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1.C.77.1.1
α-synuclein (140 aas). In addition to β-amyloid, the cellular prion protein, PrPC  binds α-synuclein, which is responsible for neurodegenerative synucleopathies (Urrea et al. 2017). β-barrel channels such as α-hemolysin may serve as sensitive probes of α-synuclein (α-syn) interactions with membranes as well as model systems for studies of channel-assisted protein transport (Gurnev et al. 2014).  α-synuclein interacts with membranes to affect Ca2+ signalling, and the oligomeric β-sheet-rich α-synuclein leads to Ca2+ dysregulation and Ca2+-dependent cell death (Angelova et al. 2016).

Accession Number:P37840
Protein Name:Alpha-synuclein
Length:140
Molecular Weight:14460.00
Species:Homo sapiens (Human) [9606]
Location1 / Topology2 / Orientation3: Cytoplasm1
Substrate molecule

Cross database links:

DIP: DIP-46126N
RefSeq: NP_000336.1    NP_001139526.1    NP_001139527.1    NP_009292.1   
Entrez Gene ID: 6622   
Pfam: PF01387   
OMIM: 127750  phenotype
163890  gene
168600  phenotype
168601  phenotype
605543  phenotype
KEGG: hsa:6622   

Gene Ontology

GO:0015629 C:actin cytoskeleton
GO:0030424 C:axon
GO:0005938 C:cell cortex
GO:0005829 C:cytosol
GO:0043205 C:fibril
GO:0030426 C:growth cone
GO:0005634 C:nucleus
GO:0005886 C:plasma membrane
GO:0043014 F:alpha-tubulin binding
GO:0005509 F:calcium ion binding
GO:0043027 F:caspase inhibitor activity
GO:0045502 F:dynein binding
GO:0008198 F:ferrous iron binding
GO:0042393 F:histone binding
GO:0030544 F:Hsp70 protein binding
GO:0019894 F:kinesin binding
GO:0000287 F:magnesium ion binding
GO:0043274 F:phospholipase binding
GO:0048156 F:tau protein binding
GO:0008270 F:zinc ion binding
GO:0006916 P:anti-apoptosis
GO:0043154 P:negative regulation of caspase activity
GO:0051585 P:negative regulation of dopamine uptake
GO:0045920 P:negative regulation of exocytosis
GO:0035067 P:negative regulation of histone acetylation
GO:0032769 P:negative regulation of monooxygenase activity
GO:0051622 P:negative regulation of norepinephrine uptake
GO:0010642 P:negative regulation of platelet-derived gro...
GO:0051612 P:negative regulation of serotonin uptake
GO:0070495 P:negative regulation of thrombin receptor si...
GO:0032410 P:negative regulation of transporter activity
GO:0045807 P:positive regulation of endocytosis
GO:0060732 P:positive regulation of inositol phosphate b...
GO:0001921 P:positive regulation of receptor recycling
GO:0051281 P:positive regulation of release of sequester...
GO:0031623 P:receptor internalization
GO:0010517 P:regulation of phospholipase activity
GO:0034341 P:response to interferon-gamma
GO:0070555 P:response to interleukin-1
GO:0010040 P:response to iron(II) ion
GO:0032496 P:response to lipopolysaccharide
GO:0032026 P:response to magnesium ion
GO:0048488 P:synaptic vesicle endocytosis

References (18)

[1] “Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease.”  Ueda K.et.al.   8248242
[2] “The NACP/synuclein gene: chromosomal assignment and screening for alterations in Alzheimer disease.”  Campion D.et.al.   7601450
[3] “Tissue-dependent alternative splicing of mRNA for NACP, the precursor of non-A beta component of Alzheimer's disease amyloid.”  Ueda K.et.al.   7802671
[4] “Human and mouse alpha-synuclein genes: comparative genomic sequence analysis and identification of a novel gene regulatory element.”  Touchman J.W.et.al.   11156617
[5] “Complete sequencing and characterization of 21,243 full-length human cDNAs.”  Ota T.et.al.   14702039
[6] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[7] “Constitutive phosphorylation of the Parkinson's disease associated alpha-synuclein.”  Okochi M.et.al.   10617630
[8] “Synucleins are a novel class of substrates for G protein-coupled receptor kinases.”  Pronin A.N.et.al.   10852916
[9] “Alpha-synuclein interacts with phospholipase D isozymes and inhibits pervanadate-induced phospholipase D activation in human embryonic kidney-293 cells.”  Ahn B.H.et.al.   11821392
[10] “Nuclear localization of alpha-synuclein and its interaction with histones.”  Goers J.et.al.   12859192
[11] “Role of alpha-synuclein carboxy-terminus on fibril formation in vitro.”  Murray I.V.et.al.   12859200
[12] “Recent advances on alpha-synuclein cell biology: functions and dysfunctions.”  Alves da Costa C.et.al.   12558071
[13] “Identification and characterization of a novel Pyk2/related adhesion focal tyrosine kinase-associated protein that inhibits alpha-synuclein phosphorylation.”  Takahashi T.et.al.   12893833
[14] “Structure and dynamics of micelle-bound human alpha-synuclein.”  Ulmer T.S.et.al.   15615727
[15] “Mutation in the alpha-synuclein gene identified in families with Parkinson's disease.”  Polymeropoulos M.H.et.al.   9197268
[16] “Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease.”  Krueger R.et.al.   9462735
[17] “The new mutation, E46K, of alpha-synuclein causes Parkinson and Lewy body dementia.”  Zarranz J.J.et.al.   14755719
[18] “Mutation E46K increases phospholipid binding and assembly into filaments of human alpha-synuclein.”  Choi W.et.al.   15498564
Structure:
1XQ8   2JN5   2KKW   2M55   2X6M   3Q25   3Q26   3Q27   3Q28   3Q29   [...more]

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence 
1:	MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK 
61:	EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP 
121:	DNEAYEMPSE EGYQDYEPEA