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InterPro: IPR001388 Synaptobrevin

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1130 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession List
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Accession

IPR001388 Synaptobrevin

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00957	Synaptobrevin	1064
PRINTS	PR00219	SYNAPTOBREVN	683
PROSITE pattern	PS00417	SYNAPTOBREVIN	428
PROSITE profile	PS50892	V_SNARE	1097
Signatures in BioMart

InterPro Relationships Help

Found in

IPR016444 Synaptobrevin, metazoa/fungi

GO Term annotation Help

Process

GO:0016192 vesicle-mediated transport

Component

GO:0016021 integral to membrane

InterPro annotation

Entry Details in BioMart

Abstract

Synaptobrevin is an intrinsic membrane protein of small synaptic vesicles [1], specialised secretory organelles of neurons that actively accumulate neurotransmitters and participate in their calcium-dependent release by exocytosis. Vesicle function is mediated by proteins in their membranes, although the precise nature of the protein-protein interactions underlying this are still uncertain [2]. Synaptobrevin may play a role in the molecular events underlying neurotransmitter release and vesicle recycling and may be involved in the regulation of membrane flow in the nerve terminal, a process mediated by interaction with low molecular weight GTP-binding proteins [3]. Synaptic vesicle-associated membrane proteins (VAMPs) from Torpedo californica (Pacific electric ray) and SNC1 from yeast are related to synaptobrevin.

Structural links Help

PDB - click here

SCOP: d.110.4.1 , h.1.15.1

CATH: 1.20.5.110 , 3.30.450.50

Database links Help

PDBe-motif: PS00417

PROSITE doc: PDOC00368 , PDOC50892

PANDIT: PF00957

Blocks: IPB001388

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001388

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O02495 Synaptobrevin-1

O08547 Vesicle-trafficking protein SEC22b

O75396 Vesicle-trafficking protein SEC22b

P18489 Synaptobrevin

P31109 Synaptobrevin homolog 1

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR016444	Synaptobrevin, metazoa/fungi
IPR010908	Longin
IPR001388	Synaptobrevin
IPR011012	Longin-like
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Sudhof TC, Baumert M, Perin MS, Jahn R. A synaptic vesicle membrane protein is conserved from mammals to Drosophila. Neuron 2 1475-81 1989 [PubMed: 2560644] http://dx.doi.org/10.1016/0896-6273(89)90193-1
2.	Archer BT 3rd, Ozcelik T, Jahn R, Francke U, Sudhof TC. Structures and chromosomal localizations of two human genes encoding synaptobrevins 1 and 2. J. Biol. Chem. 265 17267-73 1990 [PubMed: 1976629] http://intl.jbc.org/cgi/reprint/265/28/17267.pdf
3.	Chin AC, Burgess RW, Wong BR, Schwarz TL, Scheller RH. Differential expression of transcripts from syb, a Drosophila melanogaster gene encoding VAMP (synaptobrevin) that is abundant in non-neuronal cells. Gene 131 175-81 1993 [PubMed: 8406010] http://dx.doi.org/10.1016/0378-1119(93)90291-A

Additional Reading Open in usermanual
	Strop P, Kaiser SE, Vrljic M, Brunger AT. The structure of the yeast plasma membrane SNARE complex reveals destabilizing water-filled cavities. J. Biol. Chem. 283 2008 1113-9 [PubMed: 17956869] http://dx.doi.org/10.1074/jbc.M707912200
	Fasshauer D, Sutton RB, Brunger AT, Jahn R. Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs. Proc. Natl. Acad. Sci. U.S.A. 95 1998 15781-6 [PubMed: 9861047] http://dx.doi.org/10.1073/pnas.95.26.15781
	Scales SJ, Hesser BA, Masuda ES, Scheller RH. Amisyn, a novel syntaxin-binding protein that may regulate SNARE complex assembly. J. Biol. Chem. 277 2002 28271-9 [PubMed: 12145319] http://dx.doi.org/10.1074/jbc.M204929200
	Terrian DM, White MK. Phylogenetic analysis of membrane trafficking proteins: a family reunion and secondary structure predictions. Eur. J. Cell Biol. 73 1997 198-204 [PubMed: 9243180]
	Gerst JE, Rodgers L, Riggs M, Wigler M. SNC1, a yeast homolog of the synaptic vesicle-associated membrane protein/synaptobrevin gene family: genetic interactions with the RAS and CAP genes. Proc. Natl. Acad. Sci. U.S.A. 89 1992 4338-42 [PubMed: 1316605] http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=1316605&action=stream&blobtype=pdf
	Pobbati AV, Razeto A, Boddener M, Becker S, Fasshauer D. Structural basis for the inhibitory role of tomosyn in exocytosis. J. Biol. Chem. 279 2004 47192-200 [PubMed: 15316007] http://dx.doi.org/10.1074/jbc.M408767200
	Pylypenko O, Schonichen A, Ludwig D, Ungermann C, Goody RS, Rak A, Geyer M. Farnesylation of the SNARE protein Ykt6 increases its stability and helical folding. J. Mol. Biol. 377 2008 1334-45 [PubMed: 18329045] http://dx.doi.org/10.1016/j.jmb.2008.01.099
	Zwilling D, Cypionka A, Pohl WH, Fasshauer D, Walla PJ, Wahl MC, Jahn R. Early endosomal SNAREs form a structurally conserved SNARE complex and fuse liposomes with multiple topologies. EMBO J. 26 2007 9-18 [PubMed: 17159904] http://dx.doi.org/10.1038/sj.emboj.7601467
	Ernst JA, Brunger AT. High resolution structure, stability, and synaptotagmin binding of a truncated neuronal SNARE complex. J. Biol. Chem. 278 2003 8630-6 [PubMed: 12496247] http://dx.doi.org/10.1074/jbc.M211889200

InterPro 24.0