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   27-MAR-2024, entry version 172.
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   GlyCosmos; P25961; 4 sites, No reported glycans.
DR   GlyGen; P25961; 4 sites.
DR   iPTMnet; P25961; -.
DR   PhosphoSitePlus; P25961; -.
DR   PaxDb; 10116-ENSRNOP00000028435; -.
DR   Ensembl; ENSRNOT00000028435.5; ENSRNOP00000028435.3; ENSRNOG00000020948.6.
DR   Ensembl; ENSRNOT00055012880; ENSRNOP00055010265; ENSRNOG00055007695.
DR   Ensembl; ENSRNOT00060034689; ENSRNOP00060028487; ENSRNOG00060020032.
DR   Ensembl; ENSRNOT00065007057; ENSRNOP00065004870; ENSRNOG00065004853.
DR   GeneID; 56813; -.
DR   KEGG; rno:56813; -.
DR   UCSC; RGD:3442; rat.
DR   AGR; RGD:3442; -.
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   OrthoDB; 5397182at2759; -.
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 cell types or tissues.
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:0005886; C:plasma membrane; ISO: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: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:0008283; P:cell population proliferation; ISO:RGD.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
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:0006874; P:intracellular calcium ion homeostasis; 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; GPCR, family 2, extracellular hormone receptor domain; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
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; PARATHYROID HORMONE_PARATHYROID HORMONE-RELATED PEPTIDE RECEPTOR; 1.
DR   PANTHER; PTHR45620; PDF RECEPTOR-LIKE PROTEIN-RELATED; 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; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   SUPFAM; SSF111418; Hormone receptor domain; 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.
DR   Genevisible; P25961; RN.
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
//