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Calcitonin gene-related peptide type 1 receptor (CGRP type 1 receptor) (Calcitonin receptor-like receptor)

 CALRL_HUMAN             Reviewed;         461 AA.
Q16602; A8K6G5; A8KAD3; Q53S02; Q53TS5;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
14-APR-2009, sequence version 2.
22-NOV-2017, entry version 161.
RecName: Full=Calcitonin gene-related peptide type 1 receptor;
Short=CGRP type 1 receptor;
AltName: Full=Calcitonin receptor-like receptor;
Flags: Precursor;
Name=CALCRL; Synonyms=CGRPR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
PubMed=8626685; DOI=10.1074/jbc.271.19.11325;
Aiyar N., Rand K., Elshourbagy N.A., Zeng Z., Adamou J.E.,
Bergsma D.J., Li Y.;
"A cDNA encoding the calcitonin gene-related peptide type 1
receptor.";
J. Biol. Chem. 271:11325-11329(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Cerebellum;
PubMed=7818539; DOI=10.1006/bbrc.1995.1047;
Fluehmann B., Muff R., Hunziker W., Fischer J.A., Born W.;
"A human orphan calcitonin receptor-like structure.";
Biochem. Biophys. Res. Commun. 206:341-347(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart;
Kopatz S.A., Aronstam R.S., Sharma S.V.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TYR-8.
TISSUE=Placenta, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
PROTEIN SEQUENCE OF 23-37.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[7]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 23-133 IN COMPLEX WITH RAMP1
AND ANTAGONIST, SUBUNIT, AND DISULFIDE BONDS.
PubMed=20826335; DOI=10.1016/j.str.2010.05.014;
ter Haar E., Koth C.M., Abdul-Manan N., Swenson L., Coll J.T.,
Lippke J.A., Lepre C.A., Garcia-Guzman M., Moore J.M.;
"Crystal structure of the ectodomain complex of the CGRP receptor, a
class-B GPCR, reveals the site of drug antagonism.";
Structure 18:1083-1093(2010).
[8]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 23-136 IN COMPLEX WITH RAMP2,
FUNCTION, MUTAGENESIS OF TRP-72; PHE-92 AND TRP-121, AND DISULFIDE
BONDS.
PubMed=22102369; DOI=10.1002/pro.2003;
Kusano S., Kukimoto-Niino M., Hino N., Ohsawa N., Okuda K.,
Sakamoto K., Shirouzu M., Shindo T., Yokoyama S.;
"Structural basis for extracellular interactions between calcitonin
receptor-like receptor and receptor activity-modifying protein 2 for
adrenomedullin-specific binding.";
Protein Sci. 21:199-210(2012).
-!- FUNCTION: Receptor for calcitonin-gene-related peptide (CGRP)
together with RAMP1 and receptor for adrenomedullin together with
RAMP3 (By similarity). Receptor for adrenomedullin together with
RAMP2. The activity of this receptor is mediated by G proteins
which activate adenylyl cyclase. {ECO:0000250,
ECO:0000269|PubMed:22102369}.
-!- SUBUNIT: Heterodimer of CALCRL and RAMP3 (By similarity).
Heterodimer of CALCRL and RAMP1 or CALCRL and RAMP2. {ECO:0000250,
ECO:0000269|PubMed:20826335, ECO:0000269|PubMed:22102369}.
-!- INTERACTION:
P06881:CALCA; NbExp=2; IntAct=EBI-962878, EBI-962928;
O60894:RAMP1; NbExp=3; IntAct=EBI-962878, EBI-962893;
O60895:RAMP2; NbExp=6; IntAct=EBI-962878, EBI-9009040;
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
-!- TISSUE SPECIFICITY: Predominantly expressed in the lung and heart.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAF84319.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; L76380; AAC41994.1; -; mRNA.
EMBL; U17473; AAA62158.1; -; mRNA.
EMBL; AY389506; AAQ91332.1; -; mRNA.
EMBL; AK291630; BAF84319.1; ALT_INIT; mRNA.
EMBL; AK292998; BAF85687.1; -; mRNA.
EMBL; AC007319; AAY14806.1; -; Genomic_DNA.
EMBL; AC074020; AAY14996.1; -; Genomic_DNA.
CCDS; CCDS2293.1; -.
PIR; JC2477; JC2477.
RefSeq; NP_001258680.1; NM_001271751.1.
RefSeq; NP_005786.1; NM_005795.5.
UniGene; Hs.470882; -.
UniGene; Hs.744587; -.
PDB; 3AQF; X-ray; 2.60 A; B=23-136.
PDB; 3N7P; X-ray; 2.80 A; A/B/C/J=23-133.
PDB; 3N7R; X-ray; 2.90 A; A/B=23-133.
PDB; 3N7S; X-ray; 2.10 A; A/B=23-133.
PDB; 4RWF; X-ray; 1.76 A; A=31-116.
PDB; 4RWG; X-ray; 2.44 A; A/B/C=31-114.
PDBsum; 3AQF; -.
PDBsum; 3N7P; -.
PDBsum; 3N7R; -.
PDBsum; 3N7S; -.
PDBsum; 4RWF; -.
PDBsum; 4RWG; -.
ProteinModelPortal; Q16602; -.
SMR; Q16602; -.
BioGrid; 115498; 4.
CORUM; Q16602; -.
DIP; DIP-37674N; -.
IntAct; Q16602; 4.
STRING; 9606.ENSP00000376177; -.
BindingDB; Q16602; -.
ChEMBL; CHEMBL3798; -.
GuidetoPHARMACOLOGY; 47; -.
TCDB; 9.A.14.4.12; the g-protein-coupled receptor (gpcr) family.
iPTMnet; Q16602; -.
PhosphoSitePlus; Q16602; -.
DMDM; 226693507; -.
PaxDb; Q16602; -.
PeptideAtlas; Q16602; -.
PRIDE; Q16602; -.
DNASU; 10203; -.
Ensembl; ENST00000392370; ENSP00000376177; ENSG00000064989.
Ensembl; ENST00000409998; ENSP00000386972; ENSG00000064989.
Ensembl; ENST00000410068; ENSP00000387190; ENSG00000064989.
GeneID; 10203; -.
KEGG; hsa:10203; -.
UCSC; uc002upv.6; human.
CTD; 10203; -.
DisGeNET; 10203; -.
EuPathDB; HostDB:ENSG00000064989.12; -.
GeneCards; CALCRL; -.
HGNC; HGNC:16709; CALCRL.
HPA; HPA008070; -.
HPA; HPA046515; -.
MIM; 114190; gene.
neXtProt; NX_Q16602; -.
PharmGKB; PA26033; -.
eggNOG; KOG4564; Eukaryota.
eggNOG; ENOG410XRS2; LUCA.
HOVERGEN; HBG102129; -.
InParanoid; Q16602; -.
KO; K04577; -.
OrthoDB; EOG091G027C; -.
PhylomeDB; Q16602; -.
TreeFam; TF315710; -.
Reactome; R-HSA-418555; G alpha (s) signalling events.
Reactome; R-HSA-419812; Calcitonin-like ligand receptors.
EvolutionaryTrace; Q16602; -.
GeneWiki; CALCRL; -.
GenomeRNAi; 10203; -.
PRO; PR:Q16602; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000064989; -.
CleanEx; HS_CALCRL; -.
ExpressionAtlas; Q16602; baseline and differential.
Genevisible; Q16602; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0001605; F:adrenomedullin receptor activity; IDA:UniProtKB.
GO; GO:0001635; F:calcitonin gene-related peptide receptor activity; IEA:Ensembl.
GO; GO:0004948; F:calcitonin receptor activity; IEA:InterPro.
GO; GO:0004930; F:G-protein coupled receptor activity; TAS:ProtInc.
GO; GO:0008565; F:protein transporter activity; IDA:UniProtKB.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IEA:Ensembl.
GO; GO:0001525; P:angiogenesis; IDA:UniProtKB.
GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
GO; GO:0006171; P:cAMP biosynthetic process; IDA:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
GO; GO:0071329; P:cellular response to sucrose stimulus; IDA:UniProtKB.
GO; GO:0007187; P:G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; TAS:ProtInc.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
GO; GO:0045986; P:negative regulation of smooth muscle contraction; IEA:Ensembl.
GO; GO:0030819; P:positive regulation of cAMP biosynthetic process; IDA:UniProtKB.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0015031; P:protein transport; IDA:UniProtKB.
GO; GO:0031623; P:receptor internalization; IDA:UniProtKB.
CDD; cd15274; 7tmB1_calcitonin_R; 1.
Gene3D; 4.10.1240.10; -; 1.
InterPro; IPR003287; GCPR_2_calcitonin_rcpt_fam.
InterPro; IPR017981; GPCR_2-like.
InterPro; IPR003289; GPCR_2_CGRP1_rcpt.
InterPro; IPR036445; GPCR_2_extracell_dom_sf.
InterPro; IPR001879; GPCR_2_extracellular_dom.
InterPro; IPR000832; GPCR_2_secretin-like.
InterPro; IPR017983; GPCR_2_secretin-like_CS.
Pfam; PF00002; 7tm_2; 1.
Pfam; PF02793; HRM; 1.
PRINTS; PR01351; CGRPRECEPTOR.
PRINTS; PR01350; CTRFAMILY.
PRINTS; PR00249; GPCRSECRETIN.
SMART; SM00008; HormR; 1.
SUPFAM; SSF111418; SSF111418; 1.
PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; 1.
PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; G-protein coupled receptor;
Glycoprotein; Membrane; Phosphoprotein; Polymorphism; Receptor;
Reference proteome; Signal; Transducer; Transmembrane;
Transmembrane helix.
SIGNAL 1 22 {ECO:0000269|PubMed:15340161}.
CHAIN 23 461 Calcitonin gene-related peptide type 1
receptor.
/FTId=PRO_0000012811.
TOPO_DOM 23 146 Extracellular. {ECO:0000255}.
TRANSMEM 147 166 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 167 173 Cytoplasmic. {ECO:0000255}.
TRANSMEM 174 193 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 194 213 Extracellular. {ECO:0000255}.
TRANSMEM 214 236 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 237 253 Cytoplasmic. {ECO:0000255}.
TRANSMEM 254 273 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 274 289 Extracellular. {ECO:0000255}.
TRANSMEM 290 313 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 314 336 Cytoplasmic. {ECO:0000255}.
TRANSMEM 337 354 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 355 366 Extracellular. {ECO:0000255}.
TRANSMEM 367 388 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 389 461 Cytoplasmic. {ECO:0000255}.
MOD_RES 420 420 Phosphoserine.
{ECO:0000250|UniProtKB:Q9R1W5}.
MOD_RES 445 445 Phosphoserine.
{ECO:0000250|UniProtKB:Q9R1W5}.
CARBOHYD 66 66 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 118 118 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 123 123 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 48 74
DISULFID 65 105
DISULFID 88 127
VARIANT 8 8 N -> Y (in dbSNP:rs698577).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_054822.
VARIANT 16 16 F -> L (in dbSNP:rs13391909).
/FTId=VAR_049453.
VARIANT 274 274 R -> I (in dbSNP:rs34010553).
/FTId=VAR_049454.
MUTAGEN 72 72 W->A: Strongly reduced affinity for
adrenomedullin.
{ECO:0000269|PubMed:22102369}.
MUTAGEN 92 92 F->A: Strongly reduced affinity for
adrenomedullin.
{ECO:0000269|PubMed:22102369}.
MUTAGEN 121 121 W->A: Strongly reduced affinity for
adrenomedullin.
{ECO:0000269|PubMed:22102369}.
CONFLICT 144 144 L -> Q (in Ref. 4; BAF84319).
{ECO:0000305}.
STRAND 33 35 {ECO:0000244|PDB:3N7P}.
HELIX 36 54 {ECO:0000244|PDB:4RWF}.
STRAND 60 62 {ECO:0000244|PDB:4RWF}.
STRAND 63 65 {ECO:0000244|PDB:3N7S}.
STRAND 78 87 {ECO:0000244|PDB:4RWF}.
STRAND 90 92 {ECO:0000244|PDB:3N7S}.
STRAND 99 105 {ECO:0000244|PDB:4RWF}.
TURN 115 117 {ECO:0000244|PDB:4RWF}.
TURN 125 128 {ECO:0000244|PDB:4RWF}.
HELIX 131 134 {ECO:0000244|PDB:4RWG}.
HELIX 136 144 {ECO:0000244|PDB:4RWG}.
SEQUENCE 461 AA; 52929 MW; AF98E55E5454767C CRC64;
MEKKCTLNFL VLLPFFMILV TAELEESPED SIQLGVTRNK IMTAQYECYQ KIMQDPIQQA
EGVYCNRTWD GWLCWNDVAA GTESMQLCPD YFQDFDPSEK VTKICDQDGN WFRHPASNRT
WTNYTQCNVN THEKVKTALN LFYLTIIGHG LSIASLLISL GIFFYFKSLS CQRITLHKNL
FFSFVCNSVV TIIHLTAVAN NQALVATNPV SCKVSQFIHL YLMGCNYFWM LCEGIYLHTL
IVVAVFAEKQ HLMWYYFLGW GFPLIPACIH AIARSLYYND NCWISSDTHL LYIIHGPICA
ALLVNLFFLL NIVRVLITKL KVTHQAESNL YMKAVRATLI LVPLLGIEFV LIPWRPEGKI
AEEVYDYIMH ILMHFQGLLV STIFCFFNGE VQAILRRNWN QYKIQFGNSF SNSEALRSAS
YTVSTISDGP GYSHDCPSEH LNGKSIHDIE NVLLKPENLY N


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