RPH3A

From Wikipedia, the free encyclopedia
Jump to: navigation, search
Rabphilin 3A
Protein RPH3A PDB 1zbd.png
PDB rendering based on 1zbd.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols RPH3A ; KIAA0985
External IDs OMIM612159 MGI102788 HomoloGene7921 GeneCards: RPH3A Gene
RNA expression pattern
PBB GE RPH3A 205230 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 22895 19894
Ensembl ENSG00000089169 ENSMUSG00000029608
UniProt Q9Y2J0 P47708
RefSeq (mRNA) NM_001143854 NM_011286
RefSeq (protein) NP_001137326 NP_035416
Location (UCSC) Chr 12:
113.01 – 113.34 Mb
Chr 5:
120.94 – 121.01 Mb
PubMed search [1] [2]

Rabphilin-3A is a protein that in humans is encoded by the RPH3A gene.[1][2][3] 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.[4]


Interactions[edit]

RPH3A has been shown to interact with RAB3A,[5][6][7] RAB3B[5][7] and CASK.[8]

References[edit]

  1. ^ 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. 
  2. ^ 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. PMID 7822236. 
  3. ^ "Entrez Gene: RPH3A rabphilin 3A homolog (mouse)". 
  4. ^ 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. 
  5. ^ 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. (United States) 278 (17): 15373–80. doi:10.1074/jbc.M212341200. ISSN 0021-9258. PMID 12578829. 
  6. ^ 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 (UNITED STATES) 96 (3): 363–74. doi:10.1016/S0092-8674(00)80549-8. ISSN 0092-8674. PMID 10025402. 
  7. ^ 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. (UNITED STATES) 271 (12): 6963–71. doi:10.1074/jbc.271.12.6963. ISSN 0021-9258. PMID 8636125. 
  8. ^ Zhang, Y; Luan Z; Liu A; Hu G (May 2001). "The scaffolding protein CASK mediates the interaction between rabphilin3a and beta-neurexins". FEBS Lett. (Netherlands) 497 (2-3): 99–102. doi:10.1016/S0014-5793(01)02450-4. ISSN 0014-5793. PMID 11377421. 

Further reading[edit]