Q03431 · PTH1R_HUMAN
- ProteinParathyroid hormone/parathyroid hormone-related peptide receptor
- GenePTH1R
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids593 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameParathyroid hormone/parathyroid hormone-related peptide receptor
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ03431
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 27-188 | Extracellular | ||||
Sequence: DADDVMTKEEQIFLLHRAQAQCEKRLKEVLQRPASIMESDKGWTSASTSGKPRKDKASGKLYPESEEDKEAPTGSRYRGRPCLPEWDHILCWPLGAPGEVVAVPCPDYIYDFNHKGHAYRRCDRNGSWELVPGHNRTWANYSECVKFLTNETREREVFDRLG | ||||||
Transmembrane | 189-212 | Helical; Name=1 | ||||
Sequence: MIYTVGYSVSLASLTVAVLILAYF | ||||||
Topological domain | 213-219 | Cytoplasmic | ||||
Sequence: RRLHCTR | ||||||
Transmembrane | 220-239 | Helical; Name=2 | ||||
Sequence: NYIHMHLFLSFMLRAVSIFV | ||||||
Topological domain | 240-282 | Extracellular | ||||
Sequence: KDAVLYSGATLDEAERLTEEELRAIAQAPPPPATAAAGYAGCR | ||||||
Transmembrane | 283-306 | Helical; Name=3 | ||||
Sequence: VAVTFFLYFLATNYYWILVEGLYL | ||||||
Topological domain | 307-320 | Cytoplasmic | ||||
Sequence: HSLIFMAFFSEKKY | ||||||
Transmembrane | 321-342 | Helical; Name=4 | ||||
Sequence: LWGFTVFGWGLPAVFVAVWVSV | ||||||
Topological domain | 343-361 | Extracellular | ||||
Sequence: RATLANTGCWDLSSGNKKW | ||||||
Transmembrane | 362-382 | Helical; Name=5 | ||||
Sequence: IIQVPILASIVLNFILFINIV | ||||||
Topological domain | 383-409 | Cytoplasmic | ||||
Sequence: RVLATKLRETNAGRCDTRQQYRKLLKS | ||||||
Transmembrane | 410-428 | Helical; Name=6 | ||||
Sequence: TLVLMPLFGVHYIVFMATP | ||||||
Topological domain | 429-440 | Extracellular | ||||
Sequence: YTEVSGTLWQVQ | ||||||
Transmembrane | 441-463 | Helical; Name=7 | ||||
Sequence: MHYEMLFNSFQGFFVAIIYCFCN | ||||||
Topological domain | 464-593 | Cytoplasmic | ||||
Sequence: GEVQAEIKKSWSRWTLALDFKRKARSGSSSYSYGPMVSHTSVTNVGPRVGLGLPLSPRLLPTATTNGHPQLPGHAKPGTPALETLETTPPAMAAPKDDGFLNGSCSGLDEEASGPERPPALLQEEWETVM |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Metaphyseal chondrodysplasia, Jansen type (MCDJ)
- Note
- DescriptionA rare autosomal dominant disorder characterized by a short-limbed dwarfism associated with hypercalcemia and normal or low serum concentrations of the two parathyroid hormones.
- See alsoMIM:156400
Natural variants in MCDJ
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_003582 | 223 | H>R | in MCDJ; 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 | |
VAR_003583 | 410 | T>P | in MCDJ; constitutively activated; dbSNP:rs121434598 | |
VAR_038811 | 410 | T>R | in MCDJ; leads to agonist-independent cAMP formation which is less pronounced than that observed with the Pro-410 mutant; dbSNP:rs121434602 | |
VAR_016064 | 458 | I>R | in MCDJ; dbSNP:rs121434600 |
Chondrodysplasia Blomstrand type (BOCD)
- Note
- DescriptionSevere skeletal dysplasia.
- See alsoMIM:215045
Natural variants in BOCD
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_016062 | 132 | P>L | in BOCD; dbSNP:rs121434599 |
Eiken syndrome (EKNS)
- Note
- DescriptionAn 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.
- See alsoMIM:600002
Primary failure of tooth eruption (PFE)
- Note
- DescriptionRare 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.
- See alsoMIM:125350
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_016062 | 132 | in BOCD; dbSNP:rs121434599 | |||
Sequence: P → L | ||||||
Mutagenesis | 135 | Abolishes hormone binding and homodimerization. | ||||
Sequence: I → K | ||||||
Mutagenesis | 137 | Abolishes hormone binding. No effect on homodimerization. | ||||
Sequence: D → A | ||||||
Natural variant | VAR_016063 | 150 | in dbSNP:rs121434601 | |||
Sequence: R → C | ||||||
Natural variant | VAR_003582 | 223 | in MCDJ; 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 | |||
Sequence: H → R | ||||||
Natural variant | VAR_003583 | 410 | in MCDJ; constitutively activated; dbSNP:rs121434598 | |||
Sequence: T → P | ||||||
Natural variant | VAR_038811 | 410 | in MCDJ; leads to agonist-independent cAMP formation which is less pronounced than that observed with the Pro-410 mutant; dbSNP:rs121434602 | |||
Sequence: T → R | ||||||
Natural variant | VAR_016064 | 458 | in MCDJ; dbSNP:rs121434600 | |||
Sequence: I → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 738 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-26 | |||||
Sequence: MGTARIAPGLALLLCCPVLSSAYALV | ||||||
Chain | PRO_0000012845 | 27-593 | Parathyroid hormone/parathyroid hormone-related peptide receptor | |||
Sequence: DADDVMTKEEQIFLLHRAQAQCEKRLKEVLQRPASIMESDKGWTSASTSGKPRKDKASGKLYPESEEDKEAPTGSRYRGRPCLPEWDHILCWPLGAPGEVVAVPCPDYIYDFNHKGHAYRRCDRNGSWELVPGHNRTWANYSECVKFLTNETREREVFDRLGMIYTVGYSVSLASLTVAVLILAYFRRLHCTRNYIHMHLFLSFMLRAVSIFVKDAVLYSGATLDEAERLTEEELRAIAQAPPPPATAAAGYAGCRVAVTFFLYFLATNYYWILVEGLYLHSLIFMAFFSEKKYLWGFTVFGWGLPAVFVAVWVSVRATLANTGCWDLSSGNKKWIIQVPILASIVLNFILFINIVRVLATKLRETNAGRCDTRQQYRKLLKSTLVLMPLFGVHYIVFMATPYTEVSGTLWQVQMHYEMLFNSFQGFFVAIIYCFCNGEVQAEIKKSWSRWTLALDFKRKARSGSSSYSYGPMVSHTSVTNVGPRVGLGLPLSPRLLPTATTNGHPQLPGHAKPGTPALETLETTPPAMAAPKDDGFLNGSCSGLDEEASGPERPPALLQEEWETVM | ||||||
Disulfide bond | 48↔117 | |||||
Sequence: CEKRLKEVLQRPASIMESDKGWTSASTSGKPRKDKASGKLYPESEEDKEAPTGSRYRGRPCLPEWDHILC | ||||||
Disulfide bond | 108↔148 | |||||
Sequence: CLPEWDHILCWPLGAPGEVVAVPCPDYIYDFNHKGHAYRRC | ||||||
Disulfide bond | 131↔170 | |||||
Sequence: CPDYIYDFNHKGHAYRRCDRNGSWELVPGHNRTWANYSEC | ||||||
Glycosylation | 151 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 161 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 166 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 176 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 551 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
N-glycosylated.
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Tissue specificity
Expressed in most tissues. Most abundant in kidney, bone and liver.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts (via N-terminal extracellular domain) with PTHLH and PTH (PubMed:10913300, PubMed:18375760, PubMed:19674967, PubMed:8397094).
Homodimer in the absence of bound ligand. Peptide hormone binding leads to dissociation of the homodimer (PubMed:19674967, PubMed:20172855).
Homodimer in the absence of bound ligand. Peptide hormone binding leads to dissociation of the homodimer (PubMed:19674967, PubMed:20172855).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q03431 | CTNNB1 P35222 | 4 | EBI-2860297, EBI-491549 | |
BINARY | Q03431 | GPANK1 O95872 | 3 | EBI-2860297, EBI-751540 | |
BINARY | Q03431 | GUCD1 Q96NT3-2 | 3 | EBI-2860297, EBI-11978177 | |
BINARY | Q03431 | HOXA1 P49639 | 3 | EBI-2860297, EBI-740785 | |
BINARY | Q03431 | MKRN3 Q13064 | 3 | EBI-2860297, EBI-2340269 | |
BINARY | Q03431 | PTH P01270 | 6 | EBI-2860297, EBI-716817 | |
BINARY | Q03431 | PTHLH P12272 | 4 | EBI-2860297, EBI-2372758 | |
BINARY | Q03431 | SMARCC1 Q92922 | 3 | EBI-2860297, EBI-355653 | |
BINARY | Q03431 | STK16 O75716 | 3 | EBI-2860297, EBI-749295 | |
BINARY | Q03431 | TEKT4 Q8WW24 | 3 | EBI-2860297, EBI-750487 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 66-102 | Disordered | ||||
Sequence: DKGWTSASTSGKPRKDKASGKLYPESEEDKEAPTGSR | ||||||
Compositional bias | 79-101 | Basic and acidic residues | ||||
Sequence: RKDKASGKLYPESEEDKEAPTGS | ||||||
Motif | 474-477 | Important for interaction with G proteins | ||||
Sequence: WSRW | ||||||
Region | 524-593 | Disordered | ||||
Sequence: PTATTNGHPQLPGHAKPGTPALETLETTPPAMAAPKDDGFLNGSCSGLDEEASGPERPPALLQEEWETVM |
Sequence similarities
Belongs to the G-protein coupled receptor 2 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Protein family/group databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length593
- Mass (Da)66,361
- Last updated1993-10-01 v1
- ChecksumDA1400640A6C7F2B
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 79-101 | Basic and acidic residues | ||||
Sequence: RKDKASGKLYPESEEDKEAPTGS | ||||||
Sequence conflict | 471 | in Ref. 2 | ||||
Sequence: K → N | ||||||
Sequence conflict | 473 | in Ref. 2 | ||||
Sequence: S → C |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L04308 EMBL· GenBank· DDBJ | AAA36525.1 EMBL· GenBank· DDBJ | mRNA | ||
X68596 EMBL· GenBank· DDBJ | CAA48589.1 EMBL· GenBank· DDBJ | mRNA | ||
U22409 EMBL· GenBank· DDBJ | AAB60657.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U22401 EMBL· GenBank· DDBJ | AAB60657.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U22402 EMBL· GenBank· DDBJ | AAB60657.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U22403 EMBL· GenBank· DDBJ | AAB60657.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U22404 EMBL· GenBank· DDBJ | AAB60657.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U22405 EMBL· GenBank· DDBJ | AAB60657.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U22406 EMBL· GenBank· DDBJ | AAB60657.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U22407 EMBL· GenBank· DDBJ | AAB60657.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U22408 EMBL· GenBank· DDBJ | AAB60657.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U17418 EMBL· GenBank· DDBJ | AAA56774.1 EMBL· GenBank· DDBJ | mRNA | ||
AY449732 EMBL· GenBank· DDBJ | AAR18076.1 EMBL· GenBank· DDBJ | mRNA | ||
BC112221 EMBL· GenBank· DDBJ | AAI12222.1 EMBL· GenBank· DDBJ | mRNA | ||
BC112247 EMBL· GenBank· DDBJ | AAI12248.1 EMBL· GenBank· DDBJ | mRNA |