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Parathyroid hormone/parathyroid hormone-related peptide receptor (PTH/PTHrP type I receptor) (PTH/PTHr receptor) (Parathyroid hormone 1 receptor) (PTH1 receptor)

 PTH1R_HUMAN             Reviewed;         593 AA.
Q03431; Q2M1U3;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
18-JUL-2018, entry version 192.
RecName: Full=Parathyroid hormone/parathyroid hormone-related peptide receptor;
AltName: Full=PTH/PTHrP type I receptor;
Short=PTH/PTHr receptor;
AltName: Full=Parathyroid hormone 1 receptor;
Short=PTH1 receptor;
Flags: Precursor;
Name=PTH1R; Synonyms=PTHR, PTHR1;
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=Kidney;
PubMed=8386612; DOI=10.1210/endo.132.5.8386612;
Schipani E., Karga H., Karaplis A.C., Potts J.T. Jr., Kronenberg H.M.,
Abou-Samra A.-B., Segre G.V., Jueppner H.;
"Identical complementary deoxyribonucleic acids encode a human renal
and bone parathyroid hormone (PTH)/PTH-related peptide receptor.";
Endocrinology 132:2157-2165(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PTH,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Kidney;
PubMed=8397094; DOI=10.1016/0922-4106(93)90092-N;
Schneider H., Feyen J.-H., Rao Movva N.;
"Cloning and functional expression of a human parathyroid hormone
receptor.";
Eur. J. Pharmacol. 246:149-155(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7745008; DOI=10.1210/jcem.80.5.7745008;
Schipani E., Weinstein L.S., Bergwitz C., Iida-Klein A., Kong X.F.,
Stuhrmann M., Kruse K., Whyte M.P., Murray T., Schmidtke J., Dop C.,
Brickman A.S., Crawford J.D., Potts J.T. Jr., Kronenberg H.M.,
Abou-Samra A.-B., Segre G.V., Jueppner H.;
"Pseudohypoparathyroidism type Ib is not caused by mutations in the
coding exons of the human parathyroid hormone (PTH)/PTH-related
peptide receptor gene.";
J. Clin. Endocrinol. Metab. 80:1611-1621(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
Levine M.A.;
"Characterization of cDNA and genomic DNA encoding the human PTH/PTHrP
receptor.";
Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
King M.M., Aronstam R.S., Sharma S.V.;
"Isolation of cDNA coding for parathyroid hormone receptor 1
(PTHR1).";
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
DISULFIDE BONDS IN EXTRACELLULAR DOMAIN, AND INTERACTION WITH PTH.
PubMed=10913300; DOI=10.1021/bi0001426;
Grauschopf U., Lilie H., Honold K., Wozny M., Reusch D., Esswein A.,
Schafer W., Rucknagel K.P., Rudolph R.;
"The N-terminal fragment of human parathyroid hormone receptor 1
constitutes a hormone binding domain and reveals a distinct disulfide
pattern.";
Biochemistry 39:8878-8887(2000).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-551, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[9]
STRUCTURE BY NMR OF 168-198.
PubMed=9737850; DOI=10.1021/bi981265h;
Pellegrini M., Bisello A., Rosenblatt M., Chorev M., Mierke D.F.;
"Binding domain of human parathyroid hormone receptor: from
conformation to function.";
Biochemistry 37:12737-12743(1998).
[10]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 29-187 IN COMPLEX WITH PTH,
AND DISULFIDE BONDS.
PubMed=18375760; DOI=10.1073/pnas.0801027105;
Pioszak A.A., Xu H.E.;
"Molecular recognition of parathyroid hormone by its G protein-coupled
receptor.";
Proc. Natl. Acad. Sci. U.S.A. 105:5034-5039(2008).
[11]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 474-481.
PubMed=18611381; DOI=10.1016/j.str.2008.04.010;
Johnston C.A., Kimple A.J., Giguere P.M., Siderovski D.P.;
"Structure of the parathyroid hormone receptor C terminus bound to the
G-protein dimer Gbeta1gamma2.";
Structure 16:1086-1094(2008).
[12]
ERRATUM, AND RETRACTION.
DOI=10.1016/j.str.2011.07.010;
Johnston C.A., Kimple A.J., Giguere P.M., Siderovski D.P.;
Structure 0:0-0(2011).
[13]
X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 29-187 IN COMPLEX WITH
PTHLH, SUBUNIT, AND DISULFIDE BONDS.
PubMed=19674967; DOI=10.1074/jbc.M109.022905;
Pioszak A.A., Parker N.R., Gardella T.J., Xu H.E.;
"Structural basis for parathyroid hormone-related protein binding to
the parathyroid hormone receptor and design of conformation-selective
peptides.";
J. Biol. Chem. 284:28382-28391(2009).
[14]
X-RAY CRYSTALLOGRAPHY (3.24 ANGSTROMS) OF 29-187, FUNCTION, SUBUNIT,
SUBCELLULAR LOCATION, MUTAGENESIS OF ILE-135 AND ASP-137, AND
DISULFIDE BONDS.
PubMed=20172855; DOI=10.1074/jbc.M109.093138;
Pioszak A.A., Harikumar K.G., Parker N.R., Miller L.J., Xu H.E.;
"Dimeric arrangement of the parathyroid hormone receptor and a
structural mechanism for ligand-induced dissociation.";
J. Biol. Chem. 285:12435-12444(2010).
[15]
VARIANT JMC ARG-223.
PubMed=7701349; DOI=10.1126/science.7701349;
Schipani E., Kruse K., Jueppner H.;
"A constitutively active mutant PTH-PTHrP receptor in Jansen-type
metaphyseal chondrodysplasia.";
Science 268:98-100(1995).
[16]
VARIANTS JMC ARG-223 AND PRO-410.
PubMed=8703170; DOI=10.1056/NEJM199609053351004;
Schipani E., Langman C.B., Parfitt A.M., Jensen G.S., Kikuchi S.,
Kooh S.W., Cole W.G., Jueppner H.;
"Constitutively activated receptors for parathyroid hormone and
parathyroid hormone-related peptide in Jansen's metaphyseal
chondrodysplasia.";
N. Engl. J. Med. 335:708-714(1996).
[17]
CHARACTERIZATION OF VARIANTS JMC ARG-223 AND PRO-410.
PubMed=9178745; DOI=10.1210/mend.11.7.9934;
Schipani E., Jensen G.S., Pincus J., Nissenson R.A., Gardella T.J.,
Jueppner H.;
"Constitutive activation of the cyclic adenosine 3',5'-monophosphate
signaling pathway by parathyroid hormone (PTH)/PTH-related peptide
receptors mutated at the two loci for Jansen's metaphyseal
chondrodysplasia.";
Mol. Endocrinol. 11:851-858(1997).
[18]
VARIANT BOCD LEU-132.
PubMed=9745456; DOI=10.1210/jc.83.9.3373;
Zhang P., Jobert A.-S., Couvineau A., Silve C.;
"A homozygous inactivating mutation in the parathyroid
hormone/parathyroid hormone-related peptide receptor causing
Blomstrand chondrodysplasia.";
J. Clin. Endocrinol. Metab. 83:3365-3368(1998).
[19]
VARIANT JMC ARG-458.
PubMed=10487664; DOI=10.1210/jcem.84.9.6000;
Schipani E., Langman C.B., Hunzelman J., Le Merrer M., Loke K.Y.,
Dillon M.J., Silve C., Jueppner H.;
"A novel parathyroid hormone (PTH)/PTH-related peptide receptor
mutation in Jansen's metaphyseal chondrodysplasia.";
J. Clin. Endocrinol. Metab. 84:3052-3057(1999).
[20]
VARIANT ENCHOM CYS-150.
PubMed=11850620; DOI=10.1038/ng844;
Hopyan S., Gokgoz N., Poon R., Gensure R.C., Yu C., Cole W.G.,
Bell R.S., Jueppner H., Andrulis I.L., Wunder J.S., Alman B.A.;
"A mutant PTH/PTHrP type I receptor in enchondromatosis.";
Nat. Genet. 30:306-310(2002).
[21]
DISCUSSION OF THE ASSOCIATION OF CYS-150 WITH ENCHOM.
PubMed=15523647; DOI=10.1002/humu.20095;
Rozeman L.B., Sangiorgi L., Briaire-de Bruijn I.H., Mainil-Varlet P.,
Bertoni F., Cleton-Jansen A.-M., Hogendoorn P.C.W., Bovee J.V.M.G.;
"Enchondromatosis (Ollier disease, Maffucci syndrome) is not caused by
the PTHR1 mutation p.R150C.";
Hum. Mutat. 24:466-473(2004).
[22]
VARIANT JMC ARG-410, AND CHARACTERIZATION OF VARIANT JMC ARG-410.
PubMed=15240651; DOI=10.1210/jc.2004-0036;
Bastepe M., Raas-Rothschild A., Silver J., Weissman I., Wientroub S.,
Jueppner H., Gillis D.;
"A form of Jansen's metaphyseal chondrodysplasia with limited
metabolic and skeletal abnormalities is caused by a novel activating
parathyroid hormone (PTH)/PTH-related peptide receptor mutation.";
J. Clin. Endocrinol. Metab. 89:3595-3600(2004).
[23]
INVOLVEMENT IN EISD.
PubMed=15525660; DOI=10.1093/hmg/ddi001;
Duchatelet S., Ostergaard E., Cortes D., Lemainque A., Julier C.;
"Recessive mutations in PTHR1 cause contrasting skeletal dysplasias in
Eiken and Blomstrand syndromes.";
Hum. Mol. Genet. 14:1-5(2005).
[24]
INVOLVEMENT IN PRIMARY FAILURE OF TOOTH ERUPTION.
PubMed=19061984; DOI=10.1016/j.ajhg.2008.11.006;
Decker E., Stellzig-Eisenhauer A., Fiebig B.S., Rau C., Kress W.,
Saar K., Rueschendorf F., Hubner N., Grimm T., Weber B.H.F.;
"PTHR1 loss-of-function mutations in familial, nonsyndromic primary
failure of tooth eruption.";
Am. J. Hum. Genet. 83:781-786(2008).
[25]
VARIANT JMC ARG-223, CHARACTERIZATION OF VARIANT JMC ARG-223,
GLYCOSYLATION, FUNCTION, AND SUBUNIT.
PubMed=27160269; DOI=10.1007/s10266-016-0247-4;
Shimomura-Kuroki J., Farooq M., Sekimoto T., Amizuka N., Shimomura Y.;
"Characterization of a PTH1R missense mutation responsible for Jansen
type metaphyseal chondrodysplasia.";
Odontology 105:150-154(2017).
-!- FUNCTION: Receptor for parathyroid hormone and for parathyroid
hormone-related peptide. The activity of this receptor is mediated
by G proteins which activate adenylyl cyclase and also a
phosphatidylinositol-calcium second messenger system.
{ECO:0000269|PubMed:20172855, ECO:0000269|PubMed:27160269,
ECO:0000269|PubMed:8397094}.
-!- SUBUNIT: Interacts (via N-terminal extracellular domain) with
PTHLH and PTH (PubMed:8397094, PubMed:10913300, PubMed:18375760,
PubMed:19674967). Homodimer in the absence of bound ligand.
Peptide hormone binding leads to dissociation of the homodimer
(PubMed:19674967, PubMed:20172855). {ECO:0000269|PubMed:10913300,
ECO:0000269|PubMed:18375760, ECO:0000269|PubMed:19674967,
ECO:0000269|PubMed:20172855, ECO:0000269|PubMed:27160269,
ECO:0000269|PubMed:8397094}.
-!- INTERACTION:
P35222:CTNNB1; NbExp=4; IntAct=EBI-2860297, EBI-491549;
Q04917:YWHAH; NbExp=3; IntAct=EBI-2860297, EBI-306940;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20172855,
ECO:0000269|PubMed:8397094}; Multi-pass membrane protein
{ECO:0000269|PubMed:20172855}.
-!- TISSUE SPECIFICITY: Expressed in most tissues. Most abundant in
kidney, bone and liver. {ECO:0000269|PubMed:8397094}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:27160269}.
-!- DISEASE: Jansen metaphyseal chondrodysplasia (JMC) [MIM:156400]:
Rare autosomal dominant disorder characterized by a short-limbed
dwarfism associated with hypercalcemia and normal or low serum
concentrations of the two parathyroid hormones.
{ECO:0000269|PubMed:10487664, ECO:0000269|PubMed:15240651,
ECO:0000269|PubMed:27160269, ECO:0000269|PubMed:7701349,
ECO:0000269|PubMed:8703170, ECO:0000269|PubMed:9178745}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Chondrodysplasia Blomstrand type (BOCD) [MIM:215045]:
Severe skeletal dysplasia. {ECO:0000269|PubMed:9745456}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Enchondromatosis multiple (ENCHOM) [MIM:166000]: A
condition characterized by multiple formation of enchondromas,
benign neoplasms derived from mesodermal cells that form
cartilage. Enchondromas remain within the substance of a cartilage
or bone. Clinical problems caused by enchondromas include skeletal
deformity and the potential for malignant change to osteosarcoma.
{ECO:0000269|PubMed:11850620}. Note=The disease may be caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Eiken skeletal dysplasia (EISD) [MIM:600002]: A rare
skeletal dysplasia characterized by severely retarded
ossification, principally of the epiphyses, pelvis, hands and
feet, as well as by abnormal modeling of the bones in hands and
feet, abnormal persistence of cartilage in the pelvis and mild
growth retardation. {ECO:0000269|PubMed:15525660}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Primary failure of tooth eruption (PFE) [MIM:125350]:
Rare condition that has high penetrance and variable expressivity
and in which tooth retention occurs without evidence of any
obvious mechanical interference. Instead, malfunction of the
eruptive mechanism itself appears to cause nonankylosed permanent
teeth to fail to erupt, although the eruption pathway has been
cleared by bone resorption. {ECO:0000269|PubMed:19061984}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
{ECO:0000305}.
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EMBL; L04308; AAA36525.1; -; mRNA.
EMBL; X68596; CAA48589.1; -; mRNA.
EMBL; U22409; AAB60657.1; -; Genomic_DNA.
EMBL; U22401; AAB60657.1; JOINED; Genomic_DNA.
EMBL; U22402; AAB60657.1; JOINED; Genomic_DNA.
EMBL; U22403; AAB60657.1; JOINED; Genomic_DNA.
EMBL; U22404; AAB60657.1; JOINED; Genomic_DNA.
EMBL; U22405; AAB60657.1; JOINED; Genomic_DNA.
EMBL; U22406; AAB60657.1; JOINED; Genomic_DNA.
EMBL; U22407; AAB60657.1; JOINED; Genomic_DNA.
EMBL; U22408; AAB60657.1; JOINED; Genomic_DNA.
EMBL; U17418; AAA56774.1; -; mRNA.
EMBL; AY449732; AAR18076.1; -; mRNA.
EMBL; BC112221; AAI12222.1; -; mRNA.
EMBL; BC112247; AAI12248.1; -; mRNA.
CCDS; CCDS2747.1; -.
PIR; I38139; A49191.
RefSeq; NP_000307.1; NM_000316.2.
RefSeq; NP_001171673.1; NM_001184744.1.
RefSeq; XP_016862422.1; XM_017006933.1.
UniGene; Hs.1019; -.
PDB; 1BL1; NMR; -; A=168-197.
PDB; 1ET2; Model; -; S=168-469.
PDB; 1ET3; Model; -; S=168-469.
PDB; 3C4M; X-ray; 1.95 A; A/B=29-187.
PDB; 3H3G; X-ray; 1.94 A; A=29-187.
PDB; 3L2J; X-ray; 3.24 A; A/B=29-187.
PDB; 4Z8J; X-ray; 0.95 A; B=586-593.
PDB; 5EMB; X-ray; 0.85 A; B=586-593.
PDBsum; 1BL1; -.
PDBsum; 1ET2; -.
PDBsum; 1ET3; -.
PDBsum; 3C4M; -.
PDBsum; 3H3G; -.
PDBsum; 3L2J; -.
PDBsum; 4Z8J; -.
PDBsum; 5EMB; -.
ProteinModelPortal; Q03431; -.
SMR; Q03431; -.
BioGrid; 111717; 52.
CORUM; Q03431; -.
IntAct; Q03431; 11.
MINT; Q03431; -.
STRING; 9606.ENSP00000321999; -.
BindingDB; Q03431; -.
ChEMBL; CHEMBL1793; -.
DrugBank; DB05829; Parathyroid hormone.
DrugBank; DB06285; Teriparatide.
GuidetoPHARMACOLOGY; 331; -.
TCDB; 9.A.14.4.11; the g-protein-coupled receptor (gpcr) family.
iPTMnet; Q03431; -.
PhosphoSitePlus; Q03431; -.
BioMuta; PTH1R; -.
DMDM; 417555; -.
REPRODUCTION-2DPAGE; Q03431; -.
PaxDb; Q03431; -.
PeptideAtlas; Q03431; -.
PRIDE; Q03431; -.
ProteomicsDB; 58212; -.
TopDownProteomics; Q03431; -.
DNASU; 5745; -.
Ensembl; ENST00000313049; ENSP00000321999; ENSG00000160801.
Ensembl; ENST00000418619; ENSP00000411424; ENSG00000160801.
Ensembl; ENST00000430002; ENSP00000413774; ENSG00000160801.
Ensembl; ENST00000449590; ENSP00000402723; ENSG00000160801.
GeneID; 5745; -.
KEGG; hsa:5745; -.
UCSC; uc003cqm.4; human.
CTD; 5745; -.
DisGeNET; 5745; -.
EuPathDB; HostDB:ENSG00000160801.13; -.
GeneCards; PTH1R; -.
HGNC; HGNC:9608; PTH1R.
HPA; HPA007978; -.
MalaCards; PTH1R; -.
MIM; 125350; phenotype.
MIM; 156400; phenotype.
MIM; 166000; phenotype.
MIM; 168468; gene.
MIM; 215045; phenotype.
MIM; 600002; phenotype.
neXtProt; NX_Q03431; -.
OpenTargets; ENSG00000160801; -.
Orphanet; 50945; Blomstrand lethal chondrodysplasia.
Orphanet; 1077; Dental ankylosis.
Orphanet; 79106; Eiken syndrome.
Orphanet; 296; Enchondromatosis.
Orphanet; 33067; Metaphyseal chondrodysplasia, Jansen type.
PharmGKB; PA33953; -.
eggNOG; KOG4564; Eukaryota.
eggNOG; ENOG410XRS2; LUCA.
GeneTree; ENSGT00760000118800; -.
HOGENOM; HOG000008248; -.
HOVERGEN; HBG008318; -.
InParanoid; Q03431; -.
KO; K04585; -.
OMA; YAGCRVA; -.
OrthoDB; EOG091G0NF8; -.
PhylomeDB; Q03431; -.
TreeFam; TF315710; -.
Reactome; R-HSA-373080; Class B/2 (Secretin family receptors).
Reactome; R-HSA-418555; G alpha (s) signalling events.
SignaLink; Q03431; -.
SIGNOR; Q03431; -.
EvolutionaryTrace; Q03431; -.
GeneWiki; Parathyroid_hormone_1_receptor; -.
GenomeRNAi; 5745; -.
PMAP-CutDB; Q03431; -.
PRO; PR:Q03431; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000160801; -.
CleanEx; HS_PTH1R; -.
ExpressionAtlas; Q03431; baseline and differential.
Genevisible; Q03431; HS.
GO; GO:0016324; C:apical plasma membrane; ISS:BHF-UCL.
GO; GO:0016323; C:basolateral plasma membrane; ISS:BHF-UCL.
GO; GO:0031526; C:brush border membrane; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043235; C:receptor complex; ISS:BHF-UCL.
GO; GO:0004991; F:parathyroid hormone receptor activity; IDA:UniProtKB.
GO; GO:0017046; F:peptide hormone binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IDA:UniProtKB.
GO; GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IDA:UniProtKB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
GO; GO:0045453; P:bone resorption; IEA:Ensembl.
GO; GO:0048469; P:cell maturation; IEA:Ensembl.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0007187; P:G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; TAS:ProtInc.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0002076; P:osteoblast development; IEA:Ensembl.
GO; GO:0007200; P:phospholipase C-activating G-protein coupled receptor signaling pathway; IC:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
GO; GO:0060732; P:positive regulation of inositol phosphate biosynthetic process; ISS:BHF-UCL.
GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
Gene3D; 4.10.1240.10; -; 1.
InterPro; IPR017981; GPCR_2-like.
InterPro; IPR036445; GPCR_2_extracell_dom_sf.
InterPro; IPR001879; GPCR_2_extracellular_dom.
InterPro; IPR002170; GPCR_2_parathyroid_rcpt.
InterPro; IPR000832; GPCR_2_secretin-like.
InterPro; IPR017983; GPCR_2_secretin-like_CS.
PANTHER; PTHR12011:SF24; PTHR12011:SF24; 1.
Pfam; PF00002; 7tm_2; 1.
Pfam; PF02793; HRM; 1.
PRINTS; PR00249; GPCRSECRETIN.
PRINTS; PR00393; PTRHORMONER.
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; Disease mutation;
Disulfide bond; Dwarfism; G-protein coupled receptor; Glycoprotein;
Membrane; Phosphoprotein; Receptor; Reference proteome; Signal;
Transducer; Transmembrane; Transmembrane helix.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 593 Parathyroid hormone/parathyroid hormone-
related peptide receptor.
/FTId=PRO_0000012845.
TOPO_DOM 27 188 Extracellular. {ECO:0000255}.
TRANSMEM 189 212 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 213 219 Cytoplasmic. {ECO:0000255}.
TRANSMEM 220 239 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 240 282 Extracellular. {ECO:0000255}.
TRANSMEM 283 306 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 307 320 Cytoplasmic. {ECO:0000255}.
TRANSMEM 321 342 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 343 361 Extracellular. {ECO:0000255}.
TRANSMEM 362 382 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 383 409 Cytoplasmic. {ECO:0000255}.
TRANSMEM 410 428 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 429 440 Extracellular. {ECO:0000255}.
TRANSMEM 441 463 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 464 593 Cytoplasmic. {ECO:0000255}.
MOTIF 474 477 Important for interaction with G
proteins.
MOD_RES 551 551 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
CARBOHYD 151 151 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 161 161 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 166 166 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 176 176 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 48 117 {ECO:0000244|PDB:3C4M,
ECO:0000244|PDB:3H3G,
ECO:0000244|PDB:3L2J,
ECO:0000269|PubMed:10913300,
ECO:0000269|PubMed:18375760,
ECO:0000269|PubMed:19674967}.
DISULFID 108 148 {ECO:0000244|PDB:3C4M,
ECO:0000244|PDB:3H3G,
ECO:0000244|PDB:3L2J,
ECO:0000269|PubMed:10913300,
ECO:0000269|PubMed:18375760,
ECO:0000269|PubMed:19674967}.
DISULFID 131 170 {ECO:0000244|PDB:3C4M,
ECO:0000244|PDB:3H3G,
ECO:0000244|PDB:3L2J,
ECO:0000269|PubMed:10913300,
ECO:0000269|PubMed:18375760,
ECO:0000269|PubMed:19674967}.
VARIANT 132 132 P -> L (in BOCD; dbSNP:rs121434599).
{ECO:0000269|PubMed:9745456}.
/FTId=VAR_016062.
VARIANT 150 150 R -> C (in ENCHOM; Ollier type; unknown
pathological significance;
dbSNP:rs121434601).
{ECO:0000269|PubMed:11850620}.
/FTId=VAR_016063.
VARIANT 223 223 H -> R (in JMC; constitutively activated;
constitutively increases adenylate
cyclase-activating G-protein coupled
receptor signaling pathway; decreases the
degree of N-glycosylation; does not
affect homodimerization;
dbSNP:rs121434597).
{ECO:0000269|PubMed:27160269,
ECO:0000269|PubMed:7701349,
ECO:0000269|PubMed:8703170,
ECO:0000269|PubMed:9178745}.
/FTId=VAR_003582.
VARIANT 410 410 T -> P (in JMC; constitutively activated;
dbSNP:rs121434598).
{ECO:0000269|PubMed:8703170,
ECO:0000269|PubMed:9178745}.
/FTId=VAR_003583.
VARIANT 410 410 T -> R (in JMC; leads to agonist-
independent cAMP formation which is less
pronounced than that observed with the
Pro-410 mutant; dbSNP:rs121434602).
{ECO:0000269|PubMed:15240651}.
/FTId=VAR_038811.
VARIANT 458 458 I -> R (in JMC; dbSNP:rs121434600).
{ECO:0000269|PubMed:10487664}.
/FTId=VAR_016064.
MUTAGEN 135 135 I->K: Abolishes hormone binding and
homodimerization.
{ECO:0000269|PubMed:20172855}.
MUTAGEN 137 137 D->A: Abolishes hormone binding. No
effect on homodimerization.
{ECO:0000269|PubMed:20172855}.
CONFLICT 471 471 K -> N (in Ref. 2). {ECO:0000305}.
CONFLICT 473 473 S -> C (in Ref. 2). {ECO:0000305}.
HELIX 34 55 {ECO:0000244|PDB:3H3G}.
STRAND 126 130 {ECO:0000244|PDB:3H3G}.
STRAND 143 148 {ECO:0000244|PDB:3H3G}.
STRAND 152 154 {ECO:0000244|PDB:3C4M}.
STRAND 160 163 {ECO:0000244|PDB:3H3G}.
TURN 168 173 {ECO:0000244|PDB:3H3G}.
HELIX 180 185 {ECO:0000244|PDB:1BL1}.
HELIX 188 196 {ECO:0000244|PDB:1BL1}.
STRAND 588 592 {ECO:0000244|PDB:5EMB}.
SEQUENCE 593 AA; 66361 MW; DA1400640A6C7F2B CRC64;
MGTARIAPGL ALLLCCPVLS SAYALVDADD VMTKEEQIFL LHRAQAQCEK RLKEVLQRPA
SIMESDKGWT SASTSGKPRK DKASGKLYPE SEEDKEAPTG SRYRGRPCLP EWDHILCWPL
GAPGEVVAVP CPDYIYDFNH KGHAYRRCDR NGSWELVPGH NRTWANYSEC VKFLTNETRE
REVFDRLGMI YTVGYSVSLA SLTVAVLILA YFRRLHCTRN YIHMHLFLSF MLRAVSIFVK
DAVLYSGATL DEAERLTEEE LRAIAQAPPP PATAAAGYAG CRVAVTFFLY FLATNYYWIL
VEGLYLHSLI FMAFFSEKKY LWGFTVFGWG LPAVFVAVWV SVRATLANTG CWDLSSGNKK
WIIQVPILAS IVLNFILFIN IVRVLATKLR ETNAGRCDTR QQYRKLLKST LVLMPLFGVH
YIVFMATPYT EVSGTLWQVQ MHYEMLFNSF QGFFVAIIYC FCNGEVQAEI KKSWSRWTLA
LDFKRKARSG SSSYSYGPMV SHTSVTNVGP RVGLGLPLSP RLLPTATTNG HPQLPGHAKP
GTPALETLET TPPAMAAPKD DGFLNGSCSG LDEEASGPER PPALLQEEWE TVM


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