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Contents

   



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1 Function  





2 See also  





3 References  





4 Further reading  





5 External links  














Prokineticin receptor 2






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PROKR2
Identifiers
AliasesPROKR2, GPR73L1, GPR73b, GPRg2, HH3, KAL3, PKR2, dJ680N4.3, prokineticin receptor 2
External IDsOMIM: 607123; MGI: 2181363; HomoloGene: 16368; GeneCards: PROKR2; OMA:PROKR2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_144773

NM_144944

RefSeq (protein)

NP_658986

NP_659193

Location (UCSC)Chr 20: 5.3 – 5.32 MbChr 2: 132.18 – 132.23 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Prokineticin receptor 2 (PKR2), is a dimeric[5] G protein-coupled receptor encoded by the PROKR2 gene in humans.[6]

Function[edit]

Prokineticins are secreted proteins that can promote angiogenesis and induce strong gastrointestinal smooth muscle contraction. The protein encoded by this gene is an integral membrane protein and G protein-coupled receptor for prokineticins. PKR2 is composed of 384 amino acids. Asparagine residues at position 7 and 27 undergo N-linked glycosylation.[5] Cysteine residues at position 128 and 208 form a disulfide bond.[5] The encoded protein is similar in sequence to GPR73, another G protein-coupled receptor for prokineticins.[6] PKR2 is also linked to mammalian circadian rhythm.[7] Levels of PKR2 mRNA fluctuate in the suprachiasmatic nucleus, increasing during the day and decreasing at night.[7]

Mutations in the PROKR2 (also known as KAL3) gene have been implicated in hypogonadotropic hypogonadism and gynecomastia.[8] Total loss of PKR2 in mice leads to spontaneous torpor usually beginning at dusk and lasting for 8 hours on average.[9]

PKR2 functions as a G protein-coupled receptor, thus it has a signaling cascade when it's ligand binds. PKR2 is a Gq-coupled protein, so when the ligand binds, beta-type phospholipase C is activated which creates inositol triphosphate. This then triggers calcium release inside the cell.[10]

See also[edit]

References[edit]

  • ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  • ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  • ^ a b c Sposini S, Caltabiano G, Hanyaloglu AC, Miele R (January 2015). "Identification of transmembrane domains that regulate spatial arrangements and activity of prokineticin receptor 2 dimers". Molecular and Cellular Endocrinology. 399: 362–372. doi:10.1016/j.mce.2014.10.024. hdl:10044/1/31246. PMID 25449422. S2CID 13491537.
  • ^ a b "Entrez Gene: PROKR2 prokineticin receptor 2".
  • ^ a b Masumoto KH, Nagano M, Takashima N, Hayasaka N, Hiyama H, Matsumoto S, et al. (June 2006). "Distinct localization of prokineticin 2 and prokineticin receptor 2 mRNAs in the rat suprachiasmatic nucleus". The European Journal of Neuroscience. 23 (11): 2959–2970. doi:10.1111/j.1460-9568.2006.04834.x. PMID 16819985. S2CID 20510543.
  • ^ Narula HS, Carlson HE (November 2014). "Gynaecomastia--pathophysiology, diagnosis and treatment". Nature Reviews. Endocrinology. 10 (11): 684–698. doi:10.1038/nrendo.2014.139. PMID 25112235. S2CID 40159424.
  • ^ Jethwa PH, I'Anson H, Warner A, Prosser HM, Hastings MH, Maywood ES, Ebling FJ (June 2008). "Loss of prokineticin receptor 2 signaling predisposes mice to torpor". American Journal of Physiology. Regulatory, Integrative and Comparative Physiology. 294 (6): R1968–R1979. doi:10.1152/ajpregu.00778.2007. PMC 2735815. PMID 18417646.
  • ^ Martin C, Balasubramanian R, Dwyer AA, Au MG, Sidis Y, Kaiser UB, et al. (April 2011). "The role of the prokineticin 2 pathway in human reproduction: evidence from the study of human and murine gene mutations". Endocrine Reviews. 32 (2): 225–246. doi:10.1210/er.2010-0007. PMC 3365793. PMID 21037178.
  • Further reading[edit]

  • Soga T, Matsumoto Si, Oda T, Saito T, Hiyama H, Takasaki J, et al. (December 2002). "Molecular cloning and characterization of prokineticin receptors". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1579 (2–3): 173–179. doi:10.1016/S0167-4781(02)00546-8. PMID 12427552.
  • Battersby S, Critchley HO, Morgan K, Millar RP, Jabbour HN (May 2004). "Expression and regulation of the prokineticins (endocrine gland-derived vascular endothelial growth factor and Bv8) and their receptors in the human endometrium across the menstrual cycle". The Journal of Clinical Endocrinology and Metabolism. 89 (5): 2463–2469. doi:10.1210/jc.2003-032012. PMID 15126578.
  • Pasquali D, Rossi V, Staibano S, De Rosa G, Chieffi P, Prezioso D, et al. (September 2006). "The endocrine-gland-derived vascular endothelial growth factor (EG-VEGF)/prokineticin 1 and 2 and receptor expression in human prostate: Up-regulation of EG-VEGF/prokineticin 1 with malignancy". Endocrinology. 147 (9): 4245–4251. doi:10.1210/en.2006-0614. PMID 16763065.
  • Dodé C, Teixeira L, Levilliers J, Fouveaut C, Bouchard P, Kottler ML, et al. (October 2006). "Kallmann syndrome: mutations in the genes encoding prokineticin-2 and prokineticin receptor-2". PLOS Genetics. 2 (10): e175. doi:10.1371/journal.pgen.0020175. PMC 1617130. PMID 17054399.
  • External links[edit]

  • t
  • e
  • This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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