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0RP3A_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionRabphilin-3a (exophilin-1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
Domain Architecture (Details)
InterPro domains assigned to SynO:
The small G protein Rab3A plays an important role in the regulation of neurotransmitter release. The crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A shows that the effector domain of rabphilin-3A contacts Rab3A in two distinct areas. The first interface involves the Rab3A switch I and switch II regions.hich are sensitive to the nucleotide-binding state of Rab3A. The second interface consists of a deep pocket in Rab3A that interacts with a SGAWFF structural element of rabphilin-3A. Sequence and structure analysis.nd biochemical data suggest that this pocket.r Rab complementarity-determining region (RabCDR).stablishes a specific interaction between each Rab protein and its effectors. It has been suggested that RabCDRs could be major determinants of effector specificity during vesicle trafficking and fusion .
  IPR003315:Rabphilin-3A effector
Synaptotagmins are synaptic vesicle membrane proteins found in abundance in nerve cells and some endocrine cells . The amino acid sequence of synaptotagmin comprises a single transmembrane region with a short vesicular N-terminal region.nd a cytoplasmic C-terminal region containing 2 internal repeats similar to the C2 regulatory domain of protein kinase C. The protein is believed to be important in the docking and fusion of synaptic vesicles with the plasma membrane..e. with neurotransmitter release .The 2 synaptotagmin C2 domains have been shown to have different functions: C2A binds phospholipid in a calcium-dependent manner.hile C2B binds inositol polyphosphate and phospholipid irrespective of the presence of Ca2+ . The structure of C2 domains in synaptotagmin I has been deduced: the C2 polypeptide forms an 8-stranded beta-sandwich constructed around a conserved 4-stranded motif.esignated a C2 key . The calcium binding region is a cup-shaped depression formed by the N- and C-terminal loops of the C2-key motif.hile the site of phospholipid interaction is thought to be a polybasic sequence on the hairpin loop connecting strands 3 and 4 .
InterPro domains unassigned to SynO:
The C2 domain is a Ca2+-dependent membrane-targeting module found in many cellular proteins involved in signal transduction or membrane trafficking. C2 domains are unique among membrane targeting domains in that they show wide range of lipid selectivity for the major components of cell membranes.ncluding phosphatidylserine and phosphatidylcholine. This C2 domain is about 116 amino-acid residues and is located between the two copies ofthe C1 domain in Protein Kinase C (that bind phorbol esters and diacylglycerol) (see )and the protein kinase catalytic domain (see ). Regions withsignificant homology to the C2-domain have been found in many proteins.The C2 domain is thought to be involved in calcium-dependent phospholipidbinding and in membrane targetting processes such as subcellular localisation. The 3D structure of theC2 domain of synaptotagmin has been reported.he domain forms an eight-stranded beta sandwich constructed around a conserved 4-stranded motif.esignated a C2 key . Calcium binds ina cup-shaped depression formed by the N- and C-terminal loops of theC2-key motif. Structural analyses of several C2 domains have shown them to consist of similar ternary structures in which three Ca2+-binding loops are located at the end of an 8 stranded antiparallel beta sandwich.
  IPR000008:C2 calcium-dependent membrane targeting
The Ca2+-dependent.ipid-binding domain (CaLB) has been identified in a number of proteins.or example the amino-terminal.38 amino acid C2 domain of cytosolic phospholipase A2 (cPLA2-C2) which mediates an initial step in the production of lipid mediators of inflammation: the Ca2+-dependent translocation of the enzyme to intracellular membranes with subsequent liberation of arachidonic acid. The domain is composed of eight antiparallel beta-strands with six interconnecting loops that fits the "type II" topology for C2 domains. The structure has been identified as a beta-sandwich in the "Greek key" motif .The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR008973:C2 calcium/lipid-binding region, CaLB
Zinc finger domains (ZnFs) are common.elatively small protein motifs that fold around one or more zinc ions. In addition to their role as a DNA-binding module.nFs have recently been shown to mediate protein:protein and protein:lipid interactions. There are at least 14 different classes of Zn fingers.hich differ in the nature and arrangement of their zinc-binding residues .The FYVE zinc finger domain is conserved from yeast to man.nd is named after four proteins that it has been found in: Fab1.OTB/ZK632.12.ac1.nd EEA1. It functions in the membrane recruitment of cytosolic proteins by binding to phosphatidylinositol 3-phosphate (PI3P).hich is found mainly on endosomes .The plant homeodomain (PHD) zinc finger domain has a C4HC3-type motif.nd is widely distributed in eukaryotes.eing found in many chromatin regulatory factors .Both the FYVE and the PHD zinc finger motifs display strikingly similar dimetal(zinc)-bound alpha+beta folds.The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR011011:Zinc finger, FYVE/PHD-type
SequencesProtein: RP3A_HUMAN (694 aa)
mRNA: AB023202 NM_014954
Local Annotation
Synapse Ontology
transport of vesicles in the presynaptic neuron
sdb:0017 Mobilization: synapsins, CAM kinase I  (Evidence:keywords,domains)
Fusion of intracellular membrane-bound vesicles with the pre-synaptic membrane of the neuronal cell resulting in release of neurotransmitter into the synaptic cleft.
sdb:0049 synaptic vesicle fusion  (Evidence:keywords,domains)
proteins that help to traffick the vesicle, such as synaptobrevin/Vamp, synaptotagmin, Rab3-rabphilin complex.
sdb:0097 vesicle trafficking protein  (Evidence:keywords,domains)
Various stages of the synaptic vesicle cycle, including attachment, prefusion, triggering, recycling and reloading of the vesicles with transmitter.
sdb:0098 synaptic vesicle cycling  (Evidence:keywords,domains)
interaction between synaptic vesicle and the scaffold.
sdb:0106 transport of synaptic vesicle in the presynaptic axon  (Evidence:keywords,domains)
priming for exocytosis prepares the calcium-dependent release and may involve partial fusion process. The vesicles are primed and become responsive to calcium.
sdb:0120 priming  (Evidence:keywords,domains)
sdb:0223 transmitter release  (Evidence:keywords,domains)
sdb:0328 transmitters release and endocytosis  (Evidence:keywords,domains)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 49 residues, 111714055-111714200Exon2: 42 residues, 111714330-111714451Exon3: 31 residues, 111750488-111750577Exon4: 6 residues, 111758678-111758690Exon5: 51 residues, 111769883-111770030Exon6: 45 residues, 111787601-111787731Exon7: 30 residues, 111788944-111789028Exon8: 57 residues, 111790617-111790783Exon9: 15 residues, 111791946-111791985Exon10: 51 residues, 111792080-111792227Exon11: 31 residues, 111797271-111797358Exon12: 23 residues, 111797866-111797929Exon13: 77 residues, 111798829-111799054Exon14: 28 residues, 111801306-111801386Exon15: 27 residues, 111803959-111804034Exon16: 38 residues, 111805480-111805590Exon17: 44 residues, 111809984-111810111Exon18: 21 residues, 111812211-111812268Exon19: 53 residues, 111813036-111813191Exon20: 29 residues, 111816765-111816847Exon21: 34 residues, 111817964-111818061Exon22: 744 residues, 111818837-111821065Exon23: 2 residues, -Jump to RP3A_HUMANExon1: 26 residues, 111714124-111714200Exon2: 42 residues, 111714330-111714451Exon3: 31 residues, 111750488-111750577Exon4: 51 residues, 111769883-111770030Exon5: 45 residues, 111787601-111787731Exon6: 30 residues, 111788944-111789028Exon7: 57 residues, 111790617-111790783Exon8: 15 residues, 111791946-111791985Exon9: 51 residues, 111792080-111792227Exon10: 31 residues, 111797271-111797358Exon11: 23 residues, 111797866-111797929Exon12: 77 residues, 111798829-111799054Exon13: 28 residues, 111801306-111801386Exon14: 27 residues, 111803959-111804034Exon15: 38 residues, 111805480-111805590Exon16: 44 residues, 111809984-111810111Exon17: 21 residues, 111812211-111812268Exon18: 53 residues, 111813036-111813191Exon19: 29 residues, 111816765-111816847Exon20: 34 residues, 111817964-111818061Exon21: 265 residues, 111818837-111819627Exon22: 2 residues, -Jump to RP3A_HUMAN  
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Loci Cluster (Details)Loci: 2790 111829121-111842094 ~-13K 9740(OAS1)(+)Loci: 2789 111714055-111821065 ~-107K 9738(RPH3A)(+)Link out to UCSC