ID   PTH2R_MOUSE             Reviewed;         546 AA.
AC   Q91V95;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 149.
DE   RecName: Full=Parathyroid hormone 2 receptor;
DE            Short=PTH2 receptor;
DE   Flags: Precursor;
GN   Name=Pth2r; Synonyms=Pthr2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ILS, and ISS;
RX   PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT   "High-throughput sequence identification of gene coding variants within
RT   alcohol-related QTLs.";
RL   Mamm. Genome 12:657-663(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
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   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC       {ECO:0000305}.
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DR   EMBL; AF332077; AAK56105.1; -; mRNA.
DR   EMBL; AF332078; AAK56106.1; -; mRNA.
DR   EMBL; AK045576; BAC32420.1; -; mRNA.
DR   CCDS; CCDS15017.1; -.
DR   RefSeq; NP_644676.1; NM_139270.2.
DR   AlphaFoldDB; Q91V95; -.
DR   SMR; Q91V95; -.
DR   STRING; 10090.ENSMUSP00000027083; -.
DR   GlyCosmos; Q91V95; 4 sites, No reported glycans.
DR   GlyGen; Q91V95; 4 sites.
DR   PhosphoSitePlus; Q91V95; -.
DR   PaxDb; 10090-ENSMUSP00000027083; -.
DR   ProteomicsDB; 291586; -.
DR   Antibodypedia; 20012; 258 antibodies from 28 providers.
DR   DNASU; 213527; -.
DR   Ensembl; ENSMUST00000027083.7; ENSMUSP00000027083.7; ENSMUSG00000025946.14.
DR   GeneID; 213527; -.
DR   KEGG; mmu:213527; -.
DR   UCSC; uc007bhu.1; mouse.
DR   AGR; MGI:2180917; -.
DR   CTD; 5746; -.
DR   MGI; MGI:2180917; Pth2r.
DR   VEuPathDB; HostDB:ENSMUSG00000025946; -.
DR   eggNOG; KOG4564; Eukaryota.
DR   GeneTree; ENSGT00940000159094; -.
DR   HOGENOM; CLU_002753_4_3_1; -.
DR   InParanoid; Q91V95; -.
DR   OMA; PGYVWSG; -.
DR   OrthoDB; 5397182at2759; -.
DR   PhylomeDB; Q91V95; -.
DR   TreeFam; TF315710; -.
DR   Reactome; R-MMU-373080; Class B/2 (Secretin family receptors).
DR   Reactome; R-MMU-418555; G alpha (s) signalling events.
DR   BioGRID-ORCS; 213527; 0 hits in 78 CRISPR screens.
DR   ChiTaRS; Pth2r; mouse.
DR   PRO; PR:Q91V95; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q91V95; Protein.
DR   Bgee; ENSMUSG00000025946; Expressed in medial geniculate body and 31 other cell types or tissues.
DR   ExpressionAtlas; Q91V95; baseline and differential.
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; ISO:MGI.
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; IMP: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.
DR   Genevisible; Q91V95; MM.
PE   1: Evidence at protein 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_0000012850"
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          497..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..522
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;  61908 MW;  628051EF181A1DF3 CRC64;
     MAWLETFTYI CGWLILSSCL LVRAQLDSDG TITIEEQIVL VMKAKMQCEL NITAQLQEGE
     GNCFPEWDGI ICWPRGTVGK MSAVPCPPYV YDFNHKGVAF RHCTPNGTWD SIHGSNKTWA
     NYSDCFLQPD INIGKQEFFE SLYILYTVGY SISFGSLAVA ILIIGYFRRL HCTRNYIHLH
     LFVSFMLRAM SIFVKDRVAQ AHLGVEALQS LVMQGDLQNF IGGPSVDKSQ YVGCKIAVVM
     FIYFLATNYY WILVEGLYLH NLIFVSFFSD TKYLWGFISI GWGFPAVFVV AWAVARATLA
     DTRCWELSAG DRWIYQAPIL AAIGLNFILF LNTVRVLATK IWETNAVGHD MRKQYRKLAK
     STLVLVLVFG VHYIVFVCQP HSFSGLWWEI RMHCELFFNS FQGFFVSIVY CYCNGEVQAE
     VKKMWTRWNL SIDWKRAPPC GGQRYGSVLT TVTHSTSSQS QMGASTRLVL ISGKPTKNAC
     RQIDSHVTLP GYVWSSSEQD CQTHSPPEET KEGHRRQGDD SPVMESSRPV AFTLDTEGCK
     GETHPI
//