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From Wikipedia, the free encyclopedia

RPH3A
Identifiers
AliasesRPH3A
External IDsOMIM: 612159; MGI: 102788; HomoloGene: 7921; GeneCards: RPH3A; OMA:RPH3A - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001143854
NM_014954

NM_011286
NM_001302344
NM_001302345

RefSeq (protein)

NP_001289273
NP_001289274
NP_035416

Location (UCSC)n/aChr 5: 121.08 – 121.15 Mb
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

Rabphilin-3A is a protein that in humans is encoded by the RPH3A gene.[4][5][6] It contains two C2 domains and binds calcium ions at low micromolar concentration. Rabphilin was shown to regulate neurotransmitter release in hippocampal neurons after neurons had an increased synaptic activity and their release rate was depressed.[7]

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Transcription

Interactions

RPH3A has been shown to interact with RAB3A,[8][9][10] RAB3B[8][10] and CASK.[11]

References

  1. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000029608Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (July 1999). "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 6 (1): 63–70. doi:10.1093/dnares/6.1.63. PMID 10231032.
  5. ^ Inagaki N, Mizuta M, Seino S (February 1995). "Cloning of a mouse Rabphilin-3A expressed in hormone-secreting cells". J Biochem. 116 (2): 239–42. doi:10.1093/oxfordjournals.jbchem.a124512. PMID 7822236.
  6. ^ "Entrez Gene: RPH3A rabphilin 3A homolog (mouse)".
  7. ^ Deák F, Shin OH, Tang J, Hanson P, Ubach J, Jahn R, Rizo J, Kavalali ET, Südhof TC (2006). "Rabphilin regulates SNARE-dependent re-priming of synaptic vesicles for fusion". EMBO J. 25 (12): 2856–66. doi:10.1038/sj.emboj.7601165. PMC 1500841. PMID 16763567.
  8. ^ a b Fukuda, Mitsunori (April 2003). "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2. Identification of a critical determinant of Rab3A/Rab27A recognition by Rim2". J. Biol. Chem. 278 (17): 15373–80. doi:10.1074/jbc.M212341200. ISSN 0021-9258. PMID 12578829.
  9. ^ Ostermeier, C; Brunger A T (February 1999). "Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A". Cell. 96 (3): 363–74. doi:10.1016/S0092-8674(00)80549-8. ISSN 0092-8674. PMID 10025402. S2CID 15162326.
  10. ^ a b Weber, E; Jilling T; Kirk K L (March 1996). "Distinct functional properties of Rab3A and Rab3B in PC12 neuroendocrine cells". J. Biol. Chem. 271 (12): 6963–71. doi:10.1074/jbc.271.12.6963. ISSN 0021-9258. PMID 8636125.
  11. ^ Zhang, Y; Luan Z; Liu A; Hu G (May 2001). "The scaffolding protein CASK mediates the interaction between rabphilin3a and beta-neurexins". FEBS Lett. 497 (2–3): 99–102. doi:10.1016/S0014-5793(01)02450-4. ISSN 0014-5793. PMID 11377421. S2CID 33119468.

Further reading

This page was last edited on 20 November 2023, at 18:42
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