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   08-NOV-2023, entry version 129.
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   GlyCosmos; P70555; 4 sites, No reported glycans.
DR   GlyGen; P70555; 4 sites.
DR   PhosphoSitePlus; P70555; -.
DR   PaxDb; 10116-ENSRNOP00000021099; -.
DR   GeneID; 81753; -.
DR   KEGG; rno:81753; -.
DR   UCSC; RGD:620612; rat.
DR   AGR; RGD:620612; -.
DR   CTD; 5746; -.
DR   RGD; 620612; Pth2r.
DR   eggNOG; KOG4564; Eukaryota.
DR   InParanoid; P70555; -.
DR   OrthoDB; 5397182at2759; -.
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: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; GPCR, family 2, extracellular hormone receptor domain; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
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   PANTHER; PTHR45620:SF7; PARATHYROID HORMONE 2 RECEPTOR; 1.
DR   PANTHER; PTHR45620; PDF RECEPTOR-LIKE PROTEIN-RELATED; 1.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF02793; HRM; 1.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   SMART; SM00008; HormR; 1.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   SUPFAM; SSF111418; Hormone receptor domain; 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
//