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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_DIDVI             Reviewed;         585 AA.
P25107;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 2.
31-JAN-2018, entry version 94.
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=PTHR, PTHR1;
Didelphis virginiana (North American opossum) (Didelphis marsupialis
virginiana).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Metatheria; Didelphimorphia; Didelphidae; Didelphis.
NCBI_TaxID=9267;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PTH AND PTHLH,
AND SUBCELLULAR LOCATION.
PubMed=1658941; DOI=10.1126/science.1658941;
Jueppner H., Abou-Samra A.-B., Freeman M., Kong X.-F., Schipani E.,
Richards J., Kolakowski L.F. Jr., Hock J., Potts J.T. Jr.,
Kronenberg H.M., Segre G.V.;
"A G protein-linked receptor for parathyroid hormone and parathyroid
hormone-related peptide.";
Science 254:1024-1026(1991).
-!- 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:1658941}.
-!- SUBUNIT: Interacts (via N-terminal extracellular domain) with
PTHLH and PTH (PubMed:1658941). 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:1658941}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1658941};
Multi-pass membrane protein {ECO:0000305}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q03431}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
{ECO:0000305}.
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EMBL; M74445; AAA30979.1; -; mRNA.
PIR; A39286; A39286.
ProteinModelPortal; P25107; -.
SMR; P25107; -.
IntAct; P25107; 1.
MINT; MINT-8146745; -.
iPTMnet; P25107; -.
HOVERGEN; HBG008318; -.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005622; C:intracellular; IEA:GOC.
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:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
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; Disulfide bond; G-protein coupled receptor;
Glycoprotein; Membrane; Receptor; Signal; Transducer; Transmembrane;
Transmembrane helix.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 585 Parathyroid hormone/parathyroid hormone-
related peptide receptor.
/FTId=PRO_0000012844.
TOPO_DOM 27 185 Extracellular. {ECO:0000255}.
TRANSMEM 186 209 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 210 216 Cytoplasmic. {ECO:0000255}.
TRANSMEM 217 236 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 237 276 Extracellular. {ECO:0000255}.
TRANSMEM 277 300 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 301 314 Cytoplasmic. {ECO:0000255}.
TRANSMEM 315 336 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 337 355 Extracellular. {ECO:0000255}.
TRANSMEM 356 376 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 377 403 Cytoplasmic. {ECO:0000255}.
TRANSMEM 404 422 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 423 434 Extracellular. {ECO:0000255}.
TRANSMEM 435 457 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 458 585 Cytoplasmic. {ECO:0000255}.
MOTIF 468 471 Important for interaction with G
proteins. {ECO:0000250}.
CARBOHYD 148 148 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 158 158 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 163 163 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 173 173 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 48 114 {ECO:0000250|UniProtKB:Q03431}.
DISULFID 105 145 {ECO:0000250|UniProtKB:Q03431}.
DISULFID 128 167 {ECO:0000250|UniProtKB:Q03431}.
SEQUENCE 585 AA; 65963 MW; 34900384CD6DF477 CRC64;
MGAPRISHSL ALLLCCSVLS SVYALVDADD VITKEEQIIL LRNAQAQCEQ RLKEVLRVPE
LAESAKDWMS RSAKTKKEKP AEKLYSQAEE SREVSDRSRL QDGFCLPEWD NIVCWPAGVP
GKVVAVPCPD YIYDFNHKGR AYRRCDSNGS WELVPGNNRT WANYSECVKF LTNETREREV
FDRLGMIYTV GYSISLGSLT VAVLILGYFR RLHCTRNYIH MHLFVSFMLR AVSIFIKDAV
LYSGVSTDEI ERITEEELRA FTEPPPADKA GFVGCRVAVT VFLYFLTTNY YWILVEGLYL
HSLIFMAFFS EKKYLWGFTL FGWGLPAVFV AVWVTVRATL ANTECWDLSS GNKKWIIQVP
ILAAIVVNFI LFINIIRVLA TKLRETNAGR CDTRQQYRKL LKSTLVLMPL FGVHYIVFMA
TPYTEVSGIL WQVQMHYEML FNSFQGFFVA IIYCFCNGEV QAEIKKSWSR WTLALDFKRK
ARSGSSTYSY GPMVSHTSVT NVGPRGGLAL SLSPRLAPGA GASANGHHQL PGYVKHGSIS
ENSLPSSGPE PGTKDDGYLN GSGLYEPMVG EQPPPLLEEE RETVM


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