PTH1R_CANLF
ID PTH1R_CANLF Reviewed; 595 AA.
AC Q9TU31;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
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=PTH1, PTHR1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PTH AND PTHLH,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=12153143; DOI=10.1023/a:1015716726452;
RA Smock S.L., Vogt G.A., Castleberry T.A., Lu B., Owen T.A.;
RT "Molecular cloning and functional characterization of the canine
RT parathyroid hormone/parathyroid hormone related peptide receptor (PTH1).";
RL Mol. Biol. Rep. 28:235-243(2001).
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:12153143}.
CC -!- SUBUNIT: Interacts (via N-terminal extracellular domain) with PTHLH and
CC PTH (PubMed:12153143). Homodimer in the absence of bound ligand.
CC Peptide hormone binding leads to dissociation of the homodimer (By
CC similarity). {ECO:0000250|UniProtKB:Q03431,
CC ECO:0000269|PubMed:12153143}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12153143};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: High levels in the kidney, with much lower levels
CC in aorta, heart, lung, prostate, testis, and skeletal muscle.
CC {ECO:0000269|PubMed:12153143}.
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; AF167095; AAD55938.1; -; mRNA.
DR RefSeq; NP_001003155.1; NM_001003155.1.
DR AlphaFoldDB; Q9TU31; -.
DR SMR; Q9TU31; -.
DR STRING; 9612.ENSCAFP00000020013; -.
DR PaxDb; Q9TU31; -.
DR Ensembl; ENSCAFT00030045882; ENSCAFP00030040086; ENSCAFG00030024884.
DR Ensembl; ENSCAFT00845019581; ENSCAFP00845015315; ENSCAFG00845010997.
DR GeneID; 403779; -.
DR KEGG; cfa:403779; -.
DR CTD; 5745; -.
DR VEuPathDB; HostDB:ENSCAFG00845010997; -.
DR eggNOG; KOG4564; Eukaryota.
DR GeneTree; ENSGT00940000158574; -.
DR HOGENOM; CLU_002753_4_3_1; -.
DR InParanoid; Q9TU31; -.
DR OMA; ESDKGWM; -.
DR OrthoDB; 651627at2759; -.
DR TreeFam; TF315710; -.
DR Reactome; R-CFA-373080; Class B/2 (Secretin family receptors).
DR Reactome; R-CFA-418555; G alpha (s) signalling events.
DR Proteomes; UP000002254; Chromosome 20.
DR Bgee; ENSCAFG00000013600; Expressed in renal medulla and 46 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0004991; F:parathyroid hormone receptor activity; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR GO; GO:0045453; P:bone resorption; IEA:Ensembl.
DR GO; GO:0048469; P:cell maturation; IEA:Ensembl.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0002076; P:osteoblast development; IEA:Ensembl.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
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; Phosphoprotein; Receptor; Reference proteome; Signal; Transducer;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..595
FT /note="Parathyroid hormone/parathyroid hormone-related
FT peptide receptor"
FT /id="PRO_0000250991"
FT TOPO_DOM 29..188
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..223
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..294
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 295..315
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..360
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..404
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 426..439
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..460
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 461..595
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 66..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 473..476
FT /note="Important for interaction with G proteins"
FT /evidence="ECO:0000250"
FT COMPBIAS 79..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..555
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 553
FT /note="Phosphothreonine"
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"
SQ 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
