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90  structures 1589  species 0  interactions 11740  sequences 201  architectures

Family: Synaptobrevin (PF00957)

Summary: Synaptobrevin

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This is the Wikipedia entry entitled "Synaptobrevin". More...

Synaptobrevin Edit Wikipedia article

Three different views of the high resolution structure of a truncated neuronal SNARE complex. Legend: synaptobrevin-2 (red), Syntaxin-1 (pink), SNAP-25 (purple).
OPM superfamily197
OPM protein4wy4

Synaptobrevins (synaptobrevin isotypes 1-2) are small integral membrane proteins of secretory vesicles with molecular weight of 18 kilodalton (kDa) that are part of the vesicle-associated membrane protein (VAMP) family.[1][2][3][4][5]

Synaptobrevin is one of the SNARE proteins involved in formation of the SNARE complexes.


Out of four α-helices of the core SNARE complex one is contributed by synaptobrevin, one by syntaxin, and two by SNAP-25 (in neurons).


SNARE proteins are the key components of the molecular machinery that drives fusion of membranes in exocytosis. Their function however is subject to fine-tuning by various regulatory proteins collectively referred to as SNARE masters.


In the Q/R nomenclature for organizing SNARE proteins, VAMP/synaptobrevin family members are classified as R-SNAREs, so named for the presence of an arginine at a specific location within the primary sequence of the protein (as opposed to the SNAREs of the target membrane, which contain a glutamine and are so named Q-SNAREs). Synaptobrevin is classified as a V-SNARE in the V/T nomenclature, an alternative classification scheme in which SNAREs are classified as V-SNAREs and T-SNAREs for their localization to vesicles and target membranes, respectively.[6]

Clinical significance

Synaptobrevin is degraded by tetanospasmin, a protein derived from the bacterium Clostridium tetani, which causes tetanus. A related bacterium, Clostridium botulinum, produces the botulinum toxin. Various botulinum toxin serotypes exist that each cleave specific peptide bonds of specific neuronal SNARE proteins, and synaptobrevin is this target protein for several of the serotypes.

Human proteins containing this domain


References and notes

  1. ^ Baumert M, Maycox PR, Navone F, De Camilli P, Jahn R (February 1, 1989). "Synaptobrevin: an integral membrane protein of 18,000 daltons present in small synaptic vesicles of rat brain". EMBO J. 8 (2): 379–84. doi:10.1002/j.1460-2075.1989.tb03388.x. PMC 400817. PMID 2498078.
  2. ^ Bock JB, Scheller RH (October 1999). "SNARE proteins mediate lipid bilayer fusion". Proc. Natl. Acad. Sci. U.S.A. 96 (22): 12227–9. doi:10.1073/pnas.96.22.12227. PMC 34255. PMID 10535902.
  3. ^ Ernst JA, Brunger AT (2003). "High resolution structure, stability, and synaptotagmin binding of a truncated neuronal SNARE complex". J Biol Chem. 278 (10): 8630–6. doi:10.1074/jbc.M211889200. PMID 12496247.
  4. ^ Fasshauer D, Sutton RB, Brunger AT, Jahn R (December 1998). "Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs". Proc. Natl. Acad. Sci. U.S.A. 95 (26): 15781–6. doi:10.1073/pnas.95.26.15781. PMC 28121. PMID 9861047.
  5. ^ Weber T, Zemelman BV, McNew JA, Westermann B, Gmachl M, Parlati F, Sollner TH, Rothman JE (1998). "SNAREpins: minimal machinery for membrane fusion". Cell. 92 (6): 759–72. doi:10.1016/S0092-8674(00)81404-X. PMID 9529252.
  6. ^ Juan S. Bonifacino and Benjamin S. Glick. "The Mechanisms of Vesicle Budding and Fusion." Cell, Vol. 116, 153–166, January 23, 2004,

External links

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Synaptobrevin Provide feedback

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Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR001388

Synaptobrevin is an intrinsic membrane protein of small synaptic vesicles [ PUBMED:2560644 ], 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 [ PUBMED:1976629 ]. 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 [ PUBMED:8406010 ]. Synaptic vesicle-associated membrane proteins (VAMPs) from Torpedo californica (Pacific electric ray) and SNC1 from yeast are related to synaptobrevin.

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan SNARE-fusion (CL0445), which has the following description:

The SNARE-fusion complex families are characterised by being tetrameric coiled-coil structures.

The clan contains the following 3 members:

Synaptobrevin Syntaxin Syntaxin_2


We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

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HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...


This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

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Seed source: Pfam-B_303 (release 3.0)
Previous IDs: synaptobrevin;
Type: Family
Sequence Ontology: SO:0100021
Author: Finn RD , Bateman A
Number in seed: 93
Number in full: 11740
Average length of the domain: 80.00 aa
Average identity of full alignment: 29 %
Average coverage of the sequence by the domain: 36.27 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 26.4 26.4
Trusted cut-off 26.4 26.4
Noise cut-off 26.3 26.3
Model length: 89
Family (HMM) version: 24
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Synaptobrevin domain has been found. There are 90 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A096MJ99 View 3D Structure Click here
A0A0P0YCQ1 View 3D Structure Click here
A0A140LH10 View 3D Structure Click here
A0A143ZWB4 View 3D Structure Click here
A0A1D5RLS7 View 3D Structure Click here
A0A1D6EN56 View 3D Structure Click here
A0A1D6G402 View 3D Structure Click here
A0A1D6GFC3 View 3D Structure Click here
A0A1D6HV32 View 3D Structure Click here
A0A1D6HWP5 View 3D Structure Click here
A0A1D6JPX1 View 3D Structure Click here
A0A1D6KH00 View 3D Structure Click here
A0A1D6L7E0 View 3D Structure Click here
A0A1D6L850 View 3D Structure Click here
A0A1D6LY65 View 3D Structure Click here
A0A1D6MEX7 View 3D Structure Click here
A0A1D6N6G8 View 3D Structure Click here
A0A1D6PKL1 View 3D Structure Click here
A0A1D6QJT6 View 3D Structure Click here
A0A1D8PFS0 View 3D Structure Click here
A0A1D8PG36 View 3D Structure Click here
A0A1D8PSL3 View 3D Structure Click here
A0A368UHK6 View 3D Structure Click here
A2BG37 View 3D Structure Click here
A4HTF3 View 3D Structure Click here
A4HY62 View 3D Structure Click here
A4HZC6 View 3D Structure Click here
A4I337 View 3D Structure Click here
A4I839 View 3D Structure Click here
B4FK20 View 3D Structure Click here
B4FPM8 View 3D Structure Click here
B4FQX6 View 3D Structure Click here
B6T9E2 View 3D Structure Click here
C0H5D3 View 3D Structure Click here
C6SVB1 View 3D Structure Click here
C6TGR3 View 3D Structure Click here
C6TME8 View 3D Structure Click here
C6TNZ7 View 3D Structure Click here
D3ZCI5 View 3D Structure Click here
E9AHV2 View 3D Structure Click here