CALCR_RABIT
ID CALCR_RABIT Reviewed; 474 AA.
AC P79222; P79223;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Calcitonin receptor {ECO:0000250|UniProtKB:P30988};
DE Short=CT-R;
DE Flags: Precursor;
GN Name=CALCR {ECO:0000250|UniProtKB:P30988};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=New Zealand white;
RX PubMed=8940110; DOI=10.1074/jbc.271.49.31127;
RA Shyu J.F., Inoue D., Baron R., Horne W.C.;
RT "The deletion of 14 amino acids in the seventh transmembrane domain of a
RT naturally occurring calcitonin receptor isoform alters ligand binding and
RT selectively abolishes coupling to phospholipase C.";
RL J. Biol. Chem. 271:31127-31134(1996).
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. Isoform 2 has altered ligand binding and abolished coupling to
CC phospholipase C.
CC -!- SUBUNIT: Interacts with GPRASP2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=C1a;
CC IsoId=P79222-1; Sequence=Displayed;
CC Name=2; Synonyms=CTRDeltae13;
CC IsoId=P79222-2; Sequence=VSP_001994;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in a tissue-
CC specific manner, with isoform 2 accounting for less than 15% of the
CC total calcitonin receptor mRNA in osteoclasts, kidney, and brain, but
CC comprising at least 50% of the transcripts in skeletal muscle and lung.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U66365; AAC48687.1; -; mRNA.
DR EMBL; U73126; AAB38258.1; -; mRNA.
DR AlphaFoldDB; P79222; -.
DR SMR; P79222; -.
DR IntAct; P79222; 1.
DR STRING; 9986.ENSOCUP00000020880; -.
DR eggNOG; KOG4564; Eukaryota.
DR InParanoid; P79222; -.
DR Proteomes; UP000001811; 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:0032841; F:calcitonin binding; IPI:UniProtKB.
DR GO; GO:0004948; F:calcitonin receptor activity; IEA:InterPro.
DR GO; GO:0007202; P:activation of phospholipase C activity; IDA:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB.
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 Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..474
FT /note="Calcitonin receptor"
FT /id="PRO_0000012809"
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..474
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"
FT VAR_SEQ 384..397
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8940110"
FT /id="VSP_001994"
SQ SEQUENCE 474 AA; 55235 MW; 85A631CAE1C61412 CRC64;
MKFTLTWRCF ALFLLLHQPT PVNPASSNDT HPTVEPEPFL YVIGRKKLMD AQYKCYDRME
QLPPYQGEGP YCNRTWDGWM CWDDTPAGVL GFQYCPDYFP DFDPTEKVTK YCDETGVWFK
HPGNNQTWSN YTMCNAFTPE KLQNAYVLYY LAIVGHSLSI FTLVISLGIF KCFRSLGCQR
VTLHKNMFLT YILNSMIIII HLVEVVPNGE LVRRDPVSCK VLHFFHQYMM SCNYFWMLCE
GIYLHTLIVV AVFAKQQHLR WYYLLGWGFP LVPTTIHAIT RAIYFNDNCW MSVETHLLYI
IHGPVMAALV VNFFFLLNIV RVLVTKMRET LEAESHMYLK AVKATMILVP LLGIQFVVFP
WRPSNKILGK IYDYLMHSLI HFQGFFVATI YCFCNNEVQT TVKRQWVQFK IQWNQRWGRR
PAHRSVSRTA ASAEEGGIPV YIYHQEPRND PAHSLGEEGA EIIPLNIIEQ ESSA
