CALRL_BOVIN
ID CALRL_BOVIN Reviewed; 462 AA.
AC A6QP74;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 25-MAY-2022, entry version 77.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for calcitonin-gene-related peptide (CGRP) together
CC with RAMP1 and receptor for adrenomedullin together with RAMP2 or
CC RAMP3. The activity of this receptor is mediated by G proteins which
CC activate adenylyl cyclase. {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of CALCRL and RAMP3 (By similarity). Heterodimer
CC of CALCRL and RAMP1 or CALCRL and RAMP2 (By similarity).
CC {ECO:0000250|UniProtKB:Q16602}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI49185.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC149184; AAI49185.1; ALT_INIT; mRNA.
DR RefSeq; NP_001095577.1; NM_001102107.1.
DR AlphaFoldDB; A6QP74; -.
DR SMR; A6QP74; -.
DR STRING; 9913.ENSBTAP00000056622; -.
DR PaxDb; A6QP74; -.
DR GeneID; 527140; -.
DR KEGG; bta:527140; -.
DR CTD; 10203; -.
DR eggNOG; KOG4564; Eukaryota.
DR InParanoid; A6QP74; -.
DR OMA; CVALHII; -.
DR OrthoDB; 1005634at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0043235; C:receptor complex; IDA:UniProtKB.
DR GO; GO:0004948; F:calcitonin receptor activity; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0031623; P:receptor internalization; IDA:UniProtKB.
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; Phosphoprotein; Receptor; Reference proteome; Signal; Transducer;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..462
FT /note="Calcitonin gene-related peptide type 1 receptor"
FT /id="PRO_0000373831"
FT TOPO_DOM 23..147
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..167
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..194
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..214
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..237
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..274
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..290
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..314
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..355
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..367
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 368..389
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 390..461
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R1W5"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R1W5"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..75
FT /evidence="ECO:0000250"
FT DISULFID 66..106
FT /evidence="ECO:0000250"
FT DISULFID 89..128
FT /evidence="ECO:0000250"
SQ SEQUENCE 462 AA; 53387 MW; D89FEE4F03676D04 CRC64;
MEKKFFLSFL FLLPFFMILV IAESEEENPD DLIQLGVTRN KIMTAQYECY QKIMQDPVQQ
TEGIYCNRTW DGWLCWNDVA AGTESMQHCP DYFQDFDPSE KVTKICDQDG NWFRHPASNR
TWTNYTQCNV NTHEKVKTAL NLFYLTIIGH VLSIASLLIS LGIFFYFKSL SCQRITLHKN
LFFSFVCNSV ITIIHLTAVA NNQALVATNP VSCKVSQFIH LYLMGCNYFW MLCEGIYLHT
LVVVAVFAEK QHLMWYYFLG WGFPLIPACI HAVARRLYYN DNCWISSDTQ LLYIIHGPIC
AALLVNLFFL LNIVRVLITK LKVTHQAESN LYMKAVRATL ILVPLLGIEF VLIPWRPEGK
IAEEIYDYII NILMHYQGLL VSTIFCFFNG EVQAILRRNW NQYKIQFGNN FSHSDTLRSA
SYTVSTISDG TGYSHDCLSE HLNGKSIHDT DNVVIKPEKL YD
