PTH1R_DIDVI
ID PTH1R_DIDVI Reviewed; 585 AA.
AC P25107;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 107.
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 Didelphis virginiana (North American opossum) (Didelphis marsupialis
OS virginiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Didelphimorphia; Didelphidae; Didelphis.
OX NCBI_TaxID=9267;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PTH AND PTHLH, AND
RP SUBCELLULAR LOCATION.
RX PubMed=1658941; DOI=10.1126/science.1658941;
RA Jueppner H., Abou-Samra A.-B., Freeman M., Kong X.-F., Schipani E.,
RA Richards J., Kolakowski L.F. Jr., Hock J., Potts J.T. Jr., Kronenberg H.M.,
RA Segre G.V.;
RT "A G protein-linked receptor for parathyroid hormone and parathyroid
RT hormone-related peptide.";
RL Science 254:1024-1026(1991).
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:1658941}.
CC -!- SUBUNIT: Interacts (via N-terminal extracellular domain) with PTHLH and
CC PTH (PubMed:1658941). Homodimer in the absence of bound ligand. Peptide
CC hormone binding leads to dissociation of the homodimer (By similarity).
CC {ECO:0000250|UniProtKB:Q03431, ECO:0000269|PubMed:1658941}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1658941};
CC Multi-pass membrane protein {ECO:0000305}.
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; M74445; AAA30979.1; -; mRNA.
DR PIR; A39286; A39286.
DR AlphaFoldDB; P25107; -.
DR SMR; P25107; -.
DR IntAct; P25107; 1.
DR MINT; P25107; -.
DR iPTMnet; P25107; -.
DR PRIDE; P25107; -.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
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 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; Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..585
FT /note="Parathyroid hormone/parathyroid hormone-related
FT peptide receptor"
FT /id="PRO_0000012844"
FT TOPO_DOM 27..185
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..209
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..236
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..276
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..300
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..314
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..336
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..355
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..403
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..422
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..434
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..457
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 458..585
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 69..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 468..471
FT /note="Important for interaction with G proteins"
FT /evidence="ECO:0000250"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..114
FT /evidence="ECO:0000250|UniProtKB:Q03431"
FT DISULFID 105..145
FT /evidence="ECO:0000250|UniProtKB:Q03431"
FT DISULFID 128..167
FT /evidence="ECO:0000250|UniProtKB:Q03431"
SQ 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
