PTH1R
entrez
5745
canonical
uniprot
Q03431
canonical
ensembl
ENSG00000160801
resolver
ensp
ENSP00000321999
resolver
ensp
ENSP00000402723
resolver
ensp
ENSP00000411424
resolver
ensp
ENSP00000413774
resolver
ensp
ENSP00000547413
resolver
ensp
ENSP00000547414
resolver
ensp
ENSP00000547415
resolver
ensp
ENSP00000547416
resolver
ensp
ENSP00000547417
resolver
ensp
ENSP00000629022
resolver
ensp
ENSP00000677584
resolver
enst
ENST00000313049
resolver
enst
ENST00000418619
resolver
enst
ENST00000430002
resolver
enst
ENST00000449590
resolver
enst
ENST00000877354
resolver
enst
ENST00000877355
resolver
enst
ENST00000877356
resolver
enst
ENST00000877358
resolver
genesymbol
PTH1R
resolver
genesymbol_syn
PTHR
resolver
genesymbol_syn
PTHR1
resolver
hgnc
HGNC:9608
resolver
uniprot
Q0VGD7
resolver
uniprot
Q2M1U3
resolver
uniprot_entry
PTH1R_HUMAN
resolver
uniprot_entry
Q0VGD7_HUMAN
resolver
uniprot_sec
Q2M1U3
resolver
amino_acid_sequence
MGTARIAPGLALLLCCPVLSSAYALVDADDVMTKEEQIFLLHRAQAQCEKRLKEVLQRPASIMESDKGWTSASTSGKPRKDKASGKLYPESEEDKEAPTGSRYRGRPCLPEWDHILCWPLGAPGEVVAVPCPDYIYDFNHKGHAYRRCDRNGSWELVPGHNRTWANYSECVKFLTNETREREVFDRLGMIYTVGYSVSLASLTVAVLILAYFRRLHCTRNYIHMHLFLSFMLRAVSIFVKDAVLYSGATLDEAERLTEEELRAIAQAPPPPATAAAGYAGCRVAVTFFLYFLATNYYWILVEGLYLHSLIFMAFFSEKKYLWGFTVFGWGLPAVFVAVWVSVRATLANTGCWDLSSGNKKWIIQVPILASIVLNFILFINIVRVLATKLRETNAGRCDTRQQYRKLLKSTLVLMPLFGVHYIVFMATPYTEVSGTLWQVQMHYEMLFNSFQGFFVAIIYCFCNGEVQAEIKKSWSRWTLALDFKRKARSGSSSYSYGPMVSHTSVTNVGPRVGLGLPLSPRLLPTATTNGHPQLPGHAKPGTPALETLETTPPAMAAPKDDGFLNGSCSGLDEEASGPERPPALLQEEWETVM
uniprot
proteins
disease_involvement
DISEASE: Metaphyseal chondrodysplasia, Jansen type (MCDJ) [MIM:156400]: A 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 variants 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 variants affecting the gene represented in this entry.; DISEASE: Eiken syndrome (EKNS) [MIM:600002]: An autosomal recessive 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 variants 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 variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: G protein-coupled receptor for parathyroid hormone (PTH) and for parathyroid hormone-related peptide (PTHLH) (PubMed:10913300, PubMed:11773434, PubMed:18375760, PubMed:19674967, PubMed:27160269, PubMed:30975883, PubMed:35932760, PubMed:8397094). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as adenylate cyclase (cAMP) (PubMed:30975883, PubMed:35932760). PTH1R is coupled to G(s) G alpha proteins and mediates activation of adenylate cyclase activity (PubMed:20172855, PubMed:30975883, PubMed:35932760). PTHLH dissociates from PTH1R more rapidly than PTH; as consequence, the cAMP response induced by PTHLH decays faster than the response induced by PTH (PubMed:35932760). {ECO:0000269|PubMed:10913300, ECO:0000269|PubMed:11773434, ECO:0000269|PubMed:18375760, ECO:0000269|PubMed:19674967, ECO:0000269|PubMed:20172855, ECO:0000269|PubMed:27160269, ECO:0000269|PubMed:30975883, ECO:0000269|PubMed:35932760, ECO:0000269|PubMed:8397094}.
uniprot
proteins
mass_dalton
66361
uniprot
proteins
mutagenesis
MUTAGEN 35; /note="E->A: Slightly increased parathyroid hormone (PTH) efficiency and decreased potency for parathyroid hormone-related peptide (PTHLH)."; /evidence="ECO:0000269|PubMed:35932760"; MUTAGEN 135; /note="I->K: Abolishes hormone binding and homodimerization."; /evidence="ECO:0000269|PubMed:20172855"; MUTAGEN 137; /note="D->A: Abolishes parathyroid hormone (PTH) and parathyroid hormone-related peptide (PTHLH) hormone-binding. No effect on homodimerization."; /evidence="ECO:0000269|PubMed:20172855, ECO:0000269|PubMed:35932760"; MUTAGEN 195; /note="Y->F: Decreased potencies of parathyroid hormone (PTH) and parathyroid hormone-related peptide (PTHLH)."; /evidence="ECO:0000269|PubMed:35932760"; MUTAGEN 233; /note="R->A: Decreased potencies of parathyroid hormone (PTH) and parathyroid hormone-related peptide (PTHLH)."; /evidence="ECO:0000269|PubMed:35932760
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:27160269}.; PTM: Phosphorylated on multiple serine residues; these phosphorylations are important for PTH-dependent internalization. {ECO:0000269|PubMed:11773434}.
uniprot
proteins
protein_family
G protein-coupled receptor 2 family
uniprot
proteins
pubmed
10487664
uniprot
proteins
pubmed
10913300
uniprot
proteins
pubmed
11773434
uniprot
proteins
pubmed
11850620
uniprot
proteins
pubmed
15240651
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15523647
uniprot
proteins
pubmed
15525660
uniprot
proteins
pubmed
18375760
uniprot
proteins
pubmed
18611381
uniprot
proteins
pubmed
19061984
uniprot
proteins
pubmed
19674967
uniprot
proteins
pubmed
20172855
uniprot
proteins
pubmed
21827955
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
27160269
uniprot
proteins
pubmed
30975883
uniprot
proteins
pubmed
35932760
uniprot
proteins
pubmed
7701349
uniprot
proteins
pubmed
7745008
uniprot
proteins
pubmed
8386612
uniprot
proteins
pubmed
8397094
uniprot
proteins
pubmed
8703170
uniprot
proteins
pubmed
9178745
uniprot
proteins
pubmed
9737850
uniprot
proteins
pubmed
9745456
uniprot
proteins
sequence_length
593
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20172855, ECO:0000269|PubMed:8397094}; Multi-pass membrane protein {ECO:0000269|PubMed:20172855}.
uniprot
proteins
transmembrane_region
TRANSMEM 187..211; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:30975883, ECO:0007744|PDB:6NBF, ECO:0007744|PDB:6NBH, ECO:0007744|PDB:6NBI"; TRANSMEM 220..241; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:30975883, ECO:0007744|PDB:6NBF, ECO:0007744|PDB:6NBH, ECO:0007744|PDB:6NBI"; TRANSMEM 283..307; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:30975883, ECO:0007744|PDB:6NBF, ECO:0007744|PDB:6NBH, ECO:0007744|PDB:6NBI"; TRANSMEM 321..342; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:30975883, ECO:0007744|PDB:6NBF, ECO:0007744|PDB:6NBH, ECO:0007744|PDB:6NBI"; TRANSMEM 358..382; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:30975883, ECO:0007744|PDB:6NBF, ECO:0007744|PDB:6NBH, ECO:0007744|PDB:6NBI"; TRANSMEM 407..426; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:30975883, ECO:0007744|PDB:6NBF, ECO:0007744|PDB:6NBH, ECO:0007744|PDB:6NBI"; TRANSMEM 435..462; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:30975883, ECO:0007744|PDB:6NBF, ECO:0007744|PDB:6NBH, ECO:0007744|PDB:6NBI
uniprot
proteins