P47709: Rabphilin-3A (Rph3a)

Rabphilin-3A (Rph3a) is a 684-residue protein from Rattus norvegicus. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P47709.

Gene
Rph3a
Organism
Rattus norvegicus
Length
684 residues
Mean pLDDT
69.2
Model
AF-P47709-F1 v6
Model created
1 Aug 2025
PDB structures
11

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Model confidence (pLDDT)

The mean pLDDT of this model is 69.2 (low overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate37%
70 to 90Confident: backbone generally right18%
50 to 70Low: treat with caution6%
Below 50Very low: often disordered regions39%

What pLDDT means and how to read it

Function

Plays an essential role in docking and fusion steps of regulated exocytosis (PubMed:16203731, PubMed:8617225). 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 (PubMed:8617225). In the post-synaptic compartment, forms a ternary complex with GRIN2A and DLG4 and regulates NMDA receptor stability (PubMed:26679993). Also plays a role in the exocytosis of arginine vasopressin hormone (PubMed:29367474)

Subunit structure

Interacts with RAB3B, RAB3C, RAB3D, RAB8A, RAB27A and RAB27B (By similarity). Interacts with RAB3A; this interaction recruits RPH3A to synaptic vesicules (PubMed:10025402, PubMed:8617225). Interacts (via C2B domain) with SNAP25 (PubMed:16203731, PubMed:28634303). Interacts with deubiquitinating enzyme CAND1; this interaction results in the deubiquitination of RPH3A (PubMed:29367474). Interacts…

Subcellular location

Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane, Cell projection, dendritic spine, Postsynaptic cell membrane, Membrane

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
2CM5X-ray1.28 ÅA=519-684
4NS0X-ray1.8 ÅA=378-510
2CM6X-ray1.85 ÅA/B=519-684
2CHDX-ray1.92 ÅA=371-510
4NP9X-ray1.92 ÅA=378-510
4LT7X-ray2.5 ÅA=378-510
5LO8X-ray2.5 ÅA/B=536-680
1ZBDX-ray2.6 ÅB=38-170
5LOWX-ray2.8 ÅA/B/C/H/I/J=536-680
5LOBX-ray3.3 ÅA/B/C=536-680
3RPBNMRA=541-680

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