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Q91V95 (PTH2R_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Parathyroid hormone 2 receptor

Short name=PTH2 receptor
Gene names
Name:Pth2r
Synonyms:Pthr2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length546 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This is a specific receptor for parathyroid hormone. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. PTH2R may be responsible for PTH effects in a number of physiological systems. It may play a significant role in pancreatic function. PTH2R presence in neurons indicates that it may function as a neurotransmitter receptor By similarity.

Subunit structure

Binds to TIPF39/TIP39. Ref.3

Subcellular location

Cell membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the G-protein coupled receptor 2 family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 546522Parathyroid hormone 2 receptor
PRO_0000012850

Regions

Topological domain27 – 143117Extracellular Potential
Transmembrane144 – 16724Helical; Name=1; Potential
Topological domain168 – 1747Cytoplasmic Potential
Transmembrane175 – 19420Helical; Name=2; Potential
Topological domain195 – 23541Extracellular Potential
Transmembrane236 – 25823Helical; Name=3; Potential
Topological domain259 – 27315Cytoplasmic Potential
Transmembrane274 – 29522Helical; Name=4; Potential
Topological domain296 – 31318Extracellular Potential
Transmembrane314 – 33421Helical; Name=5; Potential
Topological domain335 – 36127Cytoplasmic Potential
Transmembrane362 – 38019Helical; Name=6; Potential
Topological domain381 – 39111Extracellular Potential
Transmembrane392 – 41423Helical; Name=7; Potential
Topological domain415 – 546132Cytoplasmic Potential

Amino acid modifications

Glycosylation511N-linked (GlcNAc...) Potential
Glycosylation1061N-linked (GlcNAc...) Potential
Glycosylation1161N-linked (GlcNAc...) Potential
Glycosylation1211N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q91V95 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 628051EF181A1DF3

FASTA54661,908
        10         20         30         40         50         60 
MAWLETFTYI CGWLILSSCL LVRAQLDSDG TITIEEQIVL VMKAKMQCEL NITAQLQEGE 

        70         80         90        100        110        120 
GNCFPEWDGI ICWPRGTVGK MSAVPCPPYV YDFNHKGVAF RHCTPNGTWD SIHGSNKTWA 

       130        140        150        160        170        180 
NYSDCFLQPD INIGKQEFFE SLYILYTVGY SISFGSLAVA ILIIGYFRRL HCTRNYIHLH 

       190        200        210        220        230        240 
LFVSFMLRAM SIFVKDRVAQ AHLGVEALQS LVMQGDLQNF IGGPSVDKSQ YVGCKIAVVM 

       250        260        270        280        290        300 
FIYFLATNYY WILVEGLYLH NLIFVSFFSD TKYLWGFISI GWGFPAVFVV AWAVARATLA 

       310        320        330        340        350        360 
DTRCWELSAG DRWIYQAPIL AAIGLNFILF LNTVRVLATK IWETNAVGHD MRKQYRKLAK 

       370        380        390        400        410        420 
STLVLVLVFG VHYIVFVCQP HSFSGLWWEI RMHCELFFNS FQGFFVSIVY CYCNGEVQAE 

       430        440        450        460        470        480 
VKKMWTRWNL SIDWKRAPPC GGQRYGSVLT TVTHSTSSQS QMGASTRLVL ISGKPTKNAC 

       490        500        510        520        530        540 
RQIDSHVTLP GYVWSSSEQD CQTHSPPEET KEGHRRQGDD SPVMESSRPV AFTLDTEGCK 


GETHPI 

« Hide

References

« Hide 'large scale' references
[1]"High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ILS and ISS.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Brain.
[3]"Identification and characterization of the murine and human gene encoding the tuberoinfundibular peptide of 39 residues."
John M.R., Arai M., Rubin D.A., Jonsson K.B., Jueppner H.
Endocrinology 143:1047-1057(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TIPF39/TI39.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF332077 mRNA. Translation: AAK56105.1.
AF332078 mRNA. Translation: AAK56106.1.
AK045576 mRNA. Translation: BAC32420.1.
RefSeqNP_644676.1. NM_139270.2.
UniGeneMm.294225.

3D structure databases

ProteinModelPortalQ91V95.
SMRQ91V95. Positions 24-420.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000027083.

Chemistry

GuidetoPHARMACOLOGY332.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteQ91V95.

Proteomic databases

PaxDbQ91V95.
PRIDEQ91V95.

Protocols and materials databases

DNASU213527.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027083; ENSMUSP00000027083; ENSMUSG00000025946.
GeneID213527.
KEGGmmu:213527.
UCSCuc007bhu.1. mouse.

Organism-specific databases

CTD5746.
MGIMGI:2180917. Pth2r.

Phylogenomic databases

eggNOGNOG293423.
GeneTreeENSGT00750000117453.
HOGENOMHOG000008248.
HOVERGENHBG008318.
InParanoidQ91V95.
KOK04586.
OMAVGCKIAV.
OrthoDBEOG7TF78W.
PhylomeDBQ91V95.
TreeFamTF315710.

Gene expression databases

BgeeQ91V95.
CleanExMM_PTH2R.
GenevestigatorQ91V95.

Family and domain databases

InterProIPR017981. GPCR_2-like.
IPR001879. GPCR_2_extracellular_dom.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
[Graphical view]
PfamPF00002. 7tm_2. 1 hit.
PF02793. HRM. 1 hit.
[Graphical view]
PRINTSPR00249. GPCRSECRETIN.
SMARTSM00008. HormR. 1 hit.
[Graphical view]
PROSITEPS00649. G_PROTEIN_RECEP_F2_1. 1 hit.
PS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
PS50227. G_PROTEIN_RECEP_F2_3. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio374025.
PROQ91V95.
SOURCESearch...

Entry information

Entry namePTH2R_MOUSE
AccessionPrimary (citable) accession number: Q91V95
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries