PTH1R_PONAB
ID PTH1R_PONAB Reviewed; 594 AA.
AC Q5RAQ1;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 78.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR858963; CAH91159.1; -; mRNA.
DR AlphaFoldDB; Q5RAQ1; -.
DR SMR; Q5RAQ1; -.
DR STRING; 9601.ENSPPYP00000015578; -.
DR eggNOG; KOG4564; Eukaryota.
DR InParanoid; Q5RAQ1; -.
DR Proteomes; UP000001595; Unplaced.
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; 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..594
FT /note="Parathyroid hormone/parathyroid hormone-related
FT peptide receptor"
FT /id="PRO_0000250992"
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..295
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..319
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..361
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..405
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..440
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 462..594
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 66..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 475..478
FT /note="Important for interaction with G proteins"
FT /evidence="ECO:0000250"
FT COMPBIAS 79..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 552
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q03431"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..117
FT /evidence="ECO:0000250|UniProtKB:Q03431"
FT DISULFID 108..149
FT /evidence="ECO:0000250|UniProtKB:Q03431"
FT DISULFID 132..171
FT /evidence="ECO:0000250|UniProtKB:Q03431"
SQ SEQUENCE 594 AA; 66500 MW; B2E558A22296A5E5 CRC64;
MGTARIAPGL ALLLCCPVLS SAYALVDADD VMTKEEQIFL LHRAQAQCGK RLKEVLQRPA
DIMESDKGWT SASTSGKPRK DKASGKLYPE SEEDKEAPTD SRYRGRPCLP EWDHILCWPL
GAPQGEVVAV PCPDYIYDFN HKGHAYRRCD RNGSWELVPG HNRTWANYSE CVQFLTNETR
EREVFDRLGM IYTVGYSMSL ASLTVAVLIL AYFRRLHCTR NYIHMHLFLS FMLRAVSIFV
KDAVLYSGAT LDEAERLTEE ELRAIAQAPP PPATAAAGYA GCRVAVTFFL YFLATNYYWI
LVEGLYLHSL IFMAFFSEKK YLWGFTVFGW GLPAVFVAVW VSVRATLANT GCWDLSSGNK
KWIIQVPILA SIVLHFILFI NIVRVLATKL RETNAGRCDT RQQYRKLLKS TLVLMPLFGV
HYIVFMATPY TEVSGTLWQV QMHYEMLFNS FQGFFVAIIY CFCNGEVQAE IKKSWSRWTL
ALDFKRKARS GSSSYSYGPM VSHTSVTNVG PRVGLGLPLS PRLLPTATTN GHPQLPGHAK
PGTPALETLE TTPPATAAPK DDGFLNGSCS GLDEEASGPE QPPALLQEEW ETVM
