ID A0A3P8NLC9_ASTCA Unreviewed; 451 AA.
AC A0A3P8NLC9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Calcitonin gene-related peptide type 1 receptor {ECO:0000256|ARBA:ARBA00015885, ECO:0000256|RuleBase:RU368099};
DE Short=CGRP type 1 receptor {ECO:0000256|RuleBase:RU368099};
DE AltName: Full=Calcitonin receptor-like receptor {ECO:0000256|ARBA:ARBA00030562, ECO:0000256|RuleBase:RU368099};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000005544.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000005544.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000005544.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Receptor for calcitonin-gene-related peptide (CGRP). Receptor
CC specificity may be modulated by accessory proteins. The activity of
CC this receptor is mediated by G proteins which activate adenylyl
CC cyclase. {ECO:0000256|RuleBase:RU368099}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|RuleBase:RU368099}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU368099}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000256|ARBA:ARBA00005314, ECO:0000256|RuleBase:RU368099}.
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DR AlphaFoldDB; A0A3P8NLC9; -.
DR Ensembl; ENSACLT00000005661.1; ENSACLP00000005544.1; ENSACLG00000003710.1.
DR GeneTree; ENSGT00940000165235; -.
DR Proteomes; UP000265100; Chromosome 16.
DR Bgee; ENSACLG00000003710; Expressed in ovary and 7 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004948; F:calcitonin receptor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:UniProtKB-UniRule.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR003287; GCPR_2_calcitonin_rcpt_fam.
DR InterPro; IPR017981; GPCR_2-like_7TM.
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 PANTHER; PTHR45620:SF21; CALCITONIN GENE-RELATED PEPTIDE TYPE 1 RECEPTOR; 1.
DR PANTHER; PTHR45620; PDF RECEPTOR-LIKE PROTEIN-RELATED; 1.
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; Hormone receptor domain; 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 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU368099};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|RuleBase:RU368099};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040,
KW ECO:0000256|RuleBase:RU368099};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180,
KW ECO:0000256|RuleBase:RU368099};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368099};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU368099};
KW Signal {ECO:0000256|RuleBase:RU368099};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU368099};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU368099};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU368099}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368099"
FT TRANSMEM 156..179
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368099"
FT TRANSMEM 195..214
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368099"
FT TRANSMEM 235..262
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368099"
FT TRANSMEM 268..292
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368099"
FT TRANSMEM 304..332
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368099"
FT TRANSMEM 352..375
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368099"
FT DOMAIN 62..146
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 156..336
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
SQ SEQUENCE 451 AA; 51610 MW; F32F562703DAFEAC CRC64;
MADRKLDGFG QIWMVALILL CNPAAFMVKA SLAINETQQQ ASTSVYNDIT VTRNKIVTAQ
FECYQKLMKE NTHSRQEPVC NRTWDGWLCW DDTKAGVTSE QHCPDYFQDF DPSEMVTKIC
TDSGQWFLHP ESNRTWTNYT RCNEHTVEGR MTAMNLFYLA LIGHGLSLTS LLISLAIFFH
FKSLSCQRIT LHKNLFFSFV LNSVITIILL TAVANNQELV QRNPTSCKVS QFIHLYLFGC
NYFWMLCEGI YLHTLIVVAV FAEKQHLMWY YLLGWGFPLI PATIHAVARS YYYNDNCWIS
SKTSLLYIIH GPICAALLVN LFFLLNIVRV LITKLKYVLL PYKPEGRVSS EIYDYIMHIL
MHYQGLLVAT IFCFFNGEVQ AVLRRHWNQY HIQFGSSIGN HSDALRSASY TASSITEVQG
CYSIDGHSEH MNGKGCHDSD ASILKSDSPF A
//
