Primary Information |
|---|
| BoMiProt ID | Bomi7830 |
|---|
| Protein Name | Parathyroid hormone/parathyroid hormone-related peptide receptor/PTH/PTHrP type I receptor/Parathyroid hormone 1 receptor |
|---|
| Organism | Bos taurus |
|---|
| Uniprot ID | Q1LZF7 |
|---|
| Milk Fraction | Whey |
|---|
| Ref Sequence ID | NP_001068800.1 |
|---|
| Aminoacid Length | 589 |
|---|
| Molecular Weight | 65862 |
|---|
| FASTA Sequence |
Download |
|---|
| Gene Name | PTH1R/PTHR1 |
|---|
| Gene ID | 507783 |
|---|
| Protein Existence Status | reviewed |
|---|
Secondary Information |
|---|
| Protein Function | is a major regulator of mineral ion homeostasis and bone metabolism. PTH is secreted from the parathyroid glands,binds to PTH1R and controls mineral ion homeostasis by triggering calcium reabsorption and phosphate secretion in the kidney as well as calcium release from the bone. |
|---|
| Biochemical Properties | G-protein coupled receptor that predominantly signals through GS alpha subunit (GαS)/adenylyl cyclase/cyclic adenosine monophosphate (cAMP)/protein kinase A (PKA) and less robustly through GQ alpha subunit (GαQ)/phospholipase C (PLC)/protein kinase C (PKC) signaling cascades to mediate gene transcription and cell fate . Contains a relatively large N-terminal extracellular domain (ECD),in addition to the canonical hepta-helical bundle (helices I–VII) of the transmembrane domain (TMD), which when activated couples to intracellular effector proteins.ECD is critically involved in peptide hormone binding |
|---|
| PTMs | N-glycosylated,disulfide bond formation,phosphorylation |
|---|
Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q1LZF7|PTH1R_BOVIN Parathyroid hormone/parathyroid hormone-related peptide receptor OS=Bos taurus OX=9913 GN=PTH1R PE=2 SV=1
MGAARIAPGLALLLCCPVLSSAYALVDADDVMTKEEQIFLLHRAQAQCEKRLKEVLQRPA
DIMESDKGWASASTSGKPKKEKPSGKLHPESEEDKEVPTGSRPRGRPCLPEWDHILCWPL
GAPGEVVAMPCPDYIYDFNHKGHAYRRCDRN*151GSWELVPGHN*161RTWAN*166YSECVKFLTN*176ETREREVFDRLGMIYTVGYSVSLASLTVAVLILAYFRRLHCTRNYIHMHLFLSFMLRAVSIFVK
DAVLYSGTALDEAERLTEEELRAIAQAPPPPAAAAGYVGCRVAVTFFLYFLATNYYWILV
EGLYLHSLIFMAFFSEKKYLWGFTVFGWGLPAIFVAVWVSVRATLANTGCWDLSSGNKKW
IIQVPILASIVLNFILFINIVRVLATKLRETNAGRCDTRQQYRKLLKSTLVLMPLFGVHY
IVFMATPYTEVSGTLWQVQMHYEMLFNSFQGFFVAIIYCFCNGEVQAEIKKSWSRWTLAL
DFKRKARSGSSSYSYGPMVSHTSVTNVGPRTGLGLPLSPRLLPAATTNGHPPLPGHTKSG
SPALQATPPAVAAPKEDGFLNGSCSGLDEEACAPERPPVLLQEEWETVM
|
|---|
| Predicted Disorder Regions | 66-106, 494-589 |
|---|
| DisProt Annotation | |
|---|
| TM Helix Prediction | 7TMHs; (188-210), (221-239), (277-299), (319-341), (360-382), (408-426), (445-463) |
|---|
| Significance of PTMs | There are total 9 sites of phosphorylation in the Cterminal tail of PTH1R.Mutational analysis revealed identified two clusters of serine and threonine residues (Ser489-Ser495 and Ser501-Thr506) specifically responsible for the majority of PTH-induced receptor phosphorylation. and involved in recruitment of arrestin3. |
|---|
| Bibliography | 1.Ehrenmann J, Schöppe J, Klenk C, Plückthun A. New views into class B GPCRs from the crystal structure of PTH1R. FEBS J. 2019 Dec;286(24):4852-4860. doi: 10.1111/febs.15115. Epub 2019 Nov 18. PMID: 31670461. 2.Diana Zindel, Sandra Engel, Andrew R. Bottrill, Jean-Philippe Pin, Laurent Prézeau, Andrew B. Tobin, Moritz Bünemann, Cornelius Krasel, Adrian J. Butcher; Identification of key phosphorylation sites in PTH1R that determine arrestin3 binding and fine-tune receptor signaling. Biochem J 15 November 2016; 473 (22): 4173–4192. doi: https://doi.org/10.1042/BCJ20160740 |
|---|
