ID   PTH1R_MOUSE             Reviewed;         591 AA.
AC   P41593; Q62119; Q80WU8;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   04-NOV-2026, entry version 198.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=C3H/HEHA;
RX   PubMed=7524627; DOI=10.1016/0925-4773(94)90093-0;
RA   Karperien M., van Dijk T.B., Hoeijmakers T., Cremers F., Abou-Samra A.-B.,
RA   Boonstra J., de Laat S.W., Defize L.H.K.;
RT   "Expression pattern of parathyroid hormone/parathyroid hormone related
RT   peptide receptor mRNA in mouse postimplantation embryos indicates
RT   involvement in multiple developmental processes.";
RL   Mech. Dev. 47:29-42(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/cJ;
RX   PubMed=8197183; DOI=10.1073/pnas.91.11.5051;
RA   McCuaig K.A., Clarke J.C., White J.H.;
RT   "Molecular cloning of the gene encoding the mouse parathyroid
RT   hormone/parathyroid hormone-related peptide receptor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:5051-5055(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: G protein-coupled receptor for parathyroid hormone (PTH) and
CC       for parathyroid hormone-related peptide (PTHLH) (PubMed:8197183).
CC       Ligand binding causes a conformation change that triggers signaling via
CC       guanine nucleotide-binding proteins (G proteins) and modulates the
CC       activity of downstream effectors, such as adenylate cyclase (cAMP) (By
CC       similarity). PTH1R is coupled to G(s) G alpha proteins and mediates
CC       activation of adenylate cyclase activity. PTHLH dissociates from PTH1R
CC       more rapidly than PTH; as consequence, the cAMP response induced by
CC       PTHLH decays faster than the response induced by PTH (By similarity).
CC       {ECO:0000250|UniProtKB:Q03431, ECO:0000269|PubMed:8197183}.
CC   -!- SUBUNIT: Homodimer in the absence of bound ligand. Peptide hormone
CC       binding leads to dissociation of the homodimer.
CC       {ECO:0000250|UniProtKB:Q03431}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8197183};
CC       Multi-pass membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Detected in kidney. {ECO:0000269|PubMed:8197183}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q03431}.
CC   -!- PTM: Phosphorylated on multiple serine residues; these phosphorylations
CC       are important for PTH-dependent internalization.
CC       {ECO:0000250|UniProtKB:Q03431}.
CC   -!- SIMILARITY: Belongs to the G protein-coupled receptor 2 family.
CC       {ECO:0000305}.
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DR   EMBL; X78936; CAA55536.1; -; mRNA.
DR   EMBL; L34611; AAA40011.1; -; Genomic_DNA.
DR   EMBL; L34608; AAA40011.1; JOINED; Genomic_DNA.
DR   EMBL; L34607; AAA40011.1; JOINED; Genomic_DNA.
DR   EMBL; L34609; AAA40011.1; JOINED; Genomic_DNA.
DR   EMBL; L34610; AAA40011.1; JOINED; Genomic_DNA.
DR   EMBL; BC051981; AAH51981.1; -; mRNA.
DR   CCDS; CCDS52940.1; -.
DR   PIR; I59297; I59297.
DR   PIR; S44203; S44203.
DR   RefSeq; NP_001077404.1; NM_001083935.1.
DR   RefSeq; NP_001077405.1; NM_001083936.1.
DR   RefSeq; NP_035329.2; NM_011199.2.
DR   AlphaFoldDB; P41593; -.
DR   SMR; P41593; -.
DR   BioGRID; 202466; 1.
DR   FunCoup; P41593; 444.
DR   IntAct; P41593; 1.
DR   STRING; 10090.ENSMUSP00000006005; -.
DR   ChEMBL; CHEMBL1075300; -.
DR   GlyCosmos; P41593; 4 sites, No reported glycans.
DR   GlyGen; P41593; 4 sites.
DR   iPTMnet; P41593; -.
DR   PhosphoSitePlus; P41593; -.
DR   PaxDb; 10090-ENSMUSP00000006005; -.
DR   ProteomicsDB; 302008; -.
DR   Antibodypedia; 1960; 492 antibodies from 43 providers.
DR   DNASU; 19228; -.
DR   Ensembl; ENSMPUT00000015208; ENSMPUP00000014971; ENSMPUG00000015082.
DR   Ensembl; ENSMUST00000006005.12; ENSMUSP00000006005.8; ENSMUSG00000032492.15.
DR   Ensembl; ENSMUST00000166716.8; ENSMUSP00000132064.2; ENSMUSG00000032492.15.
DR   Ensembl; ENSMUST00000198865.5; ENSMUSP00000143298.2; ENSMUSG00000032492.15.
DR   GeneID; 19228; -.
DR   KEGG; mmu:19228; -.
DR   UCSC; uc009ruo.1; mouse.
DR   AGR; MGI:97801; -.
DR   CTD; 5745; -.
DR   MGI; MGI:97801; Pth1r.
DR   VEuPathDB; HostDB:ENSMUSG00000032492; -.
DR   eggNOG; KOG4564; Eukaryota.
DR   GeneTree; ENSGT00940000158574; -.
DR   InParanoid; P41593; -.
DR   OMA; AANMIWS; -.
DR   OrthoDB; 6160250at2759; -.
DR   PhylomeDB; P41593; -.
DR   Reactome; R-MMU-373080; Class B/2 (Secretin family receptors).
DR   Reactome; R-MMU-418555; G alpha (s) signalling events.
DR   BioGRID-ORCS; 19228; 2 hits in 77 CRISPR screens.
DR   PRO; PR:P41593; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; P41593; protein.
DR   Bgee; ENSMUSG00000032492; Expressed in right kidney and 269 other cell types or tissues.
DR   ExpressionAtlas; P41593; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:GO_Central.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISO:GO_Central.
DR   GO; GO:0031526; C:brush border membrane; ISO:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:GO_Central.
DR   GO; GO:0005730; C:nucleolus; ISO:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; EXP:UniProtKB.
DR   GO; GO:0043235; C:signaling receptor complex; ISO:GO_Central.
DR   GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; ISO:GO_Central.
DR   GO; GO:0004991; F:parathyroid hormone receptor activity; IMP:MGI.
DR   GO; GO:0017046; F:peptide hormone binding; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:MGI.
DR   GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; ISO:GO_Central.
DR   GO; GO:0030282; P:bone mineralization; IMP:MGI.
DR   GO; GO:0045453; P:bone resorption; IMP:MGI.
DR   GO; GO:0048469; P:cell maturation; IMP:MGI.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0002062; P:chondrocyte differentiation; IMP:MGI.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:GO_Central.
DR   GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; ISO:GO_Central.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0006874; P:intracellular calcium ion homeostasis; IMP:MGI.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR   GO; GO:0001503; P:ossification; IMP:MGI.
DR   GO; GO:0002076; P:osteoblast development; IMP:MGI.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IMP:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IGI:MGI.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:GO_Central.
DR   GO; GO:0060732; P:positive regulation of inositol phosphate biosynthetic process; ISO:GO_Central.
DR   GO; GO:0070293; P:renal absorption; IDA:GO_Central.
DR   GO; GO:0044722; P:renal phosphate excretion; ISO:GO_Central.
DR   GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR   FunFam; 1.20.1070.10:FF:000070; Parathyroid hormone/parathyroid hormone-related peptide receptor; 1.
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; IPR050332; GPCR_2.
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.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; G protein-coupled receptor; Glycoprotein;
KW   Membrane; Phosphoprotein; Receptor; Reference proteome; Signal; Transducer;
KW   Transmembrane; 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_0000012846"
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   MOTIF           474..477
FT                   /note="Important for interaction with G proteins"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        81..96
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         491
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03431"
FT   MOD_RES         492
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03431"
FT   MOD_RES         493
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03431"
FT   MOD_RES         495
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03431"
FT   MOD_RES         501
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03431"
FT   MOD_RES         504
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03431"
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"
FT   CONFLICT        27..28
FT                   /note="DA -> TS (in Ref. 2; AAA40011)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        464..465
FT                   /note="Missing (in Ref. 2; AAA40011)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        500..501
FT                   /note="VS -> GA (in Ref. 1; CAA55536)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   591 AA;  66372 MW;  C2E6CCAF2ABAFEEF CRC64;
     MGTARIAPSL ALLLCCPVLS SAYALVDADD VFTKEEQIFL LHRAQAQCDK LLKEVLHTAA
     NIMESDKGWT PASTSGKPRK EKAPGKFYPE 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 RLLPATTNGH SQLPGHAKPG
     APAIENETIP VTMTVPKDDG FLNGSCSGLD EEASGSARPP PLLQEEWETV M
//