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Synuclein Edit Wikipedia article
Structure of micelle-bound human alpha-synuclein.
 Family members
The synuclein family includes three known proteins: alpha-synuclein, beta-synuclein, and gamma-synuclein. Interest in the synuclein family began when alpha-synuclein was found to be mutated in several families with autosomal dominant Parkinson's disease.
All synucleins have in common a highly conserved alpha-helical lipid-binding motif with similarity to the class-A2 lipid-binding domains of the exchangeable apolipoproteins. Synuclein family members are not found outside vertebrates, although they have some conserved structural similarity with plant 'late-embryo-abundant' proteins.
Normal cellular functions have not been determined for any of the synuclein proteins. Some data suggest a role in the regulation of membrane stability and/or turnover. Mutations in alpha-synuclein are associated with early-onset familial Parkinson's disease and the protein aggregates abnormally in Parkinson's disease, Alzheimer's disease, Lewy body disease, and other neurodegenerative diseases. The gamma-synuclein protein's expression in breast tumors is a marker for tumor progression.
 Human proteins containing this domain
- Ulmer TS, Bax A, Cole NB, Nussbaum RL (March 2005). "Structure and dynamics of micelle-bound human alpha-synuclein". J. Biol. Chem. 280 (10): 9595–603. doi:10.1074/jbc.M411805200. PMID 15615727.
- Lavedan C (September 1998). "The synuclein family". Genome Res. 8 (9): 871–80. doi:10.1101/gr.8.9.871. PMID 9750188.
- George JM (2002). "The synucleins". Genome Biol. 3 (1): REVIEWS3002. doi:10.1186/gb-2001-3-1-reviews3002. PMC 150459. PMID 11806835.
- Ma QL, Chan P, Yoshii M, Uéda K (April 2003). "Alpha-synuclein aggregation and neurodegenerative diseases". J. Alzheimers Dis. 5 (2): 139–48. PMID 12719631.
- Goedert M (July 2001). "Alpha-synuclein and neurodegenerative diseases". Nat. Rev. Neurosci. 2 (7): 492–501. doi:10.1038/35081564. PMID 11433374.
- Bruening W, Giasson BI, Klein-Szanto AJ, Lee VM, Trojanowski JQ, Godwin AK (May 2000). "Synucleins are expressed in the majority of breast and ovarian carcinomas and in preneoplastic lesions of the ovary". Cancer 88 (9): 2154–63. doi:10.1002/(SICI)1097-0142(20000501)88:9<2154::AID-CNCR23>3.0.CO;2-9. PMID 10813729.
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Synuclein Provide feedback
There are three types of synucleins in humans, these are called alpha, beta and gamma. Alpha synuclein has been found mutated in families with autosomal dominant Parkinson's disease. A peptide of alpha synuclein has also been found in amyloid plaques in Alzheimer's patients.
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR001058
Synucleins are small, soluble proteins expressed primarily in neural tissue and in certain tumors [PUBMED:9750188, [PUBMED:11806835]. The family includes three known proteins: alpha-synuclein, beta-synuclein, and gamma-synuclein. All synucleins have in common a highly conserved alpha-helical lipid-binding motif with similarity to the class-A2 lipid-binding domains of the exchangeable apolipoproteins [PUBMED:10952980].
Synuclein family members are not found outside vertebrates, although they have some conserved structural similarity with plant 'late-embryo-abundant' proteins. The alpha- and beta-synuclein proteins are found primarily in brain tissue, where they are seen mainly in presynaptic terminals [PUBMED:7857654, PUBMED:7877458]. The gamma-synuclein protein is found primarily in the peripheral nervous system and retina, but its expression in breast tumors is a marker for tumor progression [PUBMED:9044857]. Normal cellular functions have not been determined for any of the synuclein proteins, although some data suggest a role in the regulation of membrane stability and/or turnover. Mutations in alpha-synuclein are associated with rare familial cases of early-onset Parkinson's disease, and the protein accumulates abnormally in Parkinson's disease, Alzheimer's disease, and several other neurodegenerative illnesses [PUBMED:11433374].
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Curation and family details
|Number in seed:||4|
|Number in full:||229|
|Average length of the domain:||111.10 aa|
|Average identity of full alignment:||60 %|
|Average coverage of the sequence by the domain:||94.74 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||12|
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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 Synuclein domain has been found. There are 9 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 seqence.
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