PTH1R_RAT
ID PTH1R_RAT Reviewed; 591 AA.
AC P25961;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Parathyroid hormone/parathyroid hormone-related peptide receptor;
DE AltName: Full=PTH/PTHrP type I receptor;
DE Short=PTH/PTHr receptor;
DE AltName: Full=Parathyroid hormone 1 receptor;
DE Short=PTH1 receptor;
DE Flags: Precursor;
GN Name=Pth1r; Synonyms=Pthr, Pthr1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PTH AND PTHLH, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Bone;
RX PubMed=1313566; DOI=10.1073/pnas.89.7.2732;
RA Abou-Samra A.-B., Jueppner H., Force T., Freeman M.W., Kong X.-F.,
RA Schipani E., Urena P., Richards J., Bonventre J.V., Potts J.T. Jr.,
RA Kronenberg H.M., Segre G.V.;
RT "Expression cloning of a common receptor for parathyroid hormone and
RT parathyroid hormone-related peptide from rat osteoblast-like cells: a
RT single receptor stimulates intracellular accumulation of both cAMP and
RT inositol trisphosphates and increases intracellular free calcium.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:2732-2736(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8020952; DOI=10.1006/geno.1994.1122;
RA Pausova Z., Bourdon J., Clayton D., Mattei M.-G., Seldin M.F., Janicic N.,
RA Riviere M., Szpirer J., Levan G., Szpirer C.;
RT "Cloning of a parathyroid hormone/parathyroid hormone-related peptide
RT receptor (PTHR) cDNA from a rat osteosarcoma (UMR 106) cell line:
RT chromosomal assignment of the gene in the human, mouse, and rat genomes.";
RL Genomics 20:20-26(1994).
CC -!- FUNCTION: Receptor for parathyroid hormone and for parathyroid hormone-
CC related peptide. The activity of this receptor is mediated by G
CC proteins which activate adenylyl cyclase and also a
CC phosphatidylinositol-calcium second messenger system.
CC {ECO:0000269|PubMed:1313566}.
CC -!- SUBUNIT: Interacts (via N-terminal extracellular domain) with PTHLH and
CC PTH (PubMed:1313566). Homodimer in the absence of bound ligand. Peptide
CC hormone binding leads to dissociation of the homodimer (By similarity).
CC {ECO:0000250|UniProtKB:Q03431, ECO:0000269|PubMed:1313566}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1313566};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q03431}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
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DR EMBL; M77184; AAA41811.1; -; mRNA.
DR EMBL; L19475; AAA68098.1; -; mRNA.
DR PIR; I54195; I54195.
DR RefSeq; NP_064458.1; NM_020073.2.
DR RefSeq; XP_006244060.1; XM_006243998.3.
DR RefSeq; XP_006244061.1; XM_006243999.2.
DR AlphaFoldDB; P25961; -.
DR SMR; P25961; -.
DR BioGRID; 248587; 1.
DR CORUM; P25961; -.
DR DIP; DIP-46025N; -.
DR STRING; 10116.ENSRNOP00000028435; -.
DR BindingDB; P25961; -.
DR ChEMBL; CHEMBL6038; -.
DR DrugCentral; P25961; -.
DR GuidetoPHARMACOLOGY; 331; -.
DR GlyGen; P25961; 4 sites.
DR iPTMnet; P25961; -.
DR PhosphoSitePlus; P25961; -.
DR PaxDb; P25961; -.
DR Ensembl; ENSRNOT00000028435; ENSRNOP00000028435; ENSRNOG00000020948.
DR GeneID; 56813; -.
DR KEGG; rno:56813; -.
DR UCSC; RGD:3442; rat.
DR CTD; 5745; -.
DR RGD; 3442; Pth1r.
DR eggNOG; KOG4564; Eukaryota.
DR GeneTree; ENSGT00940000158574; -.
DR HOGENOM; CLU_002753_4_3_1; -.
DR InParanoid; P25961; -.
DR OMA; ESDKGWM; -.
DR OrthoDB; 651627at2759; -.
DR PhylomeDB; P25961; -.
DR TreeFam; TF315710; -.
DR Reactome; R-RNO-373080; Class B/2 (Secretin family receptors).
DR PRO; PR:P25961; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000020948; Expressed in adult mammalian kidney and 18 other tissues.
DR Genevisible; P25961; RN.
DR GO; GO:0016324; C:apical plasma membrane; IDA:BHF-UCL.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:BHF-UCL.
DR GO; GO:0031526; C:brush border membrane; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0043235; C:receptor complex; IDA:BHF-UCL.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0004991; F:parathyroid hormone receptor activity; IDA:BHF-UCL.
DR GO; GO:0017046; F:peptide hormone binding; IDA:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0043621; F:protein self-association; ISO:RGD.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0030282; P:bone mineralization; ISO:RGD.
DR GO; GO:0045453; P:bone resorption; ISO:RGD.
DR GO; GO:0048469; P:cell maturation; ISO:RGD.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:RGD.
DR GO; GO:0002062; P:chondrocyte differentiation; ISO:RGD.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IMP:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0001503; P:ossification; ISO:RGD.
DR GO; GO:0002076; P:osteoblast development; ISO:RGD.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:RGD.
DR GO; GO:0060732; P:positive regulation of inositol phosphate biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0001501; P:skeletal system development; ISO:RGD.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR002170; GPCR_2_parathyroid_rcpt.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR PANTHER; PTHR45620:SF27; PTHR45620:SF27; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF02793; HRM; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
DR PRINTS; PR00393; PTRHORMONER.
DR SMART; SM00008; HormR; 1.
DR SUPFAM; SSF111418; SSF111418; 1.
DR PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..591
FT /note="Parathyroid hormone/parathyroid hormone-related
FT peptide receptor"
FT /id="PRO_0000012848"
FT TOPO_DOM 27..188
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..212
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..219
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..239
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..282
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..306
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..320
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..342
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..361
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..409
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..428
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 429..440
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..463
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 464..591
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 67..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 474..477
FT /note="Important for interaction with G proteins"
FT /evidence="ECO:0000250"
FT COMPBIAS 79..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..117
FT /evidence="ECO:0000250|UniProtKB:Q03431"
FT DISULFID 108..148
FT /evidence="ECO:0000250|UniProtKB:Q03431"
FT DISULFID 131..170
FT /evidence="ECO:0000250|UniProtKB:Q03431"
SQ SEQUENCE 591 AA; 66261 MW; 21944F3051B9E9C1 CRC64;
MGAARIAPSL ALLLCCPVLS SAYALVDADD VFTKEEQIFL LHRAQAQCDK LLKEVLHTAA
NIMESDKGWT PASTSGKPRK EKASGKFYPE SKENKDVPTG SRRRGRPCLP EWDNIVCWPL
GAPGEVVAVP CPDYIYDFNH KGHAYRRCDR NGSWEVVPGH NRTWANYSEC LKFMTNETRE
REVFDRLGMI YTVGYSMSLA SLTVAVLILA YFRRLHCTRN YIHMHMFLSF MLRAASIFVK
DAVLYSGFTL DEAERLTEEE LHIIAQVPPP PAAAAVGYAG CRVAVTFFLY FLATNYYWIL
VEGLYLHSLI FMAFFSEKKY LWGFTIFGWG LPAVFVAVWV GVRATLANTG CWDLSSGHKK
WIIQVPILAS VVLNFILFIN IIRVLATKLR ETNAGRCDTR QQYRKLLRST LVLVPLFGVH
YTVFMALPYT EVSGTLWQIQ MHYEMLFNSF QGFFVAIIYC FCNGEVQAEI RKSWSRWTLA
LDFKRKARSG SSSYSYGPMV SHTSVTNVGP RAGLSLPLSP RLPPATTNGH SQLPGHAKPG
APATETETLP VTMAVPKDDG FLNGSCSGLD EEASGSARPP PLLQEEWETV M
