CALRL_ONCGO
ID CALRL_ONCGO Reviewed; 465 AA.
AC Q8AXU4;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Calcitonin gene-related peptide type 1 receptor;
DE Short=CGRP type 1 receptor;
DE AltName: Full=Calcitonin receptor-like receptor;
DE Flags: Precursor;
GN Name=calcrl;
OS Oncorhynchus gorbuscha (Pink salmon) (Salmo gorbuscha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8017;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=12426108; DOI=10.1016/s0378-1119(02)00974-5;
RA Pidoux E., Cressent M.;
RT "Sequencing of a calcitonin receptor-like receptor in salmon Oncorhynchus
RT gorbuscha. Functional studies using the human receptor activity-modifying
RT proteins.";
RL Gene 298:203-210(2002).
CC -!- FUNCTION: Receptor for calcitonin-gene-related peptide (CGRP) (By
CC similarity). Receptor specificity may be modulated by accessory
CC proteins. The activity of this receptor is mediated by G proteins which
CC activate adenylyl cyclase (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:12426108}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
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DR EMBL; AJ508554; CAD48406.1; -; mRNA.
DR AlphaFoldDB; Q8AXU4; -.
DR SMR; Q8AXU4; -.
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:0004948; F:calcitonin receptor activity; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR003287; GCPR_2_calcitonin_rcpt_fam.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR003289; GPCR_2_CGRP1_rcpt.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF02793; HRM; 1.
DR PRINTS; PR01351; CGRPRECEPTOR.
DR PRINTS; PR01350; CTRFAMILY.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00008; HormR; 1.
DR SUPFAM; SSF111418; SSF111418; 1.
DR PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..465
FT /note="Calcitonin gene-related peptide type 1 receptor"
FT /id="PRO_0000373834"
FT TOPO_DOM 18..148
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..168
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..195
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..215
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..238
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..275
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..291
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..315
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..338
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..356
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..368
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..390
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..465
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..76
FT /evidence="ECO:0000250"
FT DISULFID 67..107
FT /evidence="ECO:0000250"
FT DISULFID 90..129
FT /evidence="ECO:0000250"
SQ SEQUENCE 465 AA; 53494 MW; 7BF4290C0A225590 CRC64;
MVICLLLCTP TDIFVVASPE VNETQEYVPV NVYHDTDVTR KKIVTAQFEC YQKIMKDNDH
NKIGPVCNRT WDGWLCWDDT EAGFTSEQYC PDYFQDFDPS ELVTKICSDN GHWFLHPESN
RTWTNYTRCN EHTNEGRMTA MNLFYLALIG HGLSLTSLLI SLGIFFYFKS LSCQRITLHK
NLFFSFVLNS VITIIWLTAV ANNQELVQRN PTSCKVSQFI HLYLFGCNYF WMLCEGIYLH
TLIVVAVFAE KQHLMWYYLL GWGFPLIPAS IHAIARSYYY NDNCWISSNT SLLYIIHGPI
CAALLVNLFF LLNIVRVLIT KLKVTHQAES SLYMKAVRAT LILVPLLGIQ YVLLPYKPEG
RVSSEIYDYI MHILMHYQGL LVATIFCFFN GEVQGVLRRH WNQYRIQFGS TFAHSDAMRS
ASYTASSITE VQGCYSIDSH TEHLNGKGAP LDIETSILKS ENPFT
