| General information | | DisProt: | DP00068 | | Name: | Synaptosomal-associated protein 25 | | Synonym(s): | SNP25_RAT
SNAP-25
Synaptosomal-associated 25 kDa protein
Super protein
SUP
| | First appeared in release: | Release 2.0 (02/14/2005) | | UniProt: | P60881 | | UniGene: | Rn.107689 | | SwissProt: | SNP25_RAT | | TrEMBL: | | | NCBI (GI): | 46397720 | | Source organism: | Rattus norvegicus (Rat) | | Sequence length: | 206 | | Percent disordered: | 100% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MAEDADMRNE LEEMQRRADQ LADESLESTR RMLQLVEESK DAGIRTLVML DEQGEQLDRV - 60
EEGMNHINQD MKEAEKNLKD LGKCCGLYIC PCNKLKSSDA YKKAWGNNQD QVVASQPARV - 120
VDEREQMAIS GGFIRRVTND ARENEMDEDL EQVSGIIGNL RHMALDMGNE IDTQNRQIDR - 180
IMEKADSNKT RIDEANQRAT KMLGSG
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| Functional narrative |
The formation of the SNARE complex is a key step in mediating exocytosis of synaptic vesicles and molecular regulation of neurotransmitter release. SNAP-25 is a member of the SNAP-25 family. Upon binding, major structural and conformation changes occur. There is a large increase in alpha-helical content and in melting temperature during the binding process. Therefore, SNAP-25 goes from a largely unstructured protein to a highly stable and complex member of a complex of proteins.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered - Extended | | Name: | | | Location: | 1 - 206 | | Length: | 206 | | Region sequence: |
MAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLDRV
EEGMNHINQDMKEAEKNLKDLGKCCGLYICPCNKLKSSDAYKKAWGNNQDQVVASQPARV
VDEREQMAISGGFIRRVTNDARENEMDEDLEQVSGIIGNLRHMALDMGNEIDTQNRQIDR
IMEKADSNKTRIDEANQRATKMLGSG | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (277 K; pH: 7.4; NaCl (salt) 100 mM; phosphate (buffer) 10 mM)
- Nuclear magnetic resonance (NMR)
- Sensitivity to proteolysis (298 K; chymotrypsin; NaCl (salt) 100 nM; proteinase K; trypsin)
- Size exclusion/gel filtration chromatography (368 K; pH: 6.8; betamercaptoethanol (buffer) 3 %; glycerol (buffer) 10 %; SDS (buffer) 2 %; Tris (buffer) 60 mM)
- Size exclusion/gel filtration chromatography (298 K; pH: 6.8; betamercaptoethanol (buffer) 3 %; glycerol (buffer) 10 %; SDS (buffer) 2 %; Tris (buffer) 60 mM)
| References:
- Fasshauer D, Eliason WK, Brünger AT, Jahn R. "Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly." Biochemistry. 1998; 37(29): 10354-62. PubMed: 9671503
| Comments:The sequence has 98% similarity to that of chicken and human SNAP-25 but there is no 100% match to any organism when Blasted.
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| References |
- Brunger AT. "Structural insights into the molecular mechanism of Ca(2+)-dependent exocytosis." Curr Opin Neurobiol. 2000; 10(3): 293-302. PubMed: 10851178
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