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PTH1R_MOUSE
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   03-AUG-2022, entry version 178.
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], 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: Receptor for parathyroid hormone and for parathyroid hormone-
CC       related peptide (PubMed:8197183). The activity of this receptor is
CC       mediated by G proteins which activate adenylyl cyclase and also a
CC       phosphatidylinositol-calcium second messenger system.
CC       {ECO:0000250|UniProtKB:Q03431, ECO:0000269|PubMed:8197183}.
CC   -!- SUBUNIT: Interacts (via N-terminal extracellular domain) with PTHLH and
CC       PTH (PubMed:8197183). Homodimer in the absence of bound ligand. Peptide
CC       hormone binding leads to dissociation of the homodimer.
CC       {ECO:0000250|UniProtKB:Q03431, ECO:0000305|PubMed:8197183}.
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   -!- 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   IntAct; P41593; 1.
DR   STRING; 10090.ENSMUSP00000006005; -.
DR   ChEMBL; CHEMBL1075300; -.
DR   GlyGen; P41593; 4 sites.
DR   iPTMnet; P41593; -.
DR   PhosphoSitePlus; P41593; -.
DR   MaxQB; P41593; -.
DR   PaxDb; P41593; -.
DR   PRIDE; P41593; -.
DR   ProteomicsDB; 302008; -.
DR   Antibodypedia; 1960; 424 antibodies from 39 providers.
DR   DNASU; 19228; -.
DR   Ensembl; ENSMUST00000006005; ENSMUSP00000006005; ENSMUSG00000032492.
DR   Ensembl; ENSMUST00000166716; ENSMUSP00000132064; ENSMUSG00000032492.
DR   Ensembl; ENSMUST00000198865; ENSMUSP00000143298; ENSMUSG00000032492.
DR   GeneID; 19228; -.
DR   KEGG; mmu:19228; -.
DR   UCSC; uc009ruo.1; mouse.
DR   CTD; 5745; -.
DR   MGI; MGI:97801; Pth1r.
DR   VEuPathDB; HostDB:ENSMUSG00000032492; -.
DR   eggNOG; KOG4564; Eukaryota.
DR   GeneTree; ENSGT00940000158574; -.
DR   InParanoid; P41593; -.
DR   OMA; ESDKGWM; -.
DR   OrthoDB; 651627at2759; -.
DR   PhylomeDB; P41593; -.
DR   TreeFam; TF315710; -.
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 72 CRISPR screens.
DR   ChiTaRS; Pth1r; mouse.
DR   PRO; PR:P41593; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; P41593; protein.
DR   Bgee; ENSMUSG00000032492; Expressed in right kidney and 266 other tissues.
DR   ExpressionAtlas; P41593; baseline and differential.
DR   Genevisible; P41593; MM.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR   GO; GO:0031526; C:brush border membrane; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0043235; C:receptor complex; ISO:MGI.
DR   GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA: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:0043621; F:protein self-association; ISO:MGI.
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:MGI.
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:0008283; P:cell population proliferation; IMP:MGI.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:MGI.
DR   GO; GO:0002062; P:chondrocyte differentiation; IMP:MGI.
DR   GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; ISO:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; 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:MGI.
DR   GO; GO:0060732; P:positive regulation of inositol phosphate biosynthetic process; ISO:MGI.
DR   GO; GO:0001501; P:skeletal system development; IMP:MGI.
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_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        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"
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
 
 
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