Search by BoMiProt ID - Bomi7830


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 IdQ1LZF7
Milk FractionWhey
Ref Sequence Id NP_001068800.1
Aminoacid Length 589
Molecular Weight 65862
Fasta Sequence https://www.uniprot.org/uniprot/Q1LZF7.fasta
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