PTH2R_MOUSE
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 03-AUG-2022, entry version 140.
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 GlyGen; Q91V95; 4 sites.
DR PhosphoSitePlus; Q91V95; -.
DR PaxDb; Q91V95; -.
DR PRIDE; Q91V95; -.
DR Antibodypedia; 20012; 230 antibodies from 28 providers.
DR DNASU; 213527; -.
DR Ensembl; ENSMUST00000027083; ENSMUSP00000027083; ENSMUSG00000025946.
DR GeneID; 213527; -.
DR KEGG; mmu:213527; -.
DR UCSC; uc007bhu.1; mouse.
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; SLHVWGW; -.
DR OrthoDB; 651627at2759; -.
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 73 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 29 other tissues.
DR ExpressionAtlas; Q91V95; baseline and differential.
DR Genevisible; Q91V95; MM.
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; 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; -; 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 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
