PTH1R_PIG
ID PTH1R_PIG Reviewed; 585 AA.
AC P50133;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 134.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PTH AND PTHLH, AND
RP SUBCELLULAR LOCATION.
RX PubMed=8688470; DOI=10.1016/0167-4781(96)00035-8;
RA Black E.C., Smith D.P., Zhang X.Y., Frolik C.A., Harvey A.,
RA Chandrasekhar S., Hsiung H.M.;
RT "Structure and functional expression of a complementary DNA for porcine
RT parathyroid hormone/parathyroid hormone-related peptide receptor.";
RL Biochim. Biophys. Acta 1307:339-347(1996).
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:8688470}.
CC -!- SUBUNIT: Interacts (via N-terminal extracellular domain) with PTHLH and
CC PTH (PubMed:8688470). 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:8688470}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8688470};
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; U18315; AAC48619.1; -; mRNA.
DR RefSeq; NP_999547.1; NM_214382.1.
DR AlphaFoldDB; P50133; -.
DR SMR; P50133; -.
DR STRING; 9823.ENSSSCP00000012077; -.
DR PaxDb; P50133; -.
DR PRIDE; P50133; -.
DR Ensembl; ENSSSCT00030045174; ENSSSCP00030020299; ENSSSCG00030032571.
DR Ensembl; ENSSSCT00040043419; ENSSSCP00040018217; ENSSSCG00040031272.
DR Ensembl; ENSSSCT00040043508; ENSSSCP00040018263; ENSSSCG00040031272.
DR Ensembl; ENSSSCT00045027312; ENSSSCP00045018871; ENSSSCG00045016016.
DR Ensembl; ENSSSCT00045027411; ENSSSCP00045018936; ENSSSCG00045016016.
DR Ensembl; ENSSSCT00050075646; ENSSSCP00050032611; ENSSSCG00050055449.
DR Ensembl; ENSSSCT00060013714; ENSSSCP00060005256; ENSSSCG00060010537.
DR GeneID; 397675; -.
DR KEGG; ssc:397675; -.
DR CTD; 5745; -.
DR eggNOG; KOG4564; Eukaryota.
DR HOGENOM; CLU_002753_4_3_1; -.
DR InParanoid; P50133; -.
DR OrthoDB; 651627at2759; -.
DR TreeFam; TF315710; -.
DR Reactome; R-SSC-373080; Class B/2 (Secretin family receptors).
DR Reactome; R-SSC-418555; G alpha (s) signalling events.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P50133; SS.
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 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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..585
FT /note="Parathyroid hormone/parathyroid hormone-related
FT peptide receptor"
FT /id="PRO_0000012847"
FT TOPO_DOM 27..184
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..208
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..235
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..277
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..301
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..315
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..337
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..356
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 378..404
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..423
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..435
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..458
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..585
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 66..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 469..472
FT /note="Important for interaction with G proteins"
FT /evidence="ECO:0000250"
FT COMPBIAS 79..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 543
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q03431"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
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 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 48..113
FT /evidence="ECO:0000250|UniProtKB:Q03431"
FT DISULFID 104..144
FT /evidence="ECO:0000250|UniProtKB:Q03431"
FT DISULFID 127..166
FT /evidence="ECO:0000250|UniProtKB:Q03431"
SQ SEQUENCE 585 AA; 65682 MW; 60BE15CD49B7D210 CRC64;
MGAARIAPGL ALLLCCPVLS SAYALVDADD VMTKEEQIFL LHRAQAQCEK RLKEVLQRPA
DIMESDKGWA SAPTSGKPRK EKASGKLYPE SGEDTGSRHQ GRPCLPEWDH ILCWPLGAPG
EVVAMPCPDY IYDFNHKGHA YRRCDRNGSW ELVPGHNRTW ANYSECVKFL TNETREREVF
DRLGMIYTVG YSVSLASLTV AVLILAYFRR LHCTRNYIHM HLFLSFMLRA VSIFVKDAVL
YSGATLDEAE RLTEEELRAI AQAPLPPVAA TSYVGCRVAV TFFLYFLATN YYWILVEGLY
LHSLIFMAFF SEKKYLWGFT VFGWGLPAIF VAVWVSVRAT LANTGCWDLS SGNKKWIIQV
PILASIVLNF ILFINIVRVL ATKLRETNAG RCDTRQQYRK LLKSTLVLMP LFGVHYIVFM
ATPYTEVSGT LWQVQMHYEM LFNSFQGFFV AIIYCFCNGE VQAEIKKSWS RWTLALDFKR
KARSGSSSYS YGPMVSHTSV TNVGPRTGLG LPLSPRLLPA ATTNGHPQLP CHTKPETPAL
QTTPPVVAAP KDDGFLNGSC SGLDEEASAP ERPSVLLQEE WETVM
