Synaptic vesicle glycoprotein 2A - Rattus norvegicus (Rat)

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Q02563 (SV2A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 88. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Synaptic vesicle glycoprotein 2A
Short name=Synaptic vesicle protein 2
Short name=Synaptic vesicle protein 2A

Gene names

Name:	Sv2a
Synonyms:	Sv2

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	742 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.10 Ref.11 Ref.12 Receptor for the botulinium neurotoxin type A/BOTA. Ref.10 Ref.11 Ref.12
Subunit structure	Interacts with SYT1/synaptotagmin-1 in a calcium-dependent manner. Binds the adapter protein complex AP-2. Ref.5 Ref.7 Ref.8 Ref.11
Subcellular location	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. Ref.2 Ref.6 Ref.10
Tissue specificity	Widely expressed throughout the brain (at protein level). Expressed by neural and endocrine cells of brain and spinal cord. Ref.2
Post-translational modification	Phosphorylation by CK1 of the N-terminal cytoplasmic domain regulates interaction with SYT1. N-glycosylated. Ref.1
Miscellaneous	Identified as the brain binding-site for the antiepileptic drug levetiracetam/lev.
Sequence similarities	Belongs to the major facilitator superfamily.

Ontologies

Keywords
Biological process	Neurotransmitter transport Transport
Cellular component	Cell junction Cytoplasmic vesicle Membrane Synapse
Domain	Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	neurotransmitter transport Traceable author statement Ref.3. Source: RGD
Cellular component	integral to membrane Inferred from direct assay Ref.3. Source: RGD synaptic vesicle membrane Inferred from direct assay Ref.3. Source: RGD
Molecular function	protein binding Inferred from physical interaction Ref.5. Source: UniProtKB receptor activity Inferred from electronic annotation. Source: UniProtKB-KW transmembrane transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Syt1	P21707	2	EBI-466194,EBI-458098

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 742

742

Synaptic vesicle glycoprotein 2A

PRO_0000084882

Regions

Topological domain

1 – 169

169

Cytoplasmic Potential

Transmembrane

170 – 190

Helical; Potential

Topological domain

191 – 205

Extracellular Potential

Transmembrane

206 – 226

Helical; Potential

Topological domain

227 – 233

Cytoplasmic Potential

Transmembrane

234 – 254

Helical; Potential

Topological domain

255 – 262

Extracellular Potential

Transmembrane

263 – 283

Helical; Potential

Topological domain

284 – 294

Cytoplasmic Potential

Transmembrane

295 – 315

Helical; Potential

Topological domain

316 – 334

Extracellular Potential

Transmembrane

335 – 355

Helical; Potential

Topological domain

356 – 447

Cytoplasmic Potential

Transmembrane

448 – 468

Helical; Potential

Topological domain

469 – 598

130

Extracellular Potential

Transmembrane

599 – 619

Helical; Potential

Topological domain

620 – 626

Cytoplasmic Potential

Transmembrane

627 – 647

Helical; Potential

Topological domain

648 – 651

Extracellular Potential

Transmembrane

652 – 672

Helical; Potential

Topological domain

673 – 685

Cytoplasmic Potential

Transmembrane

686 – 708

Helical; Potential

Topological domain

709 – 712

Extracellular Potential

Transmembrane

713 – 731

Helical; Potential

Topological domain

732 – 742

Cytoplasmic Potential

Region

1 – 57

Interaction with SYT1

Region

543 – 580

BOTA-binding By similarity

Amino acid modifications

Modified residue

Phosphotyrosine By similarity

Modified residue

Phosphotyrosine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphothreonine By similarity

Modified residue

127

Phosphoserine By similarity

Modified residue

480

Phosphotyrosine By similarity

Glycosylation

498

N-linked (GlcNAc...) Potential

Glycosylation

548

N-linked (GlcNAc...) Potential

Glycosylation

573

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

340

C → F in AAA42188. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q02563 [UniParc].

Last modified June 13, 2006. Version 2.
Checksum: E10FC62BEEFE316A
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FASTA

742

82,661

        10         20         30         40         50         60 
MEEGFRDRAA FIRGAKDIAK EVKKHAAKKV VKGLDRVQDE YSRRSYSRFE EEEDDDDFPA 

        70         80         90        100        110        120 
PADGYYRGEG AQDEEEGGAS SDATEGHDED DEIYEGEYQG IPRAESGGKG ERMADGAPLA 

       130        140        150        160        170        180 
GVRGGLSDGE GPPGGRGEAQ RRKDREELAQ QYETILRECG HGRFQWTLYF VLGLALMADG 

       190        200        210        220        230        240 
VEVFVVGFVL PSAEKDMCLS DSNKGMLGLI VYLGMMVGAF LWGGLADRLG RRQCLLISLS 

       250        260        270        280        290        300 
VNSVFAFFSS FVQGYGTFLF CRLLSGVGIG GSIPIVFSYF SEFLAQEKRG EHLSWLCMFW 

       310        320        330        340        350        360 
MIGGVYAAAM AWAIIPHYGW SFQMGSAYQF HSWRVFVLVC AFPSVFAIGA LTTQPESPRF 

       370        380        390        400        410        420 
FLENGKHDEA WMVLKQVHDT NMRAKGHPER VFSVTHIKTI HQEDELIEIQ SDTGTWYQRW 

       430        440        450        460        470        480 
GVRALSLGGQ VWGNFLSCFS PEYRRITLMM MGVWFTMSFS YYGLTVWFPD MIRHLQAVDY 

       490        500        510        520        530        540 
AARTKVFPGE RVEHVTFNFT LENQIHRGGQ YFNDKFIGLR LKSVSFEDSL FEECYFEDVT 

       550        560        570        580        590        600 
SSNTFFRNCT FINTVFYNTD LFEYKFVNSR LVNSTFLHNK EGCPLDVTGT GEGAYMVYFV 

       610        620        630        640        650        660 
SFLGTLAVLP GNIVSALLMD KIGRLRMLAG SSVLSCVSCF FLSFGNSESA MIALLCLFGG 

       670        680        690        700        710        720 
VSIASWNALD VLTVELYPSD KRTTAFGFLN ALCKLAAVLG ISIFTSFVGI TKAAPILFAS 

       730        740 
AALALGSSLA LKLPETRGQV LQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 1355409] [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: 1426240] [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: 1519064] [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: 15489334] [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: 8910372] [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: 10625067] [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: 10455054] [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: 10747945] [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: 15210974] [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: 16306227] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]	"SV2A and SV2C contain a unique synaptotagmin-binding site." Schivell A.E., Mochida S., Kensel-Hammes P., Custer K.L., Bajjalieh S.M. Mol. Cell. Neurosci. 29:56-64(2005) [PubMed: 15866046] [Abstract] 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: 16543415] [Abstract] Cited for: FUNCTION AS A BOTA RECEPTOR.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L01788 Genomic RNA. No translation available. L05435 mRNA. Translation: AAA42188.1. BC092132 mRNA. Translation: AAH92132.1.
IPI	IPI00208115.
PIR	A43344.
RefSeq	NP_476558.2. NM_057210.2.
UniGene	Rn.11264.
3D structure databases
ProteinModelPortal	Q02563.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q02563. 2 interactions.
MINT	MINT-87493.
STRING	Q02563.
Protein family/group databases
TCDB	2.A.1.22.1. major facilitator superfamily (MFS).
PTM databases
PhosphoSite	Q02563.
Proteomic databases
PRIDE	Q02563.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000028760; ENSRNOP00000028760; ENSRNOG00000021182.
GeneID	117559.
KEGG	rno:117559.
NMPDR	fig\|10116.3.peg.16631.
UCSC	NM_057210. rat.
Organism-specific databases
CTD	9900.
RGD	619715. Sv2a.
Phylogenomic databases
eggNOG	roNOG15218.
GeneTree	ENSGT00550000074384.
HOVERGEN	HBG053967.
OrthoDB	EOG4K0QMZ.
Gene expression databases
ArrayExpress	Q02563.
Genevestigator	Q02563.
GermOnline	ENSRNOG00000021182. Rattus norvegicus.
Family and domain databases
InterPro	IPR011701. MFS. IPR020846. MFS_dom. IPR016196. MFS_dom_general_subst_transpt. IPR005828. Sub_transporter. IPR005829. Sugar_transporter_CS. IPR022308. SV2_chordata. [Graphical view]
KO	K06258.
Pfam	PF07690. MFS_1. 1 hit. PF00083. Sugar_tr. 1 hit. [Graphical view]
SUPFAM	SSF103473. MFS_gen_substrate_transporter. 1 hit.
TIGRFAMs	TIGR01299. Synapt_SV2. 1 hit.
PROSITE	PS50850. MFS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	620423.

Entry information

Entry name

SV2A_RAT

Accession

Primary (citable) accession number: Q02563
Secondary accession number(s): Q58DZ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	June 13, 2006
Last modified:	November 16, 2011
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents