PTH2R_RAT
ID PTH2R_RAT Reviewed; 546 AA.
AC P70555;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Parathyroid hormone 2 receptor;
DE Short=PTH2 receptor;
DE Flags: Precursor;
GN Name=Pth2r; Synonyms=Pthr2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8828488; DOI=10.1210/endo.137.10.8828488;
RA Usdin T.B., Bonner T.I., Harta G., Mezey E.;
RT "Distribution of parathyroid hormone-2 receptor messenger ribonucleic acid
RT in rat.";
RL Endocrinology 137:4285-4297(1996).
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.
CC -!- SUBUNIT: Binds to TIPF39/TIP39. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in brain, arterial and cardiac
CC endothelium. Found as well in sperm, in the head of the epididymis.
CC Lower expression is found in vascular smooth muscle, exocrine pancreas,
CC testis and placenta.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
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DR EMBL; U55836; AAC52849.1; -; mRNA.
DR RefSeq; NP_112351.1; NM_031089.2.
DR BioGRID; 249625; 1.
DR STRING; 10116.ENSRNOP00000021099; -.
DR DrugCentral; P70555; -.
DR GuidetoPHARMACOLOGY; 332; -.
DR GlyGen; P70555; 4 sites.
DR PhosphoSitePlus; P70555; -.
DR PaxDb; P70555; -.
DR PRIDE; P70555; -.
DR GeneID; 81753; -.
DR KEGG; rno:81753; -.
DR UCSC; RGD:620612; rat.
DR CTD; 5746; -.
DR RGD; 620612; Pth2r.
DR eggNOG; KOG4564; Eukaryota.
DR InParanoid; P70555; -.
DR OrthoDB; 651627at2759; -.
DR PhylomeDB; P70555; -.
DR Reactome; R-RNO-373080; Class B/2 (Secretin family receptors).
DR PRO; PR:P70555; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IDA:RGD.
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: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 2: Evidence at transcript level;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..546
FT /note="Parathyroid hormone 2 receptor"
FT /id="PRO_0000012851"
FT TOPO_DOM 27..143
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..167
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..194
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..235
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..258
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..295
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..313
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..361
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..380
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 381..391
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..414
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 415..546
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 498..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..523
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"
SQ SEQUENCE 546 AA; 61804 MW; 2825AE4040313527 CRC64;
MPWLEALPYI CGWLILRSCL LVGAQLDSDG TITIEEQIVL VMKAKMQCEL NITAQFQEGE
GNCFPEWDGL ICWPRGTAGK TSAMPCPSYV YDFNHKGVAF RHCTPNGTWD FIHGSNKTWA
NYSDCFLQPD INIGKQEFFE NLYILYTVGY SISFGSLAVA ILIIGYFRRL HCTRNYIHLH
LFVSFMLRAX SIFVKDRVAQ AHLGVEALQS LVMQGDLQNF IGGPSVDKSQ YVGCKIAVVM
FIYFLATNYY WILVEGLYLH NLIFVSFFSD TKYLWGFILI GWGFPAVFVV AWAVARATLA
DTRCWELSAG DRWIYXXPIL AAIGLNFILF LNTVRVLATK IWETNAVGHD MRKQYRKLAK
STLVLVLVFG VHYIVFICQP HSFSGLWWEI RMHCELFFNS FQGFFVSIVY CYCNGEVQAE
VKKTWTRWNL SIDWKKAPPC GGHRYGSVLT TVTHSTSSQS QMGPSTRLVL ISSKPAKTAC
RQIDSHVTLP GYVWSSSEQD CQPQSTPEET KKGHGRQEDD SPVGESSRPV AFTIDTEGCK
GESHPI
