Synaptic vesicle glycoprotein 2B - Rattus norvegicus (Rat)

Contribute

Send feedback

Read comments (?) or add your own

Q63564 (SV2B_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 87. History...

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

Documents (1) |

Third-party data

text xml rdf/xml gff fasta

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

Names and origin

Protein names

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

Gene names

Name:	Sv2b
Synonyms:	Sv2bb

Organism

Rattus norvegicus (Rat) [Reference proteome]

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	683 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probably plays a role in the control of regulated secretion in neural and endocrine cells By similarity. Ref.10 Receptor for the botulinium neurotoxin type A/BOTA. Ref.10
Subunit structure	Interacts with SYT1 in a calcium-independent manner. Forms a complex with SYT1, syntaxin-1 and SNAP25 By similarity. Ref.9
Subcellular location	Cytoplasmic vesicle › secretory vesicle › synaptic vesicle membrane; Multi-pass membrane protein. Cytoplasmic vesicle › secretory vesicle › acrosome. Note: Associated with synaptic-like microvesicles but not with insulin-containing vesicles in insulin-secreting cells of the pancreas. Localizes to microvesicles in the pinealocytes. Localizes to the acrosome in spermatids. Ref.1 Ref.7 Ref.8
Tissue specificity	Widely expressed throughout the brain. Specifically expressed by pinealocytes in the pineal gland. Also detected in testis (at protein level). Specifically expressed in neural tissues. Expressed in the spinal cord and in all brain regions with a stronger expression in hippocampus and cortex. Ref.1 Ref.3 Ref.5 Ref.7
Induction	By amyloid beta peptide. Ref.2
Post-translational modification	N-glycosylated. Ref.4 The N-terminal cytoplasmic domain is phosphorylated by CK1. Ref.6
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 Reference proteome
Gene Ontology (GO)
Biological_process	neurotransmitter uptake Traceable author statement Ref.1. Source: RGD
Cellular_component	acrosomal vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell cell junction Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane Inferred from direct assay Ref.1. Source: RGD synaptic vesicle Inferred from direct assay Ref.1. Source: RGD synaptic vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	transmembrane transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 683

683

Synaptic vesicle glycoprotein 2B

PRO_0000239770

Regions

Topological domain

1 – 110

110

Cytoplasmic Potential

Transmembrane

111 – 131

Helical; Potential

Topological domain

132 – 148

Extracellular Potential

Transmembrane

149 – 169

Helical; Potential

Topological domain

170 – 182

Cytoplasmic Potential

Transmembrane

183 – 203

Helical; Potential

Topological domain

204 – 205

Extracellular Potential

Transmembrane

206 – 226

Helical; Potential

Topological domain

227 – 237

Cytoplasmic Potential

Transmembrane

238 – 258

Helical; Potential

Topological domain

259 – 277

Extracellular Potential

Transmembrane

278 – 298

Helical; Potential

Topological domain

299 – 390

Cytoplasmic Potential

Transmembrane

391 – 411

Helical; Potential

Topological domain

412 – 535

124

Extracellular Potential

Transmembrane

536 – 556

Helical; Potential

Topological domain

557 – 565

Cytoplasmic Potential

Transmembrane

566 – 586

Helical; Potential

Topological domain

587 – 592

Extracellular Potential

Transmembrane

593 – 613

Helical; Potential

Topological domain

614 – 626

Cytoplasmic Potential

Transmembrane

627 – 649

Helical; Potential

Topological domain

650 – 653

Extracellular Potential

Transmembrane

654 – 672

Helical; Potential

Topological domain

673 – 683

Cytoplasmic Potential

Region

486 – 523

BOTA-binding By similarity

Amino acid modifications

Modified residue

423

Phosphotyrosine By similarity

Glycosylation

441

N-linked (GlcNAc...) Potential

Glycosylation

491

N-linked (GlcNAc...) Potential

Glycosylation

516

N-linked (GlcNAc...) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q63564 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: BF862EFD4B99EA7B
Show »

FASTA

683

77,502

        10         20         30         40         50         60 
MDDYRYRDNY EGYAPNDGYY RGNEQNPEED AQSDVTEGHD EEDEIYEGEY QGIPHPDDVK 

        70         80         90        100        110        120 
SKQTKMAPSR ADGLRGQADL MAERMEDEEQ LAHQYETIID ECGHGRFQWT LFFVLVLALM 

       130        140        150        160        170        180 
ADGVEVFVVS FALPSAEKDM CLSSSKKGML GLIVYLGMMA GAFILGGLAD KLGRKKVLSM 

       190        200        210        220        230        240 
SLAINASFAS LSSFVQGYGA FLFCRLISGI GIGGSLPIVF AYFSEFLSRE KRGEHLSWLG 

       250        260        270        280        290        300 
IFWMTGGIYA SAMAWSIIPH YGWGFSMGTN YHFHSWRVFV IVCALPATVS MVALKFMPES 

       310        320        330        340        350        360 
PRFLLEMGKH DEAWMILKQV HDTNMRAKGT PEKVFTVSHI KTPKQMDEFI EIQSSTGTWY 

       370        380        390        400        410        420 
QRWLVRFMTI FKQVWDNALY CVMGPYRMNT LILAVVWFTM ALSYYGLTVW FPDMIRYFQD 

       430        440        450        460        470        480 
EEYKSKMKVF FGEHVHGATI NFTMENQIHQ HGKLVNDKFI KMYFKHVLFE DTFFDKCYFE 

       490        500        510        520        530        540 
DVTSTDTYFK NCTIESTTFY NTDLYKHKFI DCRFINSTFL EQKEGCHMDF EEDNDFLIYL 

       550        560        570        580        590        600 
VSFLGSLSVL PGNIISALLM DRIGRLKMIG GSMLISAVCC FFLFFGNSES AMIGWQCLFC 

       610        620        630        640        650        660 
GTSIAAWNAL DVITVELYPT NQRATAFGIL NGLCKLGAIL GNTIFASFVG ITKVVPILLA 

       670        680 
AASLVGGGLV ALRLPETREQ VLM

« Hide

References

[1]	"Brain contains two forms of synaptic vesicle protein 2." Bajjalieh S.M., Peterson K.E., Linial M., Scheller R.H. Proc. Natl. Acad. Sci. U.S.A. 90:2150-2154(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION. Strain: Sprague-Dawley. Tissue: Brain.
[2]	"Identification of a new synaptic vesicle protein 2B mRNA transcript which is up-regulated in neurons by amyloid beta peptide fragment (1-42)." Heese K., Nagai Y., Sawada T. Biochem. Biophys. Res. Commun. 289:924-928(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
[3]	"Synaptic vesicle protein SV2B, but not SV2A, is predominantly expressed and associated with microvesicles in rat pinealocytes." Hayashi M., Yamamoto A., Yatsushiro S., Yamada H., Futai M., Yamaguchi A., Moriyama Y. J. Neurochem. 71:356-365(1998) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[4]	"SVOP, an evolutionarily conserved synaptic vesicle protein, suggests novel transport functions of synaptic vesicles." Janz R., Hofmann K., Suedhof T.C. J. Neurosci. 18:9269-9281(1998) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION.
[5]	"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: TISSUE SPECIFICITY.
[6]	"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.
[7]	"Brain synaptic junctional proteins at the acrosome of rat testicular germ cells." Redecker P., Kreutz M.R., Bockmann J., Gundelfinger E.D., Boeckers T.M. J. Histochem. Cytochem. 51:809-819(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[8]	"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: SUBCELLULAR LOCATION.
[9]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SYT1.
[10]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L10362 mRNA. Translation: AAA42189.1. AF372834 mRNA. Translation: AAL47714.1.
IPI	IPI00210125.
PIR	S34961.
RefSeq	NP_476555.1. NM_057207.3.
UniGene	Rn.58137.
3D structure databases
ProteinModelPortal	Q63564.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000015084.
PTM databases
PhosphoSite	Q63564.
Proteomic databases
PaxDb	Q63564.
PRIDE	Q63564.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	117556.
KEGG	rno:117556.
UCSC	RGD:619716. rat.
Organism-specific databases
CTD	9899.
RGD	619716. Sv2b.
Phylogenomic databases
eggNOG	COG0477.
HOGENOM	HOG000065727.
HOVERGEN	HBG053967.
InParanoid	Q63564.
KO	K06258.
OrthoDB	EOG4K0QMZ.
Gene expression databases
Genevestigator	Q63564.
GermOnline	ENSRNOG00000011160. Rattus norvegicus.
Family and domain databases
InterPro	IPR001646. 5peptide_repeat. IPR011701. MFS. IPR020846. MFS_dom. IPR016196. MFS_dom_general_subst_transpt. IPR005828. Sub_transporter. IPR005829. Sugar_transporter_CS. IPR022308. SV2. [Graphical view]
PANTHER	PTHR24065. PTHR24065. 1 hit.
Pfam	PF07690. MFS_1. 1 hit. PF13599. Pentapeptide_4. 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	620409.

Entry information

Entry name

SV2B_RAT

Accession

Primary (citable) accession number: Q63564

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 13, 2006
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 87 of the entry and version 1 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction 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