CNR1B_TAKRU
ID CNR1B_TAKRU Reviewed; 470 AA.
AC Q98895;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Cannabinoid receptor type 1B;
GN Name=cnr1b; Synonyms=cb1b;
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Testis;
RX PubMed=8812500; DOI=10.1006/geno.1996.0406;
RA Yamaguchi F., Macrae A., Brenner S.;
RT "Molecular cloning of two cannabinoid type 1-like receptor genes from the
RT puffer fish Fugu rubripes.";
RL Genomics 35:603-605(1996).
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 -!- PTM: Palmitoylation at Cys-412 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; X94402; CAA64175.1; -; Genomic_DNA.
DR AlphaFoldDB; Q98895; -.
DR SMR; Q98895; -.
DR STRING; 31033.ENSTRUP00000017198; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q98895; -.
DR Proteomes; UP000005226; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; 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 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 3: Inferred from homology;
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 type 1B"
FT /id="PRO_0000069321"
FT TOPO_DOM 1..113
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..139
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..184
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..209
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..252
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..270
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..296
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..374
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..396
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..470
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 418..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 412
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 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 470 AA; 52081 MW; CEE87CD37FDF9192 CRC64;
MKLALHRIAG ATMAALTTEV QYLGSNDASY EDPQADAALM KSRFNFEKPY SASSSLHRLI
PGNKELIYGG LSTILPTNAS DFPLSNGSGE ATQCGEDIVD NMECFMILTP AQQLVIVILA
ITLGTFTVLE NFVVLCVILH SHTLRSRPSY HFIGSLAVAD LIGSIIFVYS FLDFHVLHRK
DSPSIFLFKL AGVIASFTAS VGSLFLTAID RYVSIHRPMA YKRIITKTKA VIAFSVMWAI
SIEFSLLPLL GWNCKRLHSV CSDIFPLIDE KYLMFWIGMT TVLLLFIIYA YMFILWKSHH
HAVRMLSRSS QRSIIVYTSE GTKVQTVRPE QARMDLRLAK TLVLILVALI ICWGPLLAIM
VYDLFGRVND FIKTVFAFCS MLCLLNSTIN PVIYAMRSKD LRRAFVNICH MCRGTTQSLD
SSAESDWNSR SVRSTGGRAG KDRSVGGKPQ VKVAQVTVSG VTASSPAEAV
