CNR1A_TAKRU
ID CNR1A_TAKRU Reviewed; 468 AA.
AC Q98894;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Cannabinoid receptor type 1A;
GN Name=cnr1a; Synonyms=cb1a;
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-414 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; X94401; CAA64174.1; -; Genomic_DNA.
DR RefSeq; XP_003971857.1; XM_003971808.2.
DR RefSeq; XP_011610506.1; XM_011612204.1.
DR AlphaFoldDB; Q98894; -.
DR SMR; Q98894; -.
DR STRING; 31033.ENSTRUP00000045639; -.
DR GeneID; 101074068; -.
DR KEGG; tru:101074068; -.
DR CTD; 1268; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_7_0_1; -.
DR InParanoid; Q98894; -.
DR OrthoDB; 822074at2759; -.
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..468
FT /note="Cannabinoid receptor type 1A"
FT /id="PRO_0000069320"
FT TOPO_DOM 1..115
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..141
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..186
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..211
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..254
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..272
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..298
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..376
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..398
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..468
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT LIPID 414
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 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 468 AA; 52391 MW; B8628C1B043B42D7 CRC64;
MKSVLDGVAD TTFRTITSGL QYLGSNDANY DDPLNDAAFK TGFSLQKPLS AFRSNSFPNK
VPADEELIFK GIPFFPTNST DLFGNRNTTR DENSIQCGEN FMDMECFMIL TPSQQLAVAV
LSLTLGTFTV LENLVVLCVI FQSRTLRCRP SYHFIGSLAV ADLLGSVIFV YSFLDFHVFH
KKDSPNVFLF KLGGVTASFT ASVGSLFLTA IDRYISIHRP LAYRRIVTRT KAVIAFCMMW
TISIIIAVLP LLGWNCKRLN SVCSDIFPLI DENYLMFWIG VTSVLVLFII YAYIYILWKA
HHHAVRMLSR TSQKSLVVYS AEGTKVQTTR PEQTRMDIRL AKTLVLILAV LVICWGPLLA
IMVYDLFWKM DDNIKTVFAF CSMLCLLNST VNPIIYALRS RDLRHAFLSS CHACRGSAQQ
LDNSLESDCQ NRNVNISANR AAESCVKTTV KIAKVTMSVS TETSAEAV
