Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

12 structures for P47709

Entry ID Method Resolution Chain Position Source
1ZBD X-ray 260 A B 41-170 PDB
2CHD X-ray 192 A A 371-510 PDB
2CM5 X-ray 128 A A 519-684 PDB
2CM6 X-ray 185 A A/B 519-684 PDB
3RPB NMR - A 541-680 PDB
4LT7 X-ray 250 A A 378-510 PDB
4NP9 X-ray 192 A A 378-510 PDB
4NS0 X-ray 180 A A 378-510 PDB
5LO8 X-ray 250 A A/B 536-680 PDB
5LOB X-ray 330 A A/B/C 536-680 PDB
5LOW X-ray 280 A A/B/C/H/I/J 536-680 PDB
AF-P47709-F1 Predicted AlphaFoldDB

No variants for P47709

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P47709

No associated diseases with P47709

11 regional properties for P47709

Type Name Position InterPro Accession
domain C2 domain 382 - 504 IPR000008-1
domain C2 domain 540 - 673 IPR000008-2
domain Synaptotagmin 544 - 559 IPR001565-1
domain Synaptotagmin 559 - 572 IPR001565-2
domain Synaptotagmin 616 - 631 IPR001565-3
domain Synaptotagmin 636 - 646 IPR001565-4
domain Rab-binding domain 40 - 157 IPR010911
domain Zinc finger, FYVE-related 88 - 145 IPR017455
domain Rabphilin-3A, FYVE domain 88 - 168 IPR028698
domain FYVE-type zinc finger 45 - 157 IPR041282
domain Rabphilin/Doc2, first C2 domain 383 - 506 IPR047022

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane
  • Cell projection, dendritic spine
  • Postsynaptic cell membrane
  • Membrane ; Peripheral membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

15 GO annotations of cellular component

Name Definition
anchoring junction A cell junction that mechanically attaches a cell (and its cytoskeleton) to neighboring cells or to the extracellular matrix.
cholinergic synapse A synapse that uses acetylcholine as a neurotransmitter.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
dendritic spine A small, membranous protrusion from a dendrite that forms a postsynaptic compartment, typically receiving input from a single presynapse. They function as partially isolated biochemical and an electrical compartments. Spine morphology is variable:they can be thin, stubby, mushroom, or branched, with a continuum of intermediate morphologies. They typically terminate in a bulb shape, linked to the dendritic shaft by a restriction. Spine remodeling is though to be involved in synaptic plasticity.
extrinsic component of membrane The component of a membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region.
extrinsic component of synaptic vesicle membrane The component of the synaptic vesicle membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region.
neuromuscular junction The junction between the axon of a motor neuron and a muscle fiber. In response to the arrival of action potentials, the presynaptic button releases molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane of the muscle fiber, leading to a change in post-synaptic potential.
neuron projection A prolongation or process extending from a nerve cell, e.g. an axon or dendrite.
postsynaptic membrane A specialized area of membrane facing the presynaptic membrane on the tip of the nerve ending and separated from it by a minute cleft (the synaptic cleft). Neurotransmitters cross the synaptic cleft and transmit the signal to the postsynaptic membrane.
presynapse The part of a synapse that is part of the presynaptic cell.
protein-containing complex A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.
secretory granule A small subcellular vesicle, surrounded by a membrane, that is formed from the Golgi apparatus and contains a highly concentrated protein destined for secretion. Secretory granules move towards the periphery of the cell and upon stimulation, their membranes fuse with the cell membrane, and their protein load is exteriorized. Processing of the contained protein may take place in secretory granules.
synapse The junction between an axon of one neuron and a dendrite of another neuron, a muscle fiber or a glial cell. As the axon approaches the synapse it enlarges into a specialized structure, the presynaptic terminal bouton, which contains mitochondria and synaptic vesicles. At the tip of the terminal bouton is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic terminal bouton secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane.
synaptic vesicle A secretory organelle, typically 50 nm in diameter, of presynaptic nerve terminals; accumulates in high concentrations of neurotransmitters and secretes these into the synaptic cleft by fusion with the 'active zone' of the presynaptic plasma membrane.
synaptic vesicle membrane The lipid bilayer surrounding a synaptic vesicle.

10 GO annotations of molecular function

Name Definition
calcium ion binding Binding to a calcium ion (Ca2+).
calcium-dependent phospholipid binding Binding to a phospholipid, a class of lipids containing phosphoric acid as a mono- or diester, in the presence of calcium.
inositol 1,4,5 trisphosphate binding Binding to inositol 1,4,5 trisphosphate.
phosphate ion binding Binding to a phosphate ion.
phosphatidylinositol-4,5-bisphosphate binding Binding to phosphatidylinositol-4,5-bisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 4' and 5' positions.
phospholipid binding Binding to a phospholipid, a class of lipids containing phosphoric acid as a mono- or diester.
protein-containing complex binding Binding to a macromolecular complex.
selenium binding Binding to a selenium (Se) ion.
small GTPase binding Binding to a small monomeric GTPase.
zinc ion binding Binding to a zinc ion (Zn).

7 GO annotations of biological process

Name Definition
brain development The process whose specific outcome is the progression of the brain over time, from its formation to the mature structure. Brain development begins with patterning events in the neural tube and ends with the mature structure that is the center of thought and emotion. The brain is responsible for the coordination and control of bodily activities and the interpretation of information from the senses (sight, hearing, smell, etc.).
dendritic spine organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a dendritic spine. A dendritic spine is a specialized protrusion from a neuronal dendrite and is involved in synaptic transmission.
exocytosis A process of secretion by a cell that results in the release of intracellular molecules (e.g. hormones, matrix proteins) contained within a membrane-bounded vesicle. Exocytosis can occur either by full fusion, when the vesicle collapses into the plasma membrane, or by a kiss-and-run mechanism that involves the formation of a transient contact, a pore, between a granule (for exemple of chromaffin cells) and the plasma membrane. The latter process most of the time leads to only partial secretion of the granule content. Exocytosis begins with steps that prepare vesicles for fusion with the membrane (tethering and docking) and ends when molecules are secreted from the cell.
intracellular protein transport The directed movement of proteins in a cell, including the movement of proteins between specific compartments or structures within a cell, such as organelles of a eukaryotic cell.
regulation of calcium ion-dependent exocytosis Any process that modulates the frequency, rate or extent of calcium ion-dependent exocytosis.
regulation of NMDA receptor activity Any process that modulates the frequency, rate or extent of N-methyl-D-aspartate selective glutamate receptor activity.
spontaneous neurotransmitter secretion Neurotransmitter secretion that occurs in the absence of the action of a secretagogue or a presynaptic action potential.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q06846 RPH3A Rabphilin-3A Bos taurus (Bovine) PR
Q14183 DOC2A Double C2-like domain-containing protein alpha Homo sapiens (Human) PR
Q9Y2J0 RPH3A Rabphilin-3A Homo sapiens (Human) PR
Q7TNF0 Doc2a Double C2-like domain-containing protein alpha Mus musculus (Mouse) PR
P47708 Rph3a Rabphilin-3A Mus musculus (Mouse) PR
10 20 30 40 50 60
MTDTVVNRWM YPGDGPLQSN DKEQLQAGWS VHPGAQTDRQ RKQEELTDEE KEIINRVIAR
70 80 90 100 110 120
AEKMETMEQE RIGRLVDRLE TMRKNVAGDG VNRCILCGEQ LGMLGSACVV CEDCKKNVCT
130 140 150 160 170 180
KCGVETSNNR PHPVWLCKIC LEQREVWKRS GAWFFKGFPK QVLPQPMPIK KTKPQQPAGE
190 200 210 220 230 240
PATQEQPTPE SRHPARAPAR GDMEDRRAPG QKPGPDLTSA PGRGSHGPPT RRASEARMST
250 260 270 280 290 300
TTRDSEGWDH GHGGGAGDTS RSPGGEQGLR RANSVQASRP APASMPSPAP PQPVQPGPPG
310 320 330 340 350 360
GSRAAPGPGR FPEQSTEAPP SDPGYPGAVA PAREERTGPT GGFQAAPHTA GPYSQAAPAR
370 380 390 400 410 420
QPPPAEEEEE EANSYDSDQA TTLGALEFSL LYDQDNSNLQ CTIIRAKGLK PMDSNGLADP
430 440 450 460 470 480
YVKLHLLPGA SKSNKLRTKT LRNTRNPVWN ETLQYHGITE EDMQRKTLRI SVCDEDKFGH
490 500 510 520 530 540
NEFIGETRFS LKKLKANQRK NFNICLERVI PMKRAGTTGS ARGMALYEEE QVERIGDIEE
550 560 570 580 590 600
RGKILVSLMY STQQGGLIVG IIRCVHLAAM DANGYSDPFV KLWLKPDMGK KAKHKTQIKK
610 620 630 640 650 660
KTLNPEFNEE FFYDIKHSDL AKKSLDISVW DYDIGKSNDY IGGCQLGISA KGERLKHWYE
670 680
CLKNKDKKIE RWHQLQNENH VSSD