ID A0A091M2Y3_CATAU Unreviewed; 450 AA.
AC A0A091M2Y3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
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};
DE Flags: Fragment;
GN ORFNames=N323_13099 {ECO:0000313|EMBL:KFP52911.1};
OS Cathartes aura (Turkey vulture) (Vultur aura).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Accipitriformes; Cathartidae; Cathartes.
OX NCBI_TaxID=43455 {ECO:0000313|EMBL:KFP52911.1, ECO:0000313|Proteomes:UP000053745};
RN [1] {ECO:0000313|EMBL:KFP52911.1, ECO:0000313|Proteomes:UP000053745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N323 {ECO:0000313|EMBL:KFP52911.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KL310112; KFP52911.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091M2Y3; -.
DR Proteomes; UP000053745; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004948; F:calcitonin receptor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:UniProtKB-UniRule.
DR CDD; cd15274; 7tmB1_calcitonin_R; 1.
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; SSF81321; Family A G protein-coupled receptor-like; 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 Reference proteome {ECO:0000313|Proteomes:UP000053745};
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 128..153
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368099"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368099"
FT TRANSMEM 205..234
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368099"
FT TRANSMEM 241..264
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368099"
FT TRANSMEM 276..300
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368099"
FT TRANSMEM 321..342
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368099"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368099"
FT DOMAIN 34..118
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 128..375
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP52911.1"
FT NON_TER 450
FT /evidence="ECO:0000313|EMBL:KFP52911.1"
SQ SEQUENCE 450 AA; 51988 MW; 78CA903C62F09E67 CRC64;
FFATAIPSEG HQNMTEDFTQ LSVTRNKIMT AQYECYQKIM QDPIHRKEGP YCNRTWDGWL
CWSDVAAGTV SVQRCPDYFQ DFNPSEKVTK ICDPSGNWFR HPESNRTWTN YTQCNIYTHE
KVKTALNLYY LAIIGHGLSI ASLLISLGIF FYFKSLSCQR ITLHKNLFFS FVCNSVVTII
SLTAVANNQE LVATNPVSCK VSQFIYLYLM GCNYFWMLCE GIYLHTLIVV AVFAEKQHLM
WYYLLGWGFP LIPACIHAVA RSLYYNDNCW ISSDTHLLYI IHGPICAALL VNLFFLLNIV
RVLITKLKDT HKAESNLYMK AVRATLILVP LLGIEFVLFP WRPEGRIAEE VYDYVMHILM
HYQGLLVATI FCFFNGEVQA VLRRHWNQYK IQFEHSFSHS DAMRTASYTV SSISDVQGYS
YNHDCTSEHL NGKGYHDMES VVLKTEKLYG
//
