Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Synaptic vesicle glycoprotein 2A

Gene

Sv2a

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.
Receptor for the botulinium neurotoxin type A/BOTA.

GO - Molecular functioni

  • receptor activity Source: Ensembl
  • transmembrane transporter activity Source: InterPro
  • transporter activity Source: RGD

GO - Biological processi

  • cellular calcium ion homeostasis Source: Ensembl
  • neurotransmitter transport Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Neurotransmitter transport, Transport

Protein family/group databases

TCDBi2.A.1.22.1. the major facilitator superfamily (mfs).

Names & Taxonomyi

Protein namesi
Recommended name:
Synaptic vesicle glycoprotein 2A
Short name:
Synaptic vesicle protein 2
Short name:
Synaptic vesicle protein 2A
Gene namesi
Name:Sv2a
Synonyms:Sv2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi619715. Sv2a.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 169169CytoplasmicSequence analysisAdd
BLAST
Transmembranei170 – 19021HelicalSequence analysisAdd
BLAST
Topological domaini191 – 20515ExtracellularSequence analysisAdd
BLAST
Transmembranei206 – 22621HelicalSequence analysisAdd
BLAST
Topological domaini227 – 2337CytoplasmicSequence analysis
Transmembranei234 – 25421HelicalSequence analysisAdd
BLAST
Topological domaini255 – 2628ExtracellularSequence analysis
Transmembranei263 – 28321HelicalSequence analysisAdd
BLAST
Topological domaini284 – 29411CytoplasmicSequence analysisAdd
BLAST
Transmembranei295 – 31521HelicalSequence analysisAdd
BLAST
Topological domaini316 – 33419ExtracellularSequence analysisAdd
BLAST
Transmembranei335 – 35521HelicalSequence analysisAdd
BLAST
Topological domaini356 – 44792CytoplasmicSequence analysisAdd
BLAST
Transmembranei448 – 46821HelicalSequence analysisAdd
BLAST
Topological domaini469 – 598130ExtracellularSequence analysisAdd
BLAST
Transmembranei599 – 61921HelicalSequence analysisAdd
BLAST
Topological domaini620 – 6267CytoplasmicSequence analysis
Transmembranei627 – 64721HelicalSequence analysisAdd
BLAST
Topological domaini648 – 6514ExtracellularSequence analysis
Transmembranei652 – 67221HelicalSequence analysisAdd
BLAST
Topological domaini673 – 68513CytoplasmicSequence analysisAdd
BLAST
Transmembranei686 – 70823HelicalSequence analysisAdd
BLAST
Topological domaini709 – 7124ExtracellularSequence analysis
Transmembranei713 – 73119HelicalSequence analysisAdd
BLAST
Topological domaini732 – 74211CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell-cell junction Source: Ensembl
  • endoplasmic reticulum Source: Ensembl
  • integral component of membrane Source: RGD
  • neuromuscular junction Source: Ensembl
  • presynaptic active zone Source: Ensembl
  • synapse Source: MGI
  • synaptic vesicle membrane Source: RGD
  • terminal bouton Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasmic vesicle, Membrane, Synapse

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL4381.
GuidetoPHARMACOLOGYi2634.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 742742Synaptic vesicle glycoprotein 2APRO_0000084882Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei80 – 801PhosphoserineBy similarity
Modified residuei81 – 811PhosphoserineBy similarity
Modified residuei84 – 841PhosphothreonineBy similarity
Modified residuei127 – 1271PhosphoserineCombined sources
Modified residuei393 – 3931PhosphoserineCombined sources
Modified residuei480 – 4801PhosphotyrosineBy similarity
Glycosylationi498 – 4981N-linked (GlcNAc...)Sequence analysis
Glycosylationi548 – 5481N-linked (GlcNAc...)Sequence analysis
Glycosylationi573 – 5731N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Phosphorylation by CK1 of the N-terminal cytoplasmic domain regulates interaction with SYT1.1 Publication
N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ02563.
PRIDEiQ02563.

PTM databases

iPTMnetiQ02563.
PhosphoSiteiQ02563.
SwissPalmiQ02563.
UniCarbKBiQ02563.

Expressioni

Tissue specificityi

Widely expressed throughout the brain (at protein level). Expressed by neural and endocrine cells of brain and spinal cord.1 Publication

Gene expression databases

GenevisibleiQ02563. RN.

Interactioni

Subunit structurei

Interacts with SYT1/synaptotagmin-1 in a calcium-dependent manner. Binds the adapter protein complex AP-2.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
botAP108452EBI-466194,EBI-8178893From a different organism.
Syt1P217072EBI-466194,EBI-458098

Protein-protein interaction databases

BioGridi250772. 1 interaction.
IntActiQ02563. 6 interactions.
MINTiMINT-87493.
STRINGi10116.ENSRNOP00000028760.

Chemistry

BindingDBiQ02563.

Structurei

3D structure databases

ProteinModelPortaliQ02563.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 5757Interaction with SYT1Add
BLAST
Regioni543 – 58038BOTA-bindingBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the major facilitator superfamily.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IRID. Eukaryota.
ENOG410YQME. LUCA.
GeneTreeiENSGT00550000074384.
HOGENOMiHOG000065727.
HOVERGENiHBG053967.
InParanoidiQ02563.
KOiK06258.
OMAiMSCISCF.
OrthoDBiEOG74TWZ1.
PhylomeDBiQ02563.
TreeFamiTF324824.

Family and domain databases

InterProiIPR001646. 5peptide_repeat.
IPR011701. MFS.
IPR020846. MFS_dom.
IPR005828. MFS_sugar_transport_like.
IPR005829. Sugar_transporter_CS.
IPR022308. SV2.
[Graphical view]
PfamiPF07690. MFS_1. 1 hit.
PF13599. Pentapeptide_4. 1 hit.
PF00083. Sugar_tr. 1 hit.
[Graphical view]
SUPFAMiSSF103473. SSF103473. 3 hits.
TIGRFAMsiTIGR01299. synapt_SV2. 1 hit.
PROSITEiPS50850. MFS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q02563-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEGFRDRAA FIRGAKDIAK EVKKHAAKKV VKGLDRVQDE YSRRSYSRFE
60 70 80 90 100
EEEDDDDFPA PADGYYRGEG AQDEEEGGAS SDATEGHDED DEIYEGEYQG
110 120 130 140 150
IPRAESGGKG ERMADGAPLA GVRGGLSDGE GPPGGRGEAQ RRKDREELAQ
160 170 180 190 200
QYETILRECG HGRFQWTLYF VLGLALMADG VEVFVVGFVL PSAEKDMCLS
210 220 230 240 250
DSNKGMLGLI VYLGMMVGAF LWGGLADRLG RRQCLLISLS VNSVFAFFSS
260 270 280 290 300
FVQGYGTFLF CRLLSGVGIG GSIPIVFSYF SEFLAQEKRG EHLSWLCMFW
310 320 330 340 350
MIGGVYAAAM AWAIIPHYGW SFQMGSAYQF HSWRVFVLVC AFPSVFAIGA
360 370 380 390 400
LTTQPESPRF FLENGKHDEA WMVLKQVHDT NMRAKGHPER VFSVTHIKTI
410 420 430 440 450
HQEDELIEIQ SDTGTWYQRW GVRALSLGGQ VWGNFLSCFS PEYRRITLMM
460 470 480 490 500
MGVWFTMSFS YYGLTVWFPD MIRHLQAVDY AARTKVFPGE RVEHVTFNFT
510 520 530 540 550
LENQIHRGGQ YFNDKFIGLR LKSVSFEDSL FEECYFEDVT SSNTFFRNCT
560 570 580 590 600
FINTVFYNTD LFEYKFVNSR LVNSTFLHNK EGCPLDVTGT GEGAYMVYFV
610 620 630 640 650
SFLGTLAVLP GNIVSALLMD KIGRLRMLAG SSVLSCVSCF FLSFGNSESA
660 670 680 690 700
MIALLCLFGG VSIASWNALD VLTVELYPSD KRTTAFGFLN ALCKLAAVLG
710 720 730 740
ISIFTSFVGI TKAAPILFAS AALALGSSLA LKLPETRGQV LQ
Length:742
Mass (Da):82,661
Last modified:June 13, 2006 - v2
Checksum:iE10FC62BEEFE316A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti340 – 3401C → F in AAA42188 (PubMed:1355409).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01788 Genomic RNA. No translation available.
L05435 mRNA. Translation: AAA42188.1.
BC092132 mRNA. Translation: AAH92132.1.
PIRiA43344.
RefSeqiNP_476558.2. NM_057210.2.
XP_006233014.1. XM_006232952.2.
UniGeneiRn.11264.

Genome annotation databases

EnsembliENSRNOT00000028760; ENSRNOP00000028760; ENSRNOG00000021182.
GeneIDi117559.
KEGGirno:117559.
UCSCiRGD:619715. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01788 Genomic RNA. No translation available.
L05435 mRNA. Translation: AAA42188.1.
BC092132 mRNA. Translation: AAH92132.1.
PIRiA43344.
RefSeqiNP_476558.2. NM_057210.2.
XP_006233014.1. XM_006232952.2.
UniGeneiRn.11264.

3D structure databases

ProteinModelPortaliQ02563.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250772. 1 interaction.
IntActiQ02563. 6 interactions.
MINTiMINT-87493.
STRINGi10116.ENSRNOP00000028760.

Chemistry

BindingDBiQ02563.
ChEMBLiCHEMBL4381.
GuidetoPHARMACOLOGYi2634.

Protein family/group databases

TCDBi2.A.1.22.1. the major facilitator superfamily (mfs).

PTM databases

iPTMnetiQ02563.
PhosphoSiteiQ02563.
SwissPalmiQ02563.
UniCarbKBiQ02563.

Proteomic databases

PaxDbiQ02563.
PRIDEiQ02563.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000028760; ENSRNOP00000028760; ENSRNOG00000021182.
GeneIDi117559.
KEGGirno:117559.
UCSCiRGD:619715. rat.

Organism-specific databases

CTDi9900.
RGDi619715. Sv2a.

Phylogenomic databases

eggNOGiENOG410IRID. Eukaryota.
ENOG410YQME. LUCA.
GeneTreeiENSGT00550000074384.
HOGENOMiHOG000065727.
HOVERGENiHBG053967.
InParanoidiQ02563.
KOiK06258.
OMAiMSCISCF.
OrthoDBiEOG74TWZ1.
PhylomeDBiQ02563.
TreeFamiTF324824.

Miscellaneous databases

NextBioi620423.
PROiQ02563.

Gene expression databases

GenevisibleiQ02563. RN.

Family and domain databases

InterProiIPR001646. 5peptide_repeat.
IPR011701. MFS.
IPR020846. MFS_dom.
IPR005828. MFS_sugar_transport_like.
IPR005829. Sugar_transporter_CS.
IPR022308. SV2.
[Graphical view]
PfamiPF07690. MFS_1. 1 hit.
PF13599. Pentapeptide_4. 1 hit.
PF00083. Sugar_tr. 1 hit.
[Graphical view]
SUPFAMiSSF103473. SSF103473. 3 hits.
TIGRFAMsiTIGR01299. synapt_SV2. 1 hit.
PROSITEiPS50850. MFS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The synaptic vesicle protein SV2 is a novel type of transmembrane transporter."
    Feany M.B., Lee S., Edwards R.H., Buckley K.M.
    Cell 70:861-867(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA], GLYCOSYLATION.
  2. "Identification, characterization, and molecular cloning of a novel transporter-like protein localized to the central nervous system."
    Gingrich J.A., Andersen P.H., Tiberi M., el Mestikawy S., Jorgensen P.N., Fremeau R.T. Jr., Caron M.G.
    FEBS Lett. 312:115-122(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 177-194 AND 372-381, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  3. "SV2, a brain synaptic vesicle protein homologous to bacterial transporters."
    Bajjalieh S.M., Peterson K., Shingal R., Scheller R.H.
    Science 257:1271-1273(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-40.
    Tissue: Brain.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. "Isoform-specific, calcium-regulated interaction of the synaptic vesicle proteins SV2 and synaptotagmin."
    Schivell A.E., Batchelor R.H., Bajjalieh S.M.
    J. Biol. Chem. 271:27770-27775(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SYT1.
  6. "SV2C is a synaptic vesicle protein with an unusually restricted localization: anatomy of a synaptic vesicle protein family."
    Janz R., Suedhof T.C.
    Neuroscience 94:1279-1290(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "AP-2 recruitment to synaptotagmin stimulated by tyrosine-based endocytic motifs."
    Haucke V., De Camilli P.
    Science 285:1268-1271(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AP-2.
  8. "Phosphorylation of synaptic vesicle protein 2 modulates binding to synaptotagmin."
    Pyle R.A., Schivell A.E., Hidaka H., Bajjalieh S.M.
    J. Biol. Chem. 275:17195-17200(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CK1, INTERACTION WITH SYT1.
  9. "The synaptic vesicle protein SV2A is the binding site for the antiepileptic drug levetiracetam."
    Lynch B.A., Lambeng N., Nocka K., Kensel-Hammes P., Bajjalieh S.M., Matagne A., Fuks B.
    Proc. Natl. Acad. Sci. U.S.A. 101:9861-9866(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION AS BINDING-SITE FOR ANTIEPILEPTIC DRUG LEVETIRACETAM.
  10. "SV2A and SV2C are not vesicular Ca2+ transporters but control glucose-evoked granule recruitment."
    Iezzi M., Theander S., Janz R., Loze C., Wollheim C.B.
    J. Cell Sci. 118:5647-5660(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  11. Cited for: FUNCTION, INTERACTION WITH SYT1.
  12. "SV2 is the protein receptor for botulinum neurotoxin A."
    Dong M., Yeh F., Tepp W.H., Dean C., Johnson E.A., Janz R., Chapman E.R.
    Science 312:592-596(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A BOTA RECEPTOR.
  13. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-393, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSV2A_RAT
AccessioniPrimary (citable) accession number: Q02563
Secondary accession number(s): Q58DZ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: June 13, 2006
Last modified: February 17, 2016
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.