ID A0A1V4K8D3_PATFA Unreviewed; 836 AA.
AC A0A1V4K8D3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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};
GN Name=CALCRL {ECO:0000313|EMBL:OPJ80147.1};
GN ORFNames=AV530_002532 {ECO:0000313|EMBL:OPJ80147.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ80147.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ80147.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ80147.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ80147.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPJ80147.1}.
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DR EMBL; LSYS01004331; OPJ80147.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4K8D3; -.
DR STRING; 372326.A0A1V4K8D3; -.
DR Proteomes; UP000190648; 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:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:UniProtKB-UniRule.
DR CDD; cd15274; 7tmB1_calcitonin_R; 1.
DR CDD; cd22613; Kunitz_TFPI1_1-like; 1.
DR CDD; cd22614; Kunitz_TFPI1_2-like; 1.
DR CDD; cd22615; Kunitz_TFPI1_TFPI2_3-like; 1.
DR Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 3.
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 InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-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 Pfam; PF00014; Kunitz_BPTI; 3.
DR PRINTS; PR00759; BASICPTASE.
DR PRINTS; PR01351; CGRPRECEPTOR.
DR PRINTS; PR01350; CTRFAMILY.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00008; HormR; 1.
DR SMART; SM00131; KU; 3.
DR SUPFAM; SSF57362; BPTI-like; 3.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR SUPFAM; SSF111418; Hormone receptor domain; 1.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 3.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 3.
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:UP000190648};
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 514..539
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368099"
FT TRANSMEM 551..571
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368099"
FT TRANSMEM 591..619
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368099"
FT TRANSMEM 626..645
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368099"
FT TRANSMEM 665..686
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368099"
FT TRANSMEM 707..728
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368099"
FT TRANSMEM 740..760
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368099"
FT DOMAIN 71..121
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 150..200
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 275..325
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 420..504
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 514..761
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 240..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 836 AA; 95890 MW; A685A6A71AC6954C CRC64;
MTAEARMLRA TLGKREFEKM KGRKKGCSLP LMFILLFICI TGHATTDLED GEEEDVLGAA
FPPLKLGHSV CAMKADEGPC KAIHMRYYFN IQSRECEIFE YGGCHGNENN FLTLEECEKT
CVVTGTARER IRLPRKMMLA NIKKEKPDFC FHEKDPGICR GYFSRYFYNK ETNICEVFKY
GGCLGNQNNF KNLEECQTTC QGNSNLLPIV PAEEHPNTVN SSSPAEEPHQ LPEISINLLP
TAPNEKSNTL NSSSPKEERN QFPIFFEPPP IPSLCMTPMD RGLCRAKELR FFYNYSTGRC
HPFSYSGCGG NENNFTSRKS CLRICKKGFN KKKGERRLIK IKKTRKKQPN SACLNSFNYH
IKFTAPDIKM TKNWTTFLLF FISVTVFYVA AIPSKGHQNM TEDFTQLSVT RNKIMTAQYE
CYQKIMQDPI HKKEGPHCNR TWDGWLCWSD VAAGTVSVQR CPDYFQDFNP SEKVTKICDP
SGNWFKHPES NRTWTNYTQC NIYTREKVKT ALNLYYLAII GHGLSIASLL ISLGIFFYFK
SLSCQRITLH KNLFFSFVCN SVVTIISLTA VANNQELVAT NPVSCKVSQF IYLYLMGCNY
FWMLCEGIYL HTLIVVAVFA EKQHLLWYYL LGWGFPLIPA CIHAVARSLY YNDNCWISSD
THLLYIIHGP ICAALLVNLF FLLNIVRVLI TKLKDTHKAE SNLYMKAVRA TLILVPLLGI
EFVLFPWRPE GQIAEEVYDY VMHILMHYQG LLVATIFCFF NGEVQAVLRR HWNQYKIQFE
HSFSHSDAVR TASYTVSSIS DVQGYSYNHD CTSEHLNGKG YHDMESVVLK TEKLYG
//
