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Parathyroid hormone/parathyroid hormone-related peptide receptor (PTH/PTHrP type I receptor) (PTH/PTHr receptor) (Parathyroid hormone 1 receptor) (PTH1 receptor)

 PTH1R_CANLF             Reviewed;         595 AA.
Q9TU31;
03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
31-JAN-2018, entry version 106.
RecName: Full=Parathyroid hormone/parathyroid hormone-related peptide receptor;
AltName: Full=PTH/PTHrP type I receptor;
Short=PTH/PTHr receptor;
AltName: Full=Parathyroid hormone 1 receptor;
Short=PTH1 receptor;
Flags: Precursor;
Name=PTH1R; Synonyms=PTH1, PTHR1;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PTH AND PTHLH,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Kidney;
PubMed=12153143; DOI=10.1023/A:1015716726452;
Smock S.L., Vogt G.A., Castleberry T.A., Lu B., Owen T.A.;
"Molecular cloning and functional characterization of the canine
parathyroid hormone/parathyroid hormone related peptide receptor
(PTH1).";
Mol. Biol. Rep. 28:235-243(2001).
-!- FUNCTION: Receptor for parathyroid hormone and for parathyroid
hormone-related peptide. The activity of this receptor is mediated
by G proteins which activate adenylyl cyclase and also a
phosphatidylinositol-calcium second messenger system.
{ECO:0000269|PubMed:12153143}.
-!- SUBUNIT: Interacts (via N-terminal extracellular domain) with
PTHLH and PTH (PubMed:12153143). Homodimer in the absence of bound
ligand. Peptide hormone binding leads to dissociation of the
homodimer (By similarity). {ECO:0000250|UniProtKB:Q03431,
ECO:0000269|PubMed:12153143}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12153143};
Multi-pass membrane protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: High levels in the kidney, with much lower
levels in aorta, heart, lung, prostate, testis, and skeletal
muscle. {ECO:0000269|PubMed:12153143}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q03431}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
{ECO:0000305}.
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EMBL; AF167095; AAD55938.1; -; mRNA.
RefSeq; NP_001003155.1; NM_001003155.1.
UniGene; Cfa.3643; -.
ProteinModelPortal; Q9TU31; -.
SMR; Q9TU31; -.
STRING; 9615.ENSCAFP00000020013; -.
PaxDb; Q9TU31; -.
Ensembl; ENSCAFT00000021553; ENSCAFP00000020013; ENSCAFG00000013600.
GeneID; 403779; -.
KEGG; cfa:403779; -.
CTD; 5745; -.
eggNOG; KOG4564; Eukaryota.
eggNOG; ENOG410XRS2; LUCA.
GeneTree; ENSGT00760000118800; -.
HOGENOM; HOG000008248; -.
HOVERGEN; HBG008318; -.
InParanoid; Q9TU31; -.
KO; K04585; -.
OMA; YAGCRVA; -.
OrthoDB; EOG091G0NF8; -.
TreeFam; TF315710; -.
Reactome; R-CFA-373080; Class B/2 (Secretin family receptors).
Reactome; R-CFA-418555; G alpha (s) signalling events.
Proteomes; UP000002254; Chromosome 20.
Bgee; ENSCAFG00000013600; -.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005622; C:intracellular; IEA:Ensembl.
GO; GO:0004991; F:parathyroid hormone receptor activity; ISS:UniProtKB.
GO; GO:0017046; F:peptide hormone binding; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
GO; GO:0045453; P:bone resorption; IEA:Ensembl.
GO; GO:0048469; P:cell maturation; IEA:Ensembl.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:Ensembl.
GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0002076; P:osteoblast development; IEA:Ensembl.
GO; GO:0007200; P:phospholipase C-activating G-protein coupled receptor signaling pathway; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
Gene3D; 4.10.1240.10; -; 1.
InterPro; IPR017981; GPCR_2-like.
InterPro; IPR036445; GPCR_2_extracell_dom_sf.
InterPro; IPR001879; GPCR_2_extracellular_dom.
InterPro; IPR002170; GPCR_2_parathyroid_rcpt.
InterPro; IPR000832; GPCR_2_secretin-like.
InterPro; IPR017983; GPCR_2_secretin-like_CS.
PANTHER; PTHR12011:SF24; PTHR12011:SF24; 1.
Pfam; PF00002; 7tm_2; 1.
Pfam; PF02793; HRM; 1.
PRINTS; PR00249; GPCRSECRETIN.
PRINTS; PR00393; PTRHORMONER.
SMART; SM00008; HormR; 1.
SUPFAM; SSF111418; SSF111418; 1.
PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; 1.
PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disulfide bond;
G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
Receptor; Reference proteome; Signal; Transducer; Transmembrane;
Transmembrane helix.
SIGNAL 1 28 {ECO:0000255}.
CHAIN 29 595 Parathyroid hormone/parathyroid hormone-
related peptide receptor.
/FTId=PRO_0000250991.
TOPO_DOM 29 188 Extracellular. {ECO:0000255}.
TRANSMEM 189 209 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 210 223 Cytoplasmic. {ECO:0000255}.
TRANSMEM 224 244 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 245 294 Extracellular. {ECO:0000255}.
TRANSMEM 295 315 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 316 318 Cytoplasmic. {ECO:0000255}.
TRANSMEM 319 339 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 340 360 Extracellular. {ECO:0000255}.
TRANSMEM 361 381 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 382 404 Cytoplasmic. {ECO:0000255}.
TRANSMEM 405 425 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 426 439 Extracellular. {ECO:0000255}.
TRANSMEM 440 460 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 461 595 Cytoplasmic. {ECO:0000255}.
MOTIF 473 476 Important for interaction with G
proteins. {ECO:0000250}.
COMPBIAS 268 271 Poly-Pro.
COMPBIAS 524 527 Poly-Ala.
MOD_RES 553 553 Phosphothreonine.
{ECO:0000250|UniProtKB:Q03431}.
CARBOHYD 151 151 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 161 161 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 166 166 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 176 176 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 48 117 {ECO:0000250|UniProtKB:Q03431}.
DISULFID 108 148 {ECO:0000250|UniProtKB:Q03431}.
DISULFID 131 170 {ECO:0000250|UniProtKB:Q03431}.
SEQUENCE 595 AA; 66309 MW; 09568ECF38D4D258 CRC64;
MGAVRIAPGL ALLLCCPVLS SAYALVDADD VMTKEEQIFL LHRAQAQCQK RLKEVLQRPA
DIMESDKGWA SASTSGKPKK EKASGKLYPE SEEDKEVPTG SRHRGRPCLP EWDHILCWPL
GAPGEVVAVP CPDYIYDFNH KGHAYRRCDR NGSWELVPGH NRTWANYSEC VKFLTNETRE
REVFDRLGMI YTVGYSVSLA SLTVAVLILA YFRRLHCTRN YIHMHLFLSF MLRAVSIFVK
DAVLYSGATL DEAERLTEEE LRAIAQAPPP PTAAAGYAGC RVAVTFFLYF LATNYYWILV
EGLYLHSLIF MAFFSEKKYL WGFTVFGWGL PAVFVAVWVS VRATLANTGC WDLSSGNKKW
IIQVPILASI VLNFILFINI VRVLATKLRE TNAGRCDTRQ QYRKLLKSTL VLMPLFGVHY
IVFMATPYTE VSGTLWQVQM HYEMLFNSFQ GFFVAIIYCF CNGEVQAEIK KSWSRWTLAL
DFKRKARSGS SSYSYGPMVS HTSVTNVGPR AGLGLPLSPR LLPAAAATTT ATTNGHPPIP
GHTKPGAPTL PATPPATAAP KDDGFLNGSC SGLDEEASAP ERPPALLQEE WETVM


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