Q9Y2J0 · RP3A_HUMAN

  • Protein
    Rabphilin-3A
  • Gene
    RPH3A
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

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. Also plays a role in the exocytosis of arginine vasopressin hormone (By similarity).

Cofactor

Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Features

Showing features for binding site.

169450100150200250300350400450500550600650
TypeIDPosition(s)Description
Binding site98Zn2+ 1 (UniProtKB | ChEBI)
Binding site101Zn2+ 1 (UniProtKB | ChEBI)
Binding site115Zn2+ 2 (UniProtKB | ChEBI)
Binding site118Zn2+ 2 (UniProtKB | ChEBI)
Binding site123Zn2+ 1 (UniProtKB | ChEBI)
Binding site126Zn2+ 1 (UniProtKB | ChEBI)
Binding site140Zn2+ 2 (UniProtKB | ChEBI)
Binding site143Zn2+ 2 (UniProtKB | ChEBI)
Binding site422Ca2+ 1 (UniProtKB | ChEBI)
Binding site423Ca2+ 1 (UniProtKB | ChEBI)
Binding site423Ca2+ 2 (UniProtKB | ChEBI)
Binding site429Ca2+ 2 (UniProtKB | ChEBI)
Binding site484Ca2+ 1 (UniProtKB | ChEBI)
Binding site484Ca2+ 2 (UniProtKB | ChEBI)
Binding site485Ca2+ 2 (UniProtKB | ChEBI)
Binding site486Ca2+ 1 (UniProtKB | ChEBI)
Binding site486Ca2+ 2 (UniProtKB | ChEBI)
Binding site492Ca2+ 1 (UniProtKB | ChEBI)
Binding site539Ca2+ 3 (UniProtKB | ChEBI)
Binding site581Ca2+ 3 (UniProtKB | ChEBI)
Binding site581Ca2+ 4 (UniProtKB | ChEBI)
Binding site587Ca2+ 3 (UniProtKB | ChEBI)
Binding site641Ca2+ 3 (UniProtKB | ChEBI)
Binding site641Ca2+ 4 (UniProtKB | ChEBI)
Binding site642Ca2+ 3 (UniProtKB | ChEBI)
Binding site643Ca2+ 3 (UniProtKB | ChEBI)
Binding site643Ca2+ 4 (UniProtKB | ChEBI)
Binding site649Ca2+ 4 (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytosol
Cellular Componentdendritic spine
Cellular Componentextrinsic component of membrane
Cellular Componentextrinsic component of synaptic vesicle membrane
Cellular Componentneuron projection
Cellular Componentpostsynaptic membrane
Cellular Componentprotein-containing complex
Cellular Componentsecretory granule
Cellular Componentsynapse
Cellular Componentsynaptic vesicle
Cellular Componentsynaptic vesicle membrane
Molecular Functioncalcium ion binding
Molecular Functioncalcium-dependent phospholipid binding
Molecular Functioninositol 1,4,5 trisphosphate binding
Molecular Functionphosphate ion binding
Molecular Functionphosphatidylinositol phosphate binding
Molecular Functionphosphatidylinositol-4,5-bisphosphate binding
Molecular Functionprotein-containing complex binding
Molecular Functionselenium binding
Molecular Functionsmall GTPase binding
Molecular Functionzinc ion binding
Biological Processexocytosis
Biological Processintracellular protein transport
Biological Processregulation of calcium ion-dependent exocytosis
Biological Processspontaneous neurotransmitter secretion
Biological Processsynaptic vesicle priming

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Rabphilin-3A
  • Alternative names
    • Exophilin-1

Gene names

    • Name
      RPH3A
    • Synonyms
      KIAA0985

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q9Y2J0
  • Secondary accessions
    • B7Z3C3
    • Q96AE0

Proteomes

Organism-specific databases

Disease & Variants

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 933 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
ChainPRO_00001902271-694UniProtRabphilin-3A
Modified residue226UniProtOmega-N-methylarginine
Modified residue (large scale data)263PRIDEPhosphoserine
Modified residue272UniProtPhosphoserine
Modified residue (large scale data)272PRIDEPhosphoserine
Modified residue692UniProtPhosphoserine
Modified residue (large scale data)692PRIDEPhosphoserine
Modified residue693UniProtPhosphoserine
Modified residue (large scale data)693PRIDEPhosphoserine

Post-translational modification

Ubiquitinated. Deubiquitinated by CAND1 to prevent its degradation.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with RAB3B, RAB3C, RAB3D, RAB8A, RAB27A and RAB27B (By similarity).
Interacts with RAB3A; this interaction recruits RPH3A to synaptic vesicules (PubMed:15207266).
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 (PubMed:15207266).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q9Y2J0CASK O149363EBI-1216802, EBI-1215506
BINARY Q9Y2J0-2RAB27B O001943EBI-16808141, EBI-10179046

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for compositional bias, region, domain, zinc finger.

TypeIDPosition(s)Description
Compositional bias1-30Polar residues
Region1-51Disordered
Domain44-160RabBD
Zinc finger92-148FYVE-type
Region166-388Disordered
Compositional bias183-197Pro residues
Compositional bias198-214Basic and acidic residues
Compositional bias265-281Polar residues
Compositional bias282-301Pro residues
Domain392-514C2 1
Domain550-683C2 2

Domain

Binds calcium via the C2 domains. The calcium-bound C2 domains mediate interactions with phospholipid bilayers (By similarity).

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q9Y2J0-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    694
  • Mass (Da)
    76,872
  • Last updated
    1999-11-01 v1
  • Checksum
    BD9C43F306A04D69
MTDTVFSNSSNRWMYPSDRPLQSNDKEQLQAGWSVHPGGQPDRQRKQEELTDEEKEIINRVIARAEKMEEMEQERIGRLVDRLENMRKNVAGDGVNRCILCGEQLGMLGSACVVCEDCKKNVCTKCGVETNNRLHSVWLCKICIEQREVWKRSGAWFFKGFPKQVLPQPMPIKKTKPQQPVSEPAAPEQPAPEPKHPARAPARGDSEDRRGPGQKTGPDPASAPGRGNYGPPVRRASEARMSSSSRDSESWDHSGGAGDSSRSPAGLRRANSVQASRPAPGSVQSPAPPQPGQPGTPGGSRPGPGPAGRFPDQKPEVAPSDPGTTAPPREERTGGVGGYPAVGAREDRMSHPSGPYSQASAAAPQPAAARQPPPPEEEEEEANSYDSDEATTLGALEFSLLYDQDNSSLQCTIIKAKGLKPMDSNGLADPYVKLHLLPGASKSNKLRTKTLRNTRNPIWNETLVYHGITDEDMQRKTLRISVCDEDKFGHNEFIGETRFSLKKLKPNQRKNFNICLERVIPMKRAGTTGSARGMALYEEEQVERVGDIEERGKILVSLMYSTQQGGLIVGIIRCVHLAAMDANGYSDPFVKLWLKPDMGKKAKHKTQIKKKTLNPEFNEEFFYDIKHSDLAKKSLDISVWDYDIGKSNDYIGGCQLGISAKGERLKHWYECLKNKDKKIERWHQLQNENHVSSD

Q9Y2J0-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 15 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
F8VZS2F8VZS2_HUMANRPH3A94
F8VVK8F8VVK8_HUMANRPH3A163
F8VV58F8VV58_HUMANRPH3A120
F8VTR7F8VTR7_HUMANRPH3A80
F8VR41F8VR41_HUMANRPH3A104
F8VRJ1F8VRJ1_HUMANRPH3A60
F8W116F8W116_HUMANRPH3A39
F8VP47F8VP47_HUMANRPH3A645
F8W131F8W131_HUMANRPH3A115
F8W1A3F8W1A3_HUMANRPH3A125
F8W1K7F8W1K7_HUMANRPH3A181
F8VNU2F8VNU2_HUMANRPH3A83
F8W045F8W045_HUMANRPH3A12
F8VNP7F8VNP7_HUMANRPH3A133
F8VNW3F8VNW3_HUMANRPH3A127

Sequence caution

The sequence BAA76829.2 differs from that shown. Reason: Erroneous initiation

Features

Showing features for compositional bias, alternative sequence.

TypeIDPosition(s)Description
Compositional bias1-30Polar residues
Alternative sequenceVSP_02101624-28in isoform 2
Compositional bias183-197Pro residues
Compositional bias198-214Basic and acidic residues
Compositional bias265-281Polar residues
Compositional bias282-301Pro residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB023202
EMBL· GenBank· DDBJ
BAA76829.2
EMBL· GenBank· DDBJ
mRNA Different initiation
AK295696
EMBL· GenBank· DDBJ
BAH12159.1
EMBL· GenBank· DDBJ
mRNA
BC017259
EMBL· GenBank· DDBJ
AAH17259.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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