CALCR_CAVPO
ID CALCR_CAVPO Reviewed; 478 AA.
AC O08893;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Calcitonin receptor {ECO:0000250|UniProtKB:P30988};
DE Short=CT-R;
DE Flags: Precursor;
GN Name=CALCR {ECO:0000250|UniProtKB:P30988};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9231703; DOI=10.1046/j.1471-4159.1997.69020455.x;
RA Sarkar A., Dickerson I.M.;
RT "Cloning, characterization, and expression of a calcitonin receptor from
RT guinea pig brain.";
RL J. Neurochem. 69:455-464(1997).
CC -!- FUNCTION: This is a receptor for calcitonin. The activity of this
CC receptor is mediated by G proteins which activate adenylyl cyclase. The
CC calcitonin receptor is thought to couple to the heterotrimeric
CC guanosine triphosphate-binding protein that is sensitive to cholera
CC toxin.
CC -!- SUBUNIT: Interacts with GPRASP2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
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DR EMBL; U92463; AAB58586.1; -; mRNA.
DR RefSeq; NP_001166395.1; NM_001172924.1.
DR AlphaFoldDB; O08893; -.
DR SMR; O08893; -.
DR STRING; 10141.ENSCPOP00000006261; -.
DR GeneID; 100135491; -.
DR KEGG; cpoc:100135491; -.
DR CTD; 799; -.
DR eggNOG; KOG4564; Eukaryota.
DR InParanoid; O08893; -.
DR OrthoDB; 1005634at2759; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
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:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IEA:UniProt.
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; IPR001688; GPCR_2_calcitonin_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:SF8; PTHR45620:SF8; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF02793; HRM; 1.
DR PRINTS; PR00361; CALCITONINR.
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; Reference proteome; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..478
FT /note="Calcitonin receptor"
FT /id="PRO_0000012805"
FT TOPO_DOM 23..153
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..173
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..200
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 201..220
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..243
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..260
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..280
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..296
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..320
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..361
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 362..373
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..395
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..478
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 55..81
FT /evidence="ECO:0000250"
FT DISULFID 72..112
FT /evidence="ECO:0000250"
FT DISULFID 95..134
FT /evidence="ECO:0000250"
SQ SEQUENCE 478 AA; 55554 MW; AF22030A94FE2BB4 CRC64;
MRFTFTRQFL AFFILISNPA SILPRSENLT FPTFEPEPYL YSVGRKKLVD AQYRCYDRMQ
QLPPYEGEGP YCNRTWDGWM CWDDTPAGVL SVQLCPDYFP DFDPTEKVTK YCDESGVWFK
HPENNRTWSN YTLCNAFTPE KLQNAYVLYY LAIVGHSMSI ITLVVSLGIF VYFRSLGCQR
VTLHKNMFLT YILNSMIIII HLVEVVPNGE LVRKDPVSCK ILHFFHQYMM ACNYFWMLCE
GIYLHTLIVV SVFNEAKHLR WYYLLGWGFP LVPTTIHAIT RALYFNDNCW ISVDTHLLYI
IHGPVMVALV VNFFFLLNIV RVLVTKMRET HEAESYMYLK AVKATMILVP LLGIQFVVFP
WRPSNKVLGK IYDYFMHSLI HFQGFFVATI YCFCNNEVQT TLKRQWAQFK IQWNQRWGTR
PSNRSAAARA AAAAAEAGGD NIPVYICHQE PRNDPPNNQG EEGAEMIVLN IIEKESSA
