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Extracellular calcium-sensing receptor (CaSR) (Parathyroid cell calcium-sensing receptor) (PCaR1) (RaKCaR)

 CASR_RAT                Reviewed;        1079 AA.
P48442;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
27-SEP-2017, entry version 132.
RecName: Full=Extracellular calcium-sensing receptor;
Short=CaSR;
AltName: Full=Parathyroid cell calcium-sensing receptor;
Short=PCaR1;
Short=RaKCaR {ECO:0000303|PubMed:7816802};
Flags: Precursor;
Name=Casr; Synonyms=Gprc2a, Pcar1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
STRAIN=Sprague-Dawley; TISSUE=Kidney outer medulla;
PubMed=7816802; DOI=10.1073/pnas.92.1.131;
Riccardi D., Park J., Lee W., Gamba G., Brown E.M., Hebert S.C.;
"Cloning and functional expression of a rat kidney extracellular
calcium/polyvalent cation-sensing receptor.";
Proc. Natl. Acad. Sci. U.S.A. 92:131-135(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-294.
STRAIN=Wistar;
PubMed=7724534; DOI=10.1073/pnas.92.8.3161;
Ruat M., Snowman A.M., Snyder S.H.;
"Calcium sensing receptor: molecular cloning in rat and localization
to nerve terminals.";
Proc. Natl. Acad. Sci. U.S.A. 92:3161-3165(1995).
[3]
INTERACTION WITH ARRB1.
PubMed=17623778; DOI=10.1242/jcs.03469;
Bouschet T., Martin S., Kanamarlapudi V., Mundell S., Henley J.M.;
"The calcium-sensing receptor changes cell shape via a beta-arrestin-1
ARNO ARF6 ELMO protein network.";
J. Cell Sci. 120:2489-2497(2007).
-!- FUNCTION: G-protein-coupled receptor that senses changes in the
extracellular concentration of calcium ions and plays a key role
in maintaining calcium homeostasis (PubMed:7816802). Senses
fluctuations in the circulating calcium concentration and
modulates the production of parathyroid hormone (PTH) in
parathyroid glands (By similarity). The activity of this receptor
is mediated by a G-protein that activates a phosphatidylinositol-
calcium second messenger system (By similarity). The G-protein-
coupled receptor activity is activated by a co-agonist mechanism:
aromatic amino acids, such as Trp or Phe, act concertedly with
divalent cations, such as calcium or magnesium, to achieve full
receptor activation (By similarity).
{ECO:0000250|UniProtKB:P41180, ECO:0000250|UniProtKB:Q9QY96}.
-!- ENZYME REGULATION: In resting state, adopts an open conformation,
anion-binding promoting the inactive configuration. Upon aromatic
amino acid-binding, the groove in the extracellular venus flytrap
module is closed, thereby inducing the formation of a novel
homodimer interface between subunits. Calcium ions stabilize the
active state by enhancing homodimer interactions between membrane-
proximal domains to fully activate the receptor.
{ECO:0000250|UniProtKB:P41180}.
-!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts
with VCP and RNF19A (By similarity). Interacts with ARRB1
(PubMed:17623778). {ECO:0000250|UniProtKB:P41180,
ECO:0000269|PubMed:17623778}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P41180}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P41180}.
-!- DOMAIN: The extracellular regions of the homodimer interact in a
side-by-side fashion while facing opposite directions. Each
extracellular region consists of three domains, LB1 (ligand-
binding 1), LB2 and CR (cysteine-rich). The two lobe-shaped
domains LB1 and LB2 form a venus flytrap module. In the inactive
configuration, the venus flytrap modules of both protomers are in
the open conformation associated with the resting state (open-
open) and the interdomain cleft is empty. In addition, each
protomer contains three anions, which reinforce the inactive
conformation, and one calcium ion. In the active configuration,
both protomers of extracellular regions have the closed
conformation associated with agonist-binding (closed-closed). The
ligand-binding cleft of each protomer is solely occupied by an
aromatic amino-acid. Calcium is bound at four novel sites,
including one at the homodimer interface. Agonist-binding induces
large conformational changes within the extracellular region
homodimer: first, the venus flytrap module of each protomer
undergoes domain closure. Second, the LB2 regions of the two
protomers approach each other, resulting in an expansion of the
homodimer interactions involving LB2 domains. Third, the CR
regions of the two subunits interact to form a large homodimer
interface that is unique to the active state. The CR regions are
brought into close contact by the motion involving LB2 since the
two domains are rigidly associated within each subunit.
{ECO:0000250|UniProtKB:P41180}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P41180}.
-!- PTM: Ubiquitinated by RNF19A; which induces proteasomal
degradation. {ECO:0000250|UniProtKB:P41180}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U10354; AAC52149.1; -; mRNA.
EMBL; U20289; AAC52195.1; -; mRNA.
PIR; I59362; I59362.
RefSeq; NP_001296567.1; NM_001309638.1.
RefSeq; NP_058692.1; NM_016996.2.
RefSeq; XP_017453358.1; XM_017597869.1.
RefSeq; XP_017453359.1; XM_017597870.1.
RefSeq; XP_017453360.1; XM_017597871.1.
RefSeq; XP_017453361.1; XM_017597872.1.
UniGene; Rn.10019; -.
ProteinModelPortal; P48442; -.
SMR; P48442; -.
IntAct; P48442; 1.
STRING; 10116.ENSRNOP00000003092; -.
BindingDB; P48442; -.
ChEMBL; CHEMBL2516; -.
GuidetoPHARMACOLOGY; 54; -.
iPTMnet; P48442; -.
PhosphoSitePlus; P48442; -.
PaxDb; P48442; -.
PRIDE; P48442; -.
Ensembl; ENSRNOT00000003092; ENSRNOP00000003092; ENSRNOG00000002265.
Ensembl; ENSRNOT00000078341; ENSRNOP00000070633; ENSRNOG00000002265.
Ensembl; ENSRNOT00000086097; ENSRNOP00000069629; ENSRNOG00000002265.
GeneID; 24247; -.
KEGG; rno:24247; -.
UCSC; RGD:2277; rat.
CTD; 846; -.
RGD; 2277; Casr.
eggNOG; KOG1056; Eukaryota.
eggNOG; ENOG410XR6W; LUCA.
GeneTree; ENSGT00760000118974; -.
HOGENOM; HOG000232092; -.
HOVERGEN; HBG052876; -.
InParanoid; P48442; -.
KO; K04612; -.
OMA; GYTCLLA; -.
PhylomeDB; P48442; -.
TreeFam; TF331269; -.
Reactome; R-RNO-416476; G alpha (q) signalling events.
Reactome; R-RNO-418594; G alpha (i) signalling events.
Reactome; R-RNO-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
PRO; PR:P48442; -.
Proteomes; UP000002494; Chromosome 11.
Bgee; ENSRNOG00000002265; -.
Genevisible; P48442; RN.
GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0043679; C:axon terminus; IDA:RGD.
GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0016597; F:amino acid binding; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IDA:RGD.
GO; GO:0008144; F:drug binding; IDA:RGD.
GO; GO:0004930; F:G-protein coupled receptor activity; IMP:RGD.
GO; GO:0005178; F:integrin binding; IPI:RGD.
GO; GO:0044325; F:ion channel binding; IPI:RGD.
GO; GO:0000287; F:magnesium ion binding; IDA:RGD.
GO; GO:0019808; F:polyamine binding; IDA:RGD.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; IMP:RGD.
GO; GO:0006915; P:apoptotic process; IEP:RGD.
GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IMP:RGD.
GO; GO:0070509; P:calcium ion import; IEA:Ensembl.
GO; GO:0006816; P:calcium ion transport; IMP:RGD.
GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:RGD.
GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IEP:RGD.
GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; IEP:RGD.
GO; GO:1901653; P:cellular response to peptide; IEP:RGD.
GO; GO:0071305; P:cellular response to vitamin D; IEP:RGD.
GO; GO:0005513; P:detection of calcium ion; ISS:UniProtKB.
GO; GO:0060613; P:fat pad development; IEP:RGD.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007254; P:JNK cascade; IMP:RGD.
GO; GO:0001503; P:ossification; IMP:RGD.
GO; GO:0007200; P:phospholipase C-activating G-protein coupled receptor signaling pathway; IMP:RGD.
GO; GO:0032781; P:positive regulation of ATPase activity; IEA:Ensembl.
GO; GO:0090280; P:positive regulation of calcium ion import; IMP:RGD.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:RGD.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0032024; P:positive regulation of insulin secretion; IMP:RGD.
GO; GO:0050927; P:positive regulation of positive chemotaxis; IMP:RGD.
GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:RGD.
GO; GO:0051592; P:response to calcium ion; IEP:RGD.
GO; GO:0071774; P:response to fibroblast growth factor; IEP:RGD.
GO; GO:0002931; P:response to ischemia; IEP:RGD.
GO; GO:0010038; P:response to metal ion; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0042311; P:vasodilation; IMP:RGD.
InterPro; IPR001828; ANF_lig-bd_rcpt.
InterPro; IPR000337; GPCR_3.
InterPro; IPR011500; GPCR_3_9-Cys_dom.
InterPro; IPR017978; GPCR_3_C.
InterPro; IPR017979; GPCR_3_CS.
InterPro; IPR028082; Peripla_BP_I.
Pfam; PF00003; 7tm_3; 1.
Pfam; PF01094; ANF_receptor; 1.
Pfam; PF07562; NCD3G; 1.
PRINTS; PR00248; GPCRMGR.
SUPFAM; SSF53822; SSF53822; 1.
PROSITE; PS00979; G_PROTEIN_RECEP_F3_1; 1.
PROSITE; PS00980; G_PROTEIN_RECEP_F3_2; 1.
PROSITE; PS00981; G_PROTEIN_RECEP_F3_3; 1.
PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
1: Evidence at protein level;
Calcium; Cell membrane; Complete proteome; Disulfide bond;
G-protein coupled receptor; Glycoprotein; Membrane; Metal-binding;
Phosphoprotein; Receptor; Reference proteome; Signal; Transducer;
Transmembrane; Transmembrane helix; Ubl conjugation.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 1079 Extracellular calcium-sensing receptor.
/FTId=PRO_0000012948.
TOPO_DOM 20 612 Extracellular. {ECO:0000255}.
TRANSMEM 613 635 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 636 649 Cytoplasmic. {ECO:0000255}.
TRANSMEM 650 670 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 671 681 Extracellular. {ECO:0000255}.
TRANSMEM 682 700 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 701 724 Cytoplasmic. {ECO:0000255}.
TRANSMEM 725 745 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 746 769 Extracellular. {ECO:0000255}.
TRANSMEM 770 792 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 793 805 Cytoplasmic. {ECO:0000255}.
TRANSMEM 806 828 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 829 836 Extracellular. {ECO:0000255}.
TRANSMEM 837 862 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 863 1079 Cytoplasmic. {ECO:0000255}.
REGION 22 188 Ligand-binding 1 (LB1).
{ECO:0000250|UniProtKB:P41180}.
REGION 66 70 Anion binding.
{ECO:0000250|UniProtKB:P41180}.
REGION 189 324 Ligand-binding 2 (LB2).
{ECO:0000250|UniProtKB:P41180}.
REGION 415 417 Anion binding.
{ECO:0000250|UniProtKB:P41180}.
REGION 542 612 Cysteine-rich (CR).
{ECO:0000250|UniProtKB:P41180}.
REGION 880 900 Interaction with RNF19A.
{ECO:0000250|UniProtKB:P41180}.
METAL 81 81 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P41180}.
METAL 84 84 Calcium. {ECO:0000250|UniProtKB:P41180}.
METAL 87 87 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P41180}.
METAL 88 88 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P41180}.
METAL 100 100 Calcium. {ECO:0000250|UniProtKB:P41180}.
METAL 145 145 Calcium. {ECO:0000250|UniProtKB:P41180}.
METAL 231 231 Calcium. {ECO:0000250|UniProtKB:P41180}.
METAL 234 234 Calcium. {ECO:0000250|UniProtKB:P41180}.
METAL 557 557 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P41180}.
BINDING 147 147 Aromatic amino acid.
{ECO:0000250|UniProtKB:P41180}.
BINDING 168 168 Aromatic amino acid; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P41180}.
BINDING 170 170 Aromatic amino acid.
{ECO:0000250|UniProtKB:P41180}.
BINDING 297 297 Aromatic amino acid.
{ECO:0000250|UniProtKB:P41180}.
MOD_RES 920 920 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QY96}.
MOD_RES 1062 1062 Phosphoserine.
{ECO:0000250|UniProtKB:Q9QY96}.
CARBOHYD 90 90 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 130 130 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 261 261 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 287 287 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 386 386 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 446 446 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 468 468 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 488 488 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 541 541 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 594 594 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 60 101 {ECO:0000250|UniProtKB:P41180}.
DISULFID 129 129 Interchain.
{ECO:0000250|UniProtKB:P41180}.
DISULFID 131 131 Interchain.
{ECO:0000250|UniProtKB:P41180}.
DISULFID 236 561 {ECO:0000250|UniProtKB:P41180}.
DISULFID 358 395 {ECO:0000250|UniProtKB:P41180}.
DISULFID 437 449 {ECO:0000250|UniProtKB:P41180}.
DISULFID 542 562 {ECO:0000250|UniProtKB:P41180}.
DISULFID 546 565 {ECO:0000250|UniProtKB:P41180}.
DISULFID 568 582 {ECO:0000250|UniProtKB:P41180}.
DISULFID 585 598 {ECO:0000250|UniProtKB:P41180}.
SEQUENCE 1079 AA; 120868 MW; D7664550361F9736 CRC64;
MASYSCCLAL LALAWHSSAY GPDQRAQKKG DIILGGLFPI HFGVAAKDQD LKSRPESVEC
IRYNFRGFRW LQAMIFAIEE INSSPSLLPN MTLGYRIFDT CNTVSKALEA TLSFVAQNKI
DSLNLDEFCN CSEHIPSTIA VVGATGSGVS TAVANLLGLF YIPQVSYASS SRLLSNKNQY
KSFLRTIPND EHQATAMADI IEYFRWNWVG TIAADDDYGR PGIEKFREEA EERDICIDFS
ELISQYSDEE EIQQVVEVIQ NSTAKVIVVF SSGPDLEPLI KEIVRRNITG RIWLASEAWA
SSSLIAMPEY FHVVGGTIGF GLKAGQIPGF REFLQKVHPR KSVHNGFAKE FWEETFNCHL
QEGAKGPLPV DTFVRSHEEG GNRLLNSSTA FRPLCTGDEN INSVETPYMD YEHLRISYNV
YLAVYSIAHA LQDIYTCLPG RGLFTNGSCA DIKKVEAWQV LKHLRHLNFT NNMGEQVTFD
ECGDLVGNYS IINWHLSPED GSIVFKEVGY YNVYAKKGER LFINEEKILW SGFSREVPFS
NCSRDCQAGT RKGIIEGEPT CCFECVECPD GEYSGETDAS ACDKCPDDFW SNENHTSCIA
KEIEFLAWTE PFGIALTLFA VLGIFLTAFV LGVFIKFRNT PIVKATNREL SYLLLFSLLC
CFSSSLFFIG EPQDWTCRLR QPAFGISFVL CISCILVKTN RVLLVFEAKI PTSFHRKWWG
LNLQFLLVFL CTFMQILICI IWLYTAPPSS YRNHELEDEI IFITCHEGSL MALGSLIGYT
CLLAAICFFF AFKSRKLPEN FNEAKFITFS MLIFFIVWIS FIPAYASTYG KFVSAVEVIA
ILAASFGLLA CIFFNKVYII LFKPSRNTIE EVRSSTAAHA FKVAARATLR RPNISRKRSS
SLGGSTGSIP SSSISSKSNS EDRFPQPERQ KQQQPLSLTQ QEQQQQPLTL HPQQQQQPQQ
PRCKQKVIFG SGTVTFSLSF DEPQKNAMAH RNSMRQNSLE AQRSNDTLGR HQALLPLQCA
DADSEMTIQE TGLQGPMVGD HQPEMESSDE MSPALVMSTS RSFVISGGGS SVTENVLHS


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