Q7L0J3 · SV2A_HUMAN

  • Protein
    Synaptic vesicle glycoprotein 2A
  • Gene
    SV2A
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Plays a role in the control of regulated secretion in neural and endocrine cells, enhancing selectively low-frequency neurotransmission. Positively regulates vesicle fusion by maintaining the readily releasable pool of secretory vesicles (By similarity).
(Microbial infection) Receptor for the C.botulinum neurotoxin type A2 (BoNT/A, botA); glycosylation is not essential but enhances the interaction (PubMed:29649119).
Probably also serves as a receptor for the closely related C.botulinum neurotoxin type A1

Miscellaneous

Identified as the brain binding-site for the antiepileptic drug levetiracetam/lev.

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 Componentcell-cell junction
Cellular Componentdendrite
Cellular Componentendoplasmic reticulum
Cellular ComponentGABA-ergic synapse
Cellular Componentglutamatergic synapse
Cellular Componentneuromuscular junction
Cellular Componentneuron projection
Cellular Componentneuronal cell body
Cellular Componentplasma membrane
Cellular Componentpresynaptic active zone
Cellular Componentsynaptic vesicle
Cellular Componentsynaptic vesicle membrane
Molecular Functionprotein kinase binding
Molecular Functiontransmembrane transporter activity
Biological Processintracellular calcium ion homeostasis
Biological Processregulation of gamma-aminobutyric acid secretion
Biological Processsynaptic vesicle priming

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Synaptic vesicle glycoprotein 2A

Gene names

    • Name
      SV2A
    • Synonyms
      KIAA0736
    • ORF names
      PSEC0174

Organism names

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

Accessions

  • Primary accession
    Q7L0J3
  • Secondary accessions
    • D3DUZ7
    • O94841
    • Q5QNX8
    • Q7Z3L6
    • Q8NBJ6
    • Q9BVZ9

Proteomes

Organism-specific databases

Subcellular Location

Presynapse
Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane
; Multi-pass membrane protein
Note: Enriched in chromaffin granules, not present in adrenal microsomes. Associated with both insulin granules and synaptic-like microvesicles in insulin-secreting cells of the pancreas (By similarity).
Colocalizes with ATP2B1 at photoreceptor synaptic terminals

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-169Cytoplasmic
Transmembrane170-190Helical
Topological domain191-205Extracellular
Transmembrane206-226Helical
Topological domain227-233Cytoplasmic
Transmembrane234-254Helical
Topological domain255-262Extracellular
Transmembrane263-283Helical
Topological domain284-294Cytoplasmic
Transmembrane295-315Helical
Topological domain316-334Extracellular
Transmembrane335-355Helical
Topological domain356-447Cytoplasmic
Transmembrane448-468Helical
Topological domain469-598Extracellular
Transmembrane599-619Helical
Topological domain620-626Cytoplasmic
Transmembrane627-647Helical
Topological domain648-651Extracellular
Transmembrane652-672Helical
Topological domain673-685Cytoplasmic
Transmembrane686-708Helical
Topological domain709-712Extracellular
Transmembrane713-731Helical
Topological domain732-742Cytoplasmic

Keywords

Disease & Variants

Involvement in disease

Developmental and epileptic encephalopathy 113 (DEE113)

  • Note
    • The disease may be caused by variants affecting the gene represented in this entry
  • Description
    A form of epileptic encephalopathy, a heterogeneous group of early-onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. DEE113 is an autosomal recessive form characterized by severe early-onset recurrent epilepsy.
  • See also
    MIM:620772
Natural variants in DEE113
Variant IDPosition(s)ChangeDescription
VAR_089450289-742missingin DEE113; likely pathogenic
VAR_089451383R>Qin DEE113; uncertain significance

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_089450289-742in DEE113; likely pathogenic
Natural variantVAR_089451383in DEE113; uncertain significance

Variants

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

The viewer provides 743 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

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

TypeIDPosition(s)SourceDescription
ChainPRO_00002397641-742UniProtSynaptic vesicle glycoprotein 2A
Modified residue80UniProtPhosphoserine
Modified residue81UniProtPhosphoserine
Modified residue84UniProtPhosphothreonine
Modified residue127UniProtPhosphoserine
Modified residue (large scale data)127PRIDEPhosphoserine
Modified residue393UniProtPhosphoserine
Modified residue480UniProtPhosphotyrosine
Glycosylation498UniProtN-linked (GlcNAc...) asparagine
Glycosylation548UniProtN-linked (GlcNAc...) asparagine
Glycosylation573UniProtN-linked (GlcNAc...) asparagine

Post-translational modification

Phosphorylation by CK1 of the N-terminal cytoplasmic domain regulates interaction with SYT1.
N-glycosylated.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with SYT1/synaptotagmin-1 in a calcium-dependent manner. Binds the adapter protein complex AP-2 (By similarity).
(Microbial infection) Interacts with C.botulinum neurotoxin type A2 (BoNT/A, botA) (PubMed:29649119).
Interaction is improved by glycosylation of SV2 (PubMed:29649119).

Protein-protein interaction databases

Chemistry

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region1-57Interaction with SYT1
Compositional bias33-50Basic and acidic residues
Region33-144Disordered
Compositional bias68-84Basic and acidic residues

Sequence similarities

Belongs to the major facilitator superfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q7L0J3-1

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
    742
  • Mass (Da)
    82,695
  • Last updated
    2004-07-05 v1
  • Checksum
    913E216D5CFC2FB2
MEEGFRDRAAFIRGAKDIAKEVKKHAAKKVVKGLDRVQDEYSRRSYSRFEEEDDDDDFPAPSDGYYRGEGTQDEEEGGASSDATEGHDEDDEIYEGEYQGIPRAESGGKGERMADGAPLAGVRGGLSDGEGPPGGRGEAQRRKEREELAQQYEAILRECGHGRFQWTLYFVLGLALMADGVEVFVVGFVLPSAEKDMCLSDSNKGMLGLIVYLGMMVGAFLWGGLADRLGRRQCLLISLSVNSVFAFFSSFVQGYGTFLFCRLLSGVGIGGSIPIVFSYFSEFLAQEKRGEHLSWLCMFWMIGGVYAAAMAWAIIPHYGWSFQMGSAYQFHSWRVFVLVCAFPSVFAIGALTTQPESPRFFLENGKHDEAWMVLKQVHDTNMRAKGHPERVFSVTHIKTIHQEDELIEIQSDTGTWYQRWGVRALSLGGQVWGNFLSCFGPEYRRITLMMMGVWFTMSFSYYGLTVWFPDMIRHLQAVDYASRTKVFPGERVEHVTFNFTLENQIHRGGQYFNDKFIGLRLKSVSFEDSLFEECYFEDVTSSNTFFRNCTFINTVFYNTDLFEYKFVNSRLINSTFLHNKEGCPLDVTGTGEGAYMVYFVSFLGTLAVLPGNIVSALLMDKIGRLRMLAGSSVMSCVSCFFLSFGNSESAMIALLCLFGGVSIASWNALDVLTVELYPSDKRTTAFGFLNALCKLAAVLGISIFTSFVGITKAAPILFASAALALGSSLALKLPETRGQVLQ

Q7L0J3-2

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

Sequence caution

The sequence BAA34456.2 differs from that shown. Reason: Erroneous initiation Extended N-terminus.
The sequence CAI12573.1 differs from that shown. Reason: Erroneous gene model prediction

Features

Showing features for compositional bias, sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Compositional bias33-50Basic and acidic residues
Compositional bias68-84Basic and acidic residues
Sequence conflict100in Ref. 4; CAD97824
Sequence conflict404in Ref. 3; BAC11645
Sequence conflict493in Ref. 4; CAD97824
Sequence conflict524in Ref. 3; BAC11645
Sequence conflict544in Ref. 3; BAC11645
Sequence conflict582in Ref. 3; BAC11645
Sequence conflict611in Ref. 3; BAC11645
Alternative sequenceVSP_019265683-742in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB018279
EMBL· GenBank· DDBJ
BAA34456.2
EMBL· GenBank· DDBJ
mRNA Different initiation
AK075480
EMBL· GenBank· DDBJ
BAC11645.1
EMBL· GenBank· DDBJ
mRNA
BX537754
EMBL· GenBank· DDBJ
CAD97824.1
EMBL· GenBank· DDBJ
mRNA
AL591493
EMBL· GenBank· DDBJ
CAI12572.1
EMBL· GenBank· DDBJ
Genomic DNA
AL591493
EMBL· GenBank· DDBJ
CAI12573.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
CH471121
EMBL· GenBank· DDBJ
EAW53596.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471121
EMBL· GenBank· DDBJ
EAW53598.1
EMBL· GenBank· DDBJ
Genomic DNA
BC000776
EMBL· GenBank· DDBJ
AAH00776.2
EMBL· GenBank· DDBJ
mRNA
BC045111
EMBL· GenBank· DDBJ
AAH45111.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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