTGGDDSLL SIIPSEQVNI TEFYNKSLST FKDNEENIQC GENFMDMECF MILNPSQQLA
IAVLSLTLGT FTVLENLLVL CVILHSRSLR CRPSYHFIGS LAVADLLGSV IFVYSFVDFH
VFHRKDSPNV FLFKLGGVTA SFTASVGSLF LTAIDRYISI HRPLAYKRIV TRPKAVVAFC
VMWTIAIVIA VLPLLGWNCK KLNSVCSDIF PLIDETYLMF WIGVTSILLL FIVYAYMYIL
WKAHSHAVRM LQRGTQKSII IQSTEDGKVQ ITRPDQTRMD IRLAKTLVLI LVVLIICWGP
LLAIMVYDVF GKMNKLIKTI FAFCSMLCLL NSTVNPIIYA LRSKDLRHAF RSMFPTCEGT
AQPLDNSMES DCQHKHANNA GNVHRAAESC IKSTVKIAKV TMSVSTDTTA EAL
