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SB0036 : [alpha]-Synuclein

[ CaMP Format ]

* Basic Information

OrganismHomo sapiens (human)
Protein Namesalpha-synuclein isoform NACP140 [Homo sapiens]; alpha-synuclein isoform NACP140; non A-beta component of AD amyloid; synuclein alpha-140; Alpha-synuclein; Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP
Gene NamesSNCA; NACP, PARK1; NACP; PARK1; synuclein, alpha (non A4 component of amyloid precursor)
Gene Locus4q21; chromosome 4
GO FunctionNot available
Entrez Protein Entrez Nucleotide Entrez Gene UniProt OMIM HGNC HPRD KEGG
NP_000336 NM_000345 6622 P37840 163890 HGNC:11138 01227 hsa:6622

* Information From OMIM

Description: Alpha-synuclein is a highly conserved protein that is abundant in neurons, especially presynaptic terminals. Aggregated alpha-synuclein proteins form brain lesions that are hallmarks of neurodegenerative synucleinopathies (summary by Giasson et al., 2000).

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* Structure Information

1. Primary Information

Length: 140 aa

Average Mass: 14.460 kDa

Monoisotopic Mass: 14.451 kDa

2. Domain Information

Annotated Domains: interpro / pfam / smart / prosite

Computationally Assigned Domains (Pfam+HMMER):

domain namebeginendscoree-value
Synuclein 1. 11301.017.6
--- cleavage 57 (inside Synuclein 1..130) ---
--- cleavage 73 (inside Synuclein 1..130) ---
--- cleavage 74 (inside Synuclein 1..130) ---
--- cleavage 83 (inside Synuclein 1..130) ---

3. Sequence Information

Fasta Sequence: SB0036.fasta

Amino Acid Sequence and Secondary Structures (PsiPred):

4. 3D Information

Known Structures in PDB: 1XQ8 (NMR; -; A=1-140), 2JN5 (NMR; -; A=1-12), 2KKW (NMR; -; A=1-140), 2M55 (NMR; -; B=1-19), 2X6M (X-ray; 162 A; B=132-140), 3Q25 (X-ray; 190 A; A=1-19), 3Q26 (X-ray; 154 A; A=10-42), 3Q27 (X-ray; 130 A; A=32-57), 3Q28 (X-ray; 160 A; A=58-79), 3Q29 (X-ray; 230 A; A/C=1-19), 4BXL (NMR; -; C=35-56), 4R0U (X-ray; 138 A; A=72-78), 4R0W (X-ray; 150 A; A=70-76)

* Cleavage Information

4 [sites] cleaved by Calpain 1

Source Reference: [PubMed ID: 15909996] Mishizen-Eberz AJ, Norris EH, Giasson BI, Hodara R, Ischiropoulos H, Lee VM, Trojanowski JQ, Lynch DR, Cleavage of alpha-synuclein by calpain: potential role in degradation of fibrillized and nitrated species of alpha-synuclein. Biochemistry. 2005 May 31;44(21):7818-29.

Cleavage sites (±10aa)


Glu57 Lys

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'

Sequence conservation (by blast)


Gly73 Val

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'

Sequence conservation (by blast)


Val74 Thr

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'

Sequence conservation (by blast)


Glu83 Gly

P10 P9 P8 P7 P6 P5 P4 P3 P2 P1
P1' P2' P3' P4' P5' P6' P7' P8' P9' P10'

Sequence conservation (by blast)

* References

[PubMed ID: 24534465] Kang S, Heo TH, Kim SJ, Altered levels of alpha-synuclein and sphingolipids in Batten disease lymphoblast cells. Gene. 2014 Apr 15;539(2):181-5. doi: 10.1016/j.gene.2014.02.017. Epub 2014 Feb

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