UniProt functional annotation for P47708



	UniProt functional annotation for P47708

UniProt code: P47708.

Organism: Mus musculus (Mouse).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.

Function: Plays an essential role in docking and fusion steps of regulated exocytosis (By similarity). At the presynaptic level, RPH3A is recruited by RAB3A to the synaptic vesicle membrane in a GTP- dependent manner where it modulates synaptic vesicle trafficking and calcium-triggered neurotransmitter release (By similarity). In the post-synaptic compartment, forms a ternary complex with GRIN2A and DLG4 and regulates NMDA receptor stability. Plays also a role in the exocytosis of arginine vasopressin hormone (By similarity). {ECO:0000250|UniProtKB:P47709}.

Cofactor: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};

Subunit: Interacts with RAB3B, RAB3C, RAB3D, RAB8A, RAB27A and RAB27B (PubMed:12578829). Interacts with RAB3A; this interaction recruits RPH3A to synaptic vesicules (By similarity). Interacts (via C2B domain) with SNAP25 (By similarity). Interacts with deubiquitinating enzyme CAND1; this interaction results in the deubiquitination of RPH3A (By similarity). Interacts with GRIN2A and DLG4; this ternary complex regulates NMDA receptor composition at postsynaptic membranes (By similarity). Interacts with SNCA (By similarity). {ECO:0000250|UniProtKB:P47709, ECO:0000250|UniProtKB:Q9Y2J0, ECO:0000269|PubMed:12578829}.

Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:P47709}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P47709}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250|UniProtKB:P47709}. Membrane {ECO:0000250|UniProtKB:P47709}; Peripheral membrane protein {ECO:0000250|UniProtKB:P47709}.

Tissue specificity: Specifically expressed in brain.

Domain: Binds calcium via the C2 domains. The calcium-bound C2 domains mediate interactions with phospholipid bilayers.

Ptm: Ubiquitinated. Deubiquitinated by CAND1 to prevent its degradation. {ECO:0000250|UniProtKB:P47709}.

Disruption phenotype: No visible phenotype. Mice are viable and fertile and do not display any physiological impairment. Additionally, synaptic properties seem unaffected. {ECO:0000269|PubMed:10407024}.

Annotations taken from UniProtKB at the EBI.


Organism:		Mus musculus (Mouse).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.



Function:		Plays an essential role in docking and fusion steps of regulated exocytosis (By similarity). At the presynaptic level, RPH3A is recruited by RAB3A to the synaptic vesicle membrane in a GTP- dependent manner where it modulates synaptic vesicle trafficking and calcium-triggered neurotransmitter release (By similarity). In the post-synaptic compartment, forms a ternary complex with GRIN2A and DLG4 and regulates NMDA receptor stability. Plays also a role in the exocytosis of arginine vasopressin hormone (By similarity). {ECO:0000250\|UniProtKB:P47709}.


Cofactor:		Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255\|PROSITE-ProRule:PRU00041};
Subunit:		Interacts with RAB3B, RAB3C, RAB3D, RAB8A, RAB27A and RAB27B (PubMed:12578829). Interacts with RAB3A; this interaction recruits RPH3A to synaptic vesicules (By similarity). Interacts (via C2B domain) with SNAP25 (By similarity). Interacts with deubiquitinating enzyme CAND1; this interaction results in the deubiquitination of RPH3A (By similarity). Interacts with GRIN2A and DLG4; this ternary complex regulates NMDA receptor composition at postsynaptic membranes (By similarity). Interacts with SNCA (By similarity). {ECO:0000250\|UniProtKB:P47709, ECO:0000250\|UniProtKB:Q9Y2J0, ECO:0000269\|PubMed:12578829}.
Subcellular location:		Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250\|UniProtKB:P47709}. Cell projection, dendritic spine {ECO:0000250\|UniProtKB:P47709}. Cell junction, synapse, postsynaptic cell membrane {ECO:0000250\|UniProtKB:P47709}. Membrane {ECO:0000250\|UniProtKB:P47709}; Peripheral membrane protein {ECO:0000250\|UniProtKB:P47709}.
Tissue specificity:		Specifically expressed in brain.
Domain:		Binds calcium via the C2 domains. The calcium-bound C2 domains mediate interactions with phospholipid bilayers.
Ptm:		Ubiquitinated. Deubiquitinated by CAND1 to prevent its degradation. {ECO:0000250\|UniProtKB:P47709}.
Disruption phenotype:		No visible phenotype. Mice are viable and fertile and do not display any physiological impairment. Additionally, synaptic properties seem unaffected. {ECO:0000269\|PubMed:10407024}.