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UniProtKB - Q02563 (SV2A_RAT)

Protein

Synaptic vesicle glycoprotein 2A

Gene

Sv2a

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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.
(Microbial infection) Receptor for C.botulinum neurotoxin type A (BoNT/A, botA); the toxin binds via extracellular loop 4 (PubMed:16543415). Restores uptake of BoNT/A in mouse cells that are deleted for SV2 receptor (PubMed:16543415, PubMed:18815274). Glycosylation of Asn-573 is not essential for receptor activity, but enhances uptake (PubMed:18815274, PubMed:19650874). Also serves as a receptor for the closely related C.botulinum neurotoxin type A2; glycosylation is not essential but enhances the interaction (PubMed:29649119).4 Publications
Possible receptor for C.botulinum neurotoxin type D (BoNT/D, botD); BoNT/D does not bind to extracellular loop 4 as do BoNT/A and BoNT/E, nor to loop 1 or loop 3 (PubMed:21483489). Another group does not find a convincing interaction with SV2 (PubMed:21632541).2 Publications
(Microbial infection) Receptor for C.botulinum neurotoxin type E (BoNT/E); the toxin probably binds via extracellular loop 4 and requires glycosylation of Asn-573 (PubMed:18815274, PubMed:19650874). Restores uptake of BoNT/E in mouse cells that are deleted for SV2 receptor (PubMed:18815274).2 Publications
(Microbial infection) Receptor for C.botulinum neurotoxin type F (BoNT/F) (PubMed:19476346, PubMed:19650874). Binding requires glycosylation of Asn-573 (PubMed:19476346).1 Publication1 Publication

Miscellaneous

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

Caution

The use of this protein as a coreceptor for C.botulinum type D (BoNT/D, botD) is controversial. In double SV2A/SV2B knockout mice BoNT/D does not degrade its synaptobrevin target; introducing SV2A, SV2B or SV2C restores target cleavage (PubMed:21483489). However another group does not find a convincing interaction with SV2 (PubMed:21632541).2 Publications

GO - Molecular functioni

  • protein kinase binding Source: Ensembl
  • transmembrane transporter activity Source: InterPro
  • transporter activity Source: RGD
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionReceptor
Biological processNeurotransmitter 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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi619715 Sv2a

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 169CytoplasmicSequence analysisAdd BLAST169
Transmembranei170 – 190HelicalSequence analysisAdd BLAST21
Topological domaini191 – 205ExtracellularSequence analysis1 PublicationAdd BLAST15
Transmembranei206 – 226HelicalSequence analysisAdd BLAST21
Topological domaini227 – 233CytoplasmicSequence analysis7
Transmembranei234 – 254HelicalSequence analysisAdd BLAST21
Topological domaini255 – 262ExtracellularSequence analysis8
Transmembranei263 – 283HelicalSequence analysisAdd BLAST21
Topological domaini284 – 294CytoplasmicSequence analysisAdd BLAST11
Transmembranei295 – 315HelicalSequence analysisAdd BLAST21
Topological domaini316 – 334ExtracellularSequence analysis1 PublicationAdd BLAST19
Transmembranei335 – 355HelicalSequence analysisAdd BLAST21
Topological domaini356 – 447CytoplasmicSequence analysisAdd BLAST92
Transmembranei448 – 468HelicalSequence analysisAdd BLAST21
Topological domaini469 – 598ExtracellularSequence analysis2 PublicationsAdd BLAST130
Transmembranei599 – 619HelicalSequence analysisAdd BLAST21
Topological domaini620 – 626CytoplasmicSequence analysis7
Transmembranei627 – 647HelicalSequence analysisAdd BLAST21
Topological domaini648 – 651ExtracellularSequence analysis4
Transmembranei652 – 672HelicalSequence analysisAdd BLAST21
Topological domaini673 – 685CytoplasmicSequence analysisAdd BLAST13
Transmembranei686 – 708HelicalSequence analysisAdd BLAST23
Topological domaini709 – 712ExtracellularSequence analysis4
Transmembranei713 – 731HelicalSequence analysisAdd BLAST19
Topological domaini732 – 742CytoplasmicSequence analysisAdd BLAST11

Keywords - Cellular componenti

Cell junction, Cytoplasmic vesicle, Membrane, Synapse

Pathology & Biotechi

Disruption phenotypei

Short hairpin-mediated RNA knockdown of the protein in PC12 cells leads to increased resistance to C.botulinum neurotoxin type A (BoNT/A, botA) as assayed by reduced SNAP25 cleavage; uptake and degradation are restored by expression of SV2B or SV2C (PubMed:16543415).1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi196 – 200Missing : No change in uptake of C.botulinum neurotoxin type D (BoNT/D, botD) or C.botulinum neurotoxin type E (BoNT/E). 1 Publication5
Mutagenesisi321 – 331Missing : No change in uptake of BoNT/D or BoNT/E. 1 PublicationAdd BLAST11
Mutagenesisi498N → Q: No change in uptake of BoNT/E or C.botulinum neurotoxin type A (BoNT/A, botA) by mouse SV2A/SV2B knockout neurons; SV2A apparent molecular weight decreases. No change in uptake of BoNT/E; when associated with Q-548. No change in uptake of BoNT/D. 2 Publications1
Mutagenesisi548N → Q: No change in uptake of BoNT/E or BoNT/A by mouse SV2A/SV2B knockout neurons; SV2A apparent molecular weight decreases. No change in uptake of BoNT/E; when associated with Q-498. No change in uptake of BoNT/D. 2 Publications1
Mutagenesisi570 – 573RLVN → TLVQ: Restores apparent molecular weight to wild-type, does not restore uptake of BoNT/E. 1 Publication4
Mutagenesisi573N → Q: BoNT/E not taken up by mouse SV2A/SV2B knockout neurons, decreased uptake of BoNT/A; SV2A apparent molecular weight decreases. No change in uptake of BoNT/D. 2 Publications1

Chemistry databases

ChEMBLiCHEMBL4381
GuidetoPHARMACOLOGYi2634

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000848821 – 742Synaptic vesicle glycoprotein 2AAdd BLAST742

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei80PhosphoserineBy similarity1
Modified residuei81PhosphoserineBy similarity1
Modified residuei84PhosphothreonineBy similarity1
Modified residuei127PhosphoserineCombined sources1
Modified residuei393PhosphoserineCombined sources1
Modified residuei480PhosphotyrosineBy similarity1
Glycosylationi498N-linked (GlcNAc...) asparagineSequence analysis1 Publication1
Glycosylationi548N-linked (GlcNAc...) asparagineSequence analysis1 Publication1
Glycosylationi573N-linked (GlcNAc...) asparagine; alternateSequence analysis1 Publication1
Glycosylationi573N-linked (HexNAc...) asparagine; alternateCombined sources1

Post-translational modificationi

Phosphorylation by CK1 of the N-terminal cytoplasmic domain regulates interaction with SYT1.1 Publication
N-glycosylated, on at least 3 residues.3 Publications1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ02563
PRIDEiQ02563

PTM databases

iPTMnetiQ02563
PhosphoSitePlusiQ02563
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

BgeeiENSRNOG00000021182 Expressed in 10 organ(s), highest expression level in brain
GenevisibleiQ02563 RN

Interactioni

Subunit structurei

Interacts with SYT1/synaptotagmin-1 in a calcium-dependent manner. Binds the adapter protein complex AP-2.4 Publications
(Microbial infection) Interacts with C.botulinum neurotoxin type A1 and type A2 (BoNT/A, botA) (PubMed:16543415, PubMed:19650874, PubMed:21632541, PubMed:21483489, PubMed:29649119). Interaction is improved by glycosylation of SV2 (PubMed:29649119).5 Publications
(Microbial infection) Copurifies with C.botulinum neurotoxin type B (BoNT/B, botB) and synaptotagmin 1 (SYT1) (PubMed:19476346). Interaction does not require glycosylation of SV2 or SYT1 proteins (PubMed:19476346). Another group finds only copurification with SYT1 and SYT2 (PubMed:19650874).2 Publications
(Microbial infection) Interacts with C.botulinum neurotoxin type E (BoNT/E) (PubMed:18815274, PubMed:19476346, PubMed:19650874). Interaction requires glycosylation of SV2 proteins (PubMed:18815274, PubMed:19476346, PubMed:19650874).3 Publications
(Microbial infection) Copurifies with C.botulinum neurotoxin type F (BoNT/F) and synaptotagmin 1 (SYT2) (PubMed:19476346). Another group finds only copurification with BoNT/F (PubMed:19650874). Interaction requires SV2 glycosylation (PubMed:19476346).2 Publications

Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi250772, 1 interactor
IntActiQ02563, 6 interactors
MINTiQ02563
STRINGi10116.ENSRNOP00000028760

Chemistry databases

BindingDBiQ02563

Structurei

3D structure databases

ProteinModelPortaliQ02563
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 57Interaction with SYT1Add BLAST57

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
OMAiMMMAVWF
OrthoDBiEOG091G02NC
PhylomeDBiQ02563
TreeFamiTF324824

Family and domain databases

CDDicd06174 MFS, 2 hits
InterProiView protein in InterPro
IPR001646 5peptide_repeat
IPR011701 MFS
IPR020846 MFS_dom
IPR005828 MFS_sugar_transport-like
IPR036259 MFS_trans_sf
IPR005829 Sugar_transporter_CS
IPR022308 SV2
PfamiView protein in Pfam
PF07690 MFS_1, 1 hit
PF13599 Pentapeptide_4, 1 hit
PF00083 Sugar_tr, 1 hit
SUPFAMiSSF103473 SSF103473, 2 hits
TIGRFAMsiTIGR01299 synapt_SV2, 1 hit
PROSITEiView protein in PROSITE
PS50850 MFS, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti340C → F in AAA42188 (PubMed:1355409).Curated1

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_006232952.3
UniGeneiRn.11264

Genome annotation databases

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

Similar proteinsi

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_006232952.3
UniGeneiRn.11264

3D structure databases

ProteinModelPortaliQ02563
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250772, 1 interactor
IntActiQ02563, 6 interactors
MINTiQ02563
STRINGi10116.ENSRNOP00000028760

Chemistry databases

BindingDBiQ02563
ChEMBLiCHEMBL4381
GuidetoPHARMACOLOGYi2634

Protein family/group databases

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

PTM databases

iPTMnetiQ02563
PhosphoSitePlusiQ02563
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
OMAiMMMAVWF
OrthoDBiEOG091G02NC
PhylomeDBiQ02563
TreeFamiTF324824

Miscellaneous databases

PROiPR:Q02563

Gene expression databases

BgeeiENSRNOG00000021182 Expressed in 10 organ(s), highest expression level in brain
GenevisibleiQ02563 RN

Family and domain databases

CDDicd06174 MFS, 2 hits
InterProiView protein in InterPro
IPR001646 5peptide_repeat
IPR011701 MFS
IPR020846 MFS_dom
IPR005828 MFS_sugar_transport-like
IPR036259 MFS_trans_sf
IPR005829 Sugar_transporter_CS
IPR022308 SV2
PfamiView protein in Pfam
PF07690 MFS_1, 1 hit
PF13599 Pentapeptide_4, 1 hit
PF00083 Sugar_tr, 1 hit
SUPFAMiSSF103473 SSF103473, 2 hits
TIGRFAMsiTIGR01299 synapt_SV2, 1 hit
PROSITEiView protein in PROSITE
PS50850 MFS, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiSV2A_RAT
AccessioniPrimary (citable) accession number: Q02563
Secondary accession number(s): Q58DZ8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: June 13, 2006
Last modified: November 7, 2018
This is version 142 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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