CALRL_PAROL
ID CALRL_PAROL Reviewed; 465 AA.
AC Q9IB86;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 71.
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; Synonyms=cgrpr;
OS Paralichthys olivaceus (Bastard halibut) (Hippoglossus olivaceus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Paralichthyidae;
OC Paralichthys.
OX NCBI_TaxID=8255;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Gill;
RX PubMed=10689190; DOI=10.1016/s0378-1119(00)00004-4;
RA Suzuki N., Suzuki T., Kurokawa T.;
RT "Cloning of a calcitonin gene-related peptide receptor and a novel
RT calcitonin receptor-like receptor from the gill of flounder, Paralichthys
RT olivaceus.";
RL Gene 244:81-88(2000).
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in gill, brain, heart, intestine and
CC testis. {ECO:0000269|PubMed:10689190}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
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DR EMBL; AB035314; BAA92816.1; -; mRNA.
DR AlphaFoldDB; Q9IB86; -.
DR SMR; Q9IB86; -.
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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..465
FT /note="Calcitonin gene-related peptide type 1 receptor"
FT /id="PRO_0000373835"
FT TOPO_DOM 21..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 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; 53040 MW; E6D64E1E28BD92C2 CRC64;
MVVLILLCDI TKFFVEGSLG SNETEHQHPT NVYHDVGVTR DKIVTAQFEC YQKIMKDSTH
SRQEPLCNRT WDGWLCWDDT KAGVISEQHC PDYFQDFDPS EMVTKICADT GDWFLHPVSN
RTWSNYTRCN QHTNEVRVTA MNLFYLALIG HGLSLTSLLI SLGIFFHFKS LSCQRITLHK
NLFFSFVLNS VITIVLLTAV ANNQEVVQSN PTSCKVSQFI HLYLFGCNYF WMLCEGIYLH
TLIVVAVFAE KQHLMWYYLL GWGFPLIPAT IHAVARSYYY NDNCWISSKT SLLYIIHGPI
CAALLVNLFF LLNIVRVLIT KLKVTHQAES SLYMKAVRAT LILVPLLGIQ YVLLPYKPEG
RVSSEIYDYI MHILMHYQGL LVATIFCFFN GEVQAVLRRH WNQYNIQFGS SIGNHSDALR
SASYTASSIT EVQGCYSIDG HTEHMNGKGC HEADASILKS DNPFA
