PTH2R_HUMAN
ID PTH2R_HUMAN Reviewed; 550 AA.
AC P49190; Q8N429;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Parathyroid hormone 2 receptor;
DE Short=PTH2 receptor;
DE Flags: Precursor;
GN Name=PTH2R; Synonyms=PTHR2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=7797535; DOI=10.1074/jbc.270.26.15455;
RA Usdin T.B., Gruber C., Bonner T.I.;
RT "Identification and functional expression of a receptor selectively
RT recognizing parathyroid hormone, the PTH2 receptor.";
RL J. Biol. Chem. 270:15455-15458(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina;
RA King M.M., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-40 AND 306-550.
RX PubMed=8921382; DOI=10.1006/geno.1996.0532;
RA Usdin T.B., Modi W., Bonner T.I.;
RT "Assignment of the human PTH2 receptor gene (PTHR2) to chromosome 2q33 by
RT fluorescence in situ hybridization.";
RL Genomics 37:140-141(1996).
RN [5]
RP INTERACTION WITH TIPF39/TI39.
RX PubMed=11861531; DOI=10.1210/endo.143.3.8698;
RA John M.R., Arai M., Rubin D.A., Jonsson K.B., Jueppner H.;
RT "Identification and characterization of the murine and human gene encoding
RT the tuberoinfundibular peptide of 39 residues.";
RL Endocrinology 143:1047-1057(2002).
CC -!- FUNCTION: This is a specific receptor for parathyroid hormone. The
CC activity of this receptor is mediated by G proteins which activate
CC adenylyl cyclase. PTH2R may be responsible for PTH effects in a number
CC of physiological systems. It may play a significant role in pancreatic
CC function. PTH2R presence in neurons indicates that it may function as a
CC neurotransmitter receptor (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds to TIPF39/TIP39.
CC -!- INTERACTION:
CC P49190; P63172: DYNLT1; NbExp=3; IntAct=EBI-1045772, EBI-1176455;
CC P49190; Q9NP66: HMG20A; NbExp=3; IntAct=EBI-1045772, EBI-740641;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed abundantly in brain and pancreas. Also
CC expressed in the testis. {ECO:0000269|PubMed:7797535}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
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DR EMBL; U25128; AAC50157.1; -; mRNA.
DR EMBL; AY497546; AAR90849.1; -; mRNA.
DR EMBL; BC036811; AAH36811.2; -; mRNA.
DR EMBL; U47124; AAA96796.1; -; Genomic_DNA.
DR EMBL; AH006647; AAC50767.1; -; Genomic_DNA.
DR CCDS; CCDS2383.1; -.
DR PIR; A57519; A57519.
DR RefSeq; NP_001296445.1; NM_001309516.1.
DR RefSeq; NP_005039.1; NM_005048.3.
DR PDB; 7F16; EM; 2.80 A; R=24-442.
DR PDBsum; 7F16; -.
DR AlphaFoldDB; P49190; -.
DR SMR; P49190; -.
DR BioGRID; 111718; 153.
DR IntAct; P49190; 3.
DR MINT; P49190; -.
DR STRING; 9606.ENSP00000272847; -.
DR ChEMBL; CHEMBL4105836; -.
DR DrugBank; DB05829; Parathyroid hormone.
DR DrugCentral; P49190; -.
DR GuidetoPHARMACOLOGY; 332; -.
DR GlyGen; P49190; 4 sites.
DR iPTMnet; P49190; -.
DR PhosphoSitePlus; P49190; -.
DR BioMuta; PTH2R; -.
DR DMDM; 1346906; -.
DR MassIVE; P49190; -.
DR PaxDb; P49190; -.
DR PeptideAtlas; P49190; -.
DR PRIDE; P49190; -.
DR TopDownProteomics; P49190; -.
DR Antibodypedia; 20012; 230 antibodies from 28 providers.
DR DNASU; 5746; -.
DR Ensembl; ENST00000272847.7; ENSP00000272847.2; ENSG00000144407.10.
DR GeneID; 5746; -.
DR KEGG; hsa:5746; -.
DR MANE-Select; ENST00000272847.7; ENSP00000272847.2; NM_005048.4; NP_005039.1.
DR UCSC; uc002vdb.5; human.
DR CTD; 5746; -.
DR DisGeNET; 5746; -.
DR GeneCards; PTH2R; -.
DR HGNC; HGNC:9609; PTH2R.
DR HPA; ENSG00000144407; Tissue enhanced (retina).
DR MIM; 601469; gene.
DR neXtProt; NX_P49190; -.
DR OpenTargets; ENSG00000144407; -.
DR PharmGKB; PA162400333; -.
DR VEuPathDB; HostDB:ENSG00000144407; -.
DR eggNOG; KOG4564; Eukaryota.
DR GeneTree; ENSGT00940000159094; -.
DR InParanoid; P49190; -.
DR OMA; SLHVWGW; -.
DR OrthoDB; 651627at2759; -.
DR PhylomeDB; P49190; -.
DR TreeFam; TF315710; -.
DR PathwayCommons; P49190; -.
DR Reactome; R-HSA-373080; Class B/2 (Secretin family receptors).
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR SignaLink; P49190; -.
DR SIGNOR; P49190; -.
DR BioGRID-ORCS; 5746; 11 hits in 1068 CRISPR screens.
DR ChiTaRS; PTH2R; human.
DR GeneWiki; Parathyroid_hormone_2_receptor; -.
DR GenomeRNAi; 5746; -.
DR Pharos; P49190; Tchem.
DR PRO; PR:P49190; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P49190; protein.
DR Bgee; ENSG00000144407; Expressed in metanephros cortex and 106 other tissues.
DR ExpressionAtlas; P49190; baseline and differential.
DR Genevisible; P49190; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
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; IBA:GO_Central.
DR GO; GO:0017046; F:peptide hormone binding; IBA:GO_Central.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
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; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF02793; HRM; 1.
DR PRINTS; PR00249; GPCRSECRETIN.
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 3D-structure; Cell membrane; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..550
FT /note="Parathyroid hormone 2 receptor"
FT /id="PRO_0000012849"
FT TOPO_DOM 27..145
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..169
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..196
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..237
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..260
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..297
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..316
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..383
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..394
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..417
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..550
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 511..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT HELIX 34..56
FT /evidence="ECO:0007829|PDB:7F16"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:7F16"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:7F16"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:7F16"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:7F16"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:7F16"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:7F16"
FT HELIX 129..168
FT /evidence="ECO:0007829|PDB:7F16"
FT HELIX 175..204
FT /evidence="ECO:0007829|PDB:7F16"
FT HELIX 234..266
FT /evidence="ECO:0007829|PDB:7F16"
FT TURN 272..275
FT /evidence="ECO:0007829|PDB:7F16"
FT HELIX 276..301
FT /evidence="ECO:0007829|PDB:7F16"
FT TURN 312..315
FT /evidence="ECO:0007829|PDB:7F16"
FT HELIX 316..346
FT /evidence="ECO:0007829|PDB:7F16"
FT HELIX 354..372
FT /evidence="ECO:0007829|PDB:7F16"
FT HELIX 374..380
FT /evidence="ECO:0007829|PDB:7F16"
FT HELIX 389..413
FT /evidence="ECO:0007829|PDB:7F16"
FT HELIX 418..433
FT /evidence="ECO:0007829|PDB:7F16"
SQ SEQUENCE 550 AA; 62236 MW; 2ADD14DBA68A9BF8 CRC64;
MAGLGASLHV WGWLMLGSCL LARAQLDSDG TITIEEQIVL VLKAKVQCEL NITAQLQEGE
GNCFPEWDGL ICWPRGTVGK ISAVPCPPYI YDFNHKGVAF RHCNPNGTWD FMHSLNKTWA
NYSDCLRFLQ PDISIGKQEF FERLYVMYTV GYSISFGSLA VAILIIGYFR RLHCTRNYIH
MHLFVSFMLR ATSIFVKDRV VHAHIGVKEL ESLIMQDDPQ NSIEATSVDK SQYIGCKIAV
VMFIYFLATN YYWILVEGLY LHNLIFVAFF SDTKYLWGFI LIGWGFPAAF VAAWAVARAT
LADARCWELS AGDIKWIYQA PILAAIGLNF ILFLNTVRVL ATKIWETNAV GHDTRKQYRK
LAKSTLVLVL VFGVHYIVFV CLPHSFTGLG WEIRMHCELF FNSFQGFFVS IIYCYCNGEV
QAEVKKMWSR WNLSVDWKRT PPCGSRRCGS VLTTVTHSTS SQSQVAASTR MVLISGKAAK
IASRQPDSHI TLPGYVWSNS EQDCLPHSFH EETKEDSGRQ GDDILMEKPS RPMESNPDTE
GCQGETEDVL
