PTH1R_BOVIN
ID PTH1R_BOVIN Reviewed; 589 AA.
AC Q1LZF7;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=PTHR1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q03431}.
CC -!- SUBUNIT: Interacts (via N-terminal extracellular domain) with PTHLH and
CC PTH. Homodimer in the absence of bound ligand. Peptide hormone binding
CC leads to dissociation of the homodimer. {ECO:0000250|UniProtKB:Q03431}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q03431};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q03431}.
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; BC116022; AAI16023.1; -; mRNA.
DR RefSeq; NP_001068800.1; NM_001075332.1.
DR AlphaFoldDB; Q1LZF7; -.
DR SMR; Q1LZF7; -.
DR STRING; 9913.ENSBTAP00000022555; -.
DR PaxDb; Q1LZF7; -.
DR PRIDE; Q1LZF7; -.
DR GeneID; 507783; -.
DR KEGG; bta:507783; -.
DR CTD; 5745; -.
DR eggNOG; KOG4564; Eukaryota.
DR InParanoid; Q1LZF7; -.
DR OrthoDB; 651627at2759; -.
DR Proteomes; UP000009136; Unplaced.
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:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
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 2: Evidence at transcript 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..589
FT /note="Parathyroid hormone/parathyroid hormone-related
FT peptide receptor"
FT /id="PRO_0000250990"
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..589
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 64..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..549
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..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 547
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 589 AA; 65862 MW; 65C4E7970ED2CB71 CRC64;
MGAARIAPGL ALLLCCPVLS SAYALVDADD VMTKEEQIFL LHRAQAQCEK RLKEVLQRPA
DIMESDKGWA SASTSGKPKK EKPSGKLHPE SEEDKEVPTG SRPRGRPCLP EWDHILCWPL
GAPGEVVAMP CPDYIYDFNH KGHAYRRCDR NGSWELVPGH NRTWANYSEC VKFLTNETRE
REVFDRLGMI YTVGYSVSLA SLTVAVLILA YFRRLHCTRN YIHMHLFLSF MLRAVSIFVK
DAVLYSGTAL DEAERLTEEE LRAIAQAPPP PAAAAGYVGC RVAVTFFLYF LATNYYWILV
EGLYLHSLIF MAFFSEKKYL WGFTVFGWGL PAIFVAVWVS VRATLANTGC WDLSSGNKKW
IIQVPILASI VLNFILFINI VRVLATKLRE TNAGRCDTRQ QYRKLLKSTL VLMPLFGVHY
IVFMATPYTE VSGTLWQVQM HYEMLFNSFQ GFFVAIIYCF CNGEVQAEIK KSWSRWTLAL
DFKRKARSGS SSYSYGPMVS HTSVTNVGPR TGLGLPLSPR LLPAATTNGH PPLPGHTKSG
SPALQATPPA VAAPKEDGFL NGSCSGLDEE ACAPERPPVL LQEEWETVM
