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InterPro: IPR001058 Synuclein
Protein matches
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UniProtKB Matches: 108 proteins |
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Accession
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IPR001058 Synuclein |
Type
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Family |
Signatures
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InterPro Relationships
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Children
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IPR002460 Alpha-synuclein
IPR002461 Beta-synuclein
IPR002462 Gamma-synuclein
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GO Term annotation
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Component
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GO:0005737 cytoplasm
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InterPro annotation
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Entry Details in BioMart
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Abstract
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Synucleins are small, soluble proteins expressed primarily in neural tissue and in certain tumors [1, [2]. 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 [3].
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 [4, 5]. 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 [6].
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 [7].
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Structural links
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Database links
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Publications
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1.
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Lavedan C.
The synuclein family.
Genome Res. 8 871-80 1998
[PubMed: 9750188]
http://www.genome.org/cgi/content/abstract/8/9/871
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2.
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George JM.
The synucleins.
Genome Biol. 3 REVIEWS3002 2002
[PubMed: 11806835]
http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=11806835
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3.
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Perrin RJ, Woods WS, Clayton DF, George JM.
Interaction of human alpha-Synuclein and Parkinson's disease variants with phospholipids. Structural analysis using site-directed mutagenesis.
J. Biol. Chem. 275 34393-8 2000
[PubMed: 10952980]
http://dx.doi.org/10.1074/jbc.M004851200
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4.
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Iwai A, Masliah E, Yoshimoto M, Ge N, Flanagan L, de Silva HA, Kittel A, Saitoh T.
The precursor protein of non-A beta component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system.
Neuron 14 467-75 1995
[PubMed: 7857654]
http://dx.doi.org/10.1016/0896-6273(95)90302-X
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5.
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Nakajo S, Shioda S, Nakai Y, Nakaya K.
Localization of phosphoneuroprotein 14 (PNP 14) and its mRNA expression in rat brain determined by immunocytochemistry and in situ hybridization.
Brain Res. Mol. Brain Res. 27 81-6 1994
[PubMed: 7877458]
http://dx.doi.org/10.1016/0169-328X(94)90187-2
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6.
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Ji H, Liu YE, Jia T, Wang M, Liu J, Xiao G, Joseph BK, Rosen C, Shi YE.
Identification of a breast cancer-specific gene, BCSG1, by direct differential cDNA sequencing.
Cancer Res. 57 759-64 1997
[PubMed: 9044857]
http://cancerres.aacrjournals.org/cgi/content/abstract/57/4/759
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7.
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Goedert M.
Alpha-synuclein and neurodegenerative diseases.
Nat. Rev. Neurosci. 2 492-501 2001
[PubMed: 11433374]
http://dx.doi.org/10.1038/35081564
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Additional Reading
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George JM, Jin H, Woods WS, Clayton DF.
Characterization of a novel protein regulated during the critical period for song learning in the zebra finch.
Neuron 15 1995 361-72
[PubMed: 7646890]
http://dx.doi.org/10.1016/0896-6273(95)90040-3
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Ulmer TS, Bax A, Cole NB, Nussbaum RL.
Structure and dynamics of micelle-bound human alpha-synuclein.
J. Biol. Chem. 280 2005 9595-603
[PubMed: 15615727]
http://dx.doi.org/10.1074/jbc.M411805200
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Tobe T, Nakajo S, Tanaka A, Mitoya A, Omata K, Nakaya K, Tomita M, Nakamura Y.
Cloning and characterization of the cDNA encoding a novel brain-specific 14-kDa protein.
J. Neurochem. 59 1992 1624-9
[PubMed: 1402909]
http://dx.doi.org/10.1111/j.1471-4159.1992.tb10991.x
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InterPro 23.1
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