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O55042 (SYUA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-synuclein
Alternative name(s):
Non-A beta component of AD amyloid
Non-A4 component of amyloid precursor
Short name=NACP
Gene names
Name:Snca
Synonyms:Syn
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length140 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in the regulation of dopamine release and transport.

Subunit structure

Interacts with UCHL1 By similarity.

Subcellular location

Cytoplasm By similarity.

Post-translational modification

Phosphorylated, predominantly on serine residues. Phosphorylated on Tyr-125 upon osmotic stress By similarity. Ref.9

Ubiquitinated. The predominant conjugate is the diubiquitinated form By similarity.

Acetylation at Met-1 seems to be important for proper folding and native oligomeric structure By similarity.

Sequence similarities

Belongs to the synuclein family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandCopper
Metal-binding
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

adult locomotory behavior

Inferred from genetic interaction PubMed 18333965. Source: MGI

aging

Inferred from electronic annotation. Source: Ensembl

behavioral response to cocaine

Inferred from electronic annotation. Source: Ensembl

cellular response to copper ion

Inferred from electronic annotation. Source: Ensembl

cellular response to fibroblast growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to oxidative stress

Inferred from mutant phenotype PubMed 16298531. Source: MGI

dopamine biosynthetic process

Inferred from mutant phenotype PubMed 10707987. Source: MGI

dopamine metabolic process

Inferred from genetic interaction PubMed 15465911. Source: MGI

fatty acid metabolic process

Inferred from mutant phenotype PubMed 14507911PubMed 17250686. Source: MGI

long-term synaptic potentiation

Inferred from mutant phenotype PubMed 17689254. Source: MGI

membrane organization

Inferred from mutant phenotype PubMed 14507911. Source: MGI

microglial cell activation

Inferred from mutant phenotype PubMed 17035541. Source: MGI

mitochondrial ATP synthesis coupled electron transport

Inferred from mutant phenotype PubMed 16260631. Source: MGI

mitochondrial membrane organization

Inferred from mutant phenotype PubMed 16260631. Source: MGI

negative regulation of dopamine metabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of dopamine uptake involved in synaptic transmission

Inferred from electronic annotation. Source: Ensembl

negative regulation of exocytosis

Inferred from electronic annotation. Source: Ensembl

negative regulation of histone acetylation

Inferred from electronic annotation. Source: Ensembl

negative regulation of microtubule polymerization

Inferred from electronic annotation. Source: Ensembl

negative regulation of monooxygenase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron apoptotic process

Inferred from genetic interaction PubMed 16269331. Source: MGI

negative regulation of norepinephrine uptake

Inferred from electronic annotation. Source: Ensembl

negative regulation of platelet-derived growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

negative regulation of serotonin uptake

Inferred from electronic annotation. Source: Ensembl

negative regulation of thrombin receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of transporter activity

Inferred from electronic annotation. Source: Ensembl

neutral lipid metabolic process

Inferred from mutant phenotype PubMed 17250686. Source: MGI

phospholipid metabolic process

Inferred from mutant phenotype PubMed 15938614PubMed 16260631PubMed 16734431. Source: MGI

positive regulation of endocytosis

Inferred from electronic annotation. Source: Ensembl

positive regulation of inositol phosphate biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of neurotransmitter secretion

Inferred from direct assay PubMed 15510220. Source: MGI

positive regulation of peptidyl-serine phosphorylation

Inferred from mutant phenotype PubMed 21127069. Source: BHF-UCL

positive regulation of protein serine/threonine kinase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of receptor recycling

Inferred from electronic annotation. Source: Ensembl

positive regulation of release of sequestered calcium ion into cytosol

Inferred from electronic annotation. Source: Ensembl

positive regulation of synaptic transmission

Inferred from mutant phenotype PubMed 15579163. Source: MGI

protein destabilization

Inferred from electronic annotation. Source: Ensembl

receptor internalization

Inferred from electronic annotation. Source: Ensembl

regulation of acyl-CoA biosynthetic process

Inferred from direct assay PubMed 16734431. Source: MGI

regulation of dopamine secretion

Inferred from genetic interaction PubMed 18333965. Source: MGI

regulation of excitatory postsynaptic membrane potential

Inferred from mutant phenotype PubMed 17610578. Source: MGI

regulation of glutamate secretion

Inferred from mutant phenotype PubMed 17689254. Source: MGI

regulation of locomotion

Inferred from mutant phenotype PubMed 10707987. Source: MGI

regulation of long-term neuronal synaptic plasticity

Inferred from mutant phenotype PubMed 15510220. Source: MGI

regulation of macrophage activation

Inferred from mutant phenotype PubMed 17035541. Source: MGI

regulation of neuronal synaptic plasticity

Inferred from mutant phenotype PubMed 17610578. Source: MGI

regulation of neurotransmitter secretion

Inferred from mutant phenotype PubMed 10707987PubMed 12388586PubMed 15510220. Source: MGI

regulation of phospholipase activity

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from mutant phenotype PubMed 10707987. Source: MGI

response to interferon-gamma

Inferred from electronic annotation. Source: Ensembl

response to interleukin-1

Inferred from electronic annotation. Source: Ensembl

response to iron(II) ion

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to magnesium ion

Inferred from electronic annotation. Source: Ensembl

synapse organization

Inferred from genetic interaction PubMed 20974939. Source: MGI

synaptic transmission

Inferred from genetic interaction PubMed 20974939. Source: MGI

synaptic transmission, dopaminergic

Inferred from mutant phenotype PubMed 10707987PubMed 12388586. Source: MGI

synaptic vesicle endocytosis

Inferred from mutant phenotype PubMed 18980610. Source: UniProtKB

synaptic vesicle transport

Inferred from mutant phenotype PubMed 12388586. Source: MGI

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

actin cytoskeleton

Inferred from electronic annotation. Source: Ensembl

cell cortex

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 20457918. Source: BHF-UCL

cytoskeleton

Inferred from direct assay PubMed 17077307. Source: MGI

cytosol

Inferred from direct assay PubMed 18980610. Source: UniProtKB

fibril

Inferred from electronic annotation. Source: Ensembl

growth cone

Inferred from electronic annotation. Source: Ensembl

inclusion body

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nuclear outer membrane

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 16959795. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 17475220. Source: MGI

platelet alpha granule membrane

Inferred from electronic annotation. Source: Ensembl

ribosome

Inferred from electronic annotation. Source: Ensembl

rough endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

synapse

Inferred from direct assay PubMed 10964942. Source: MGI

synaptic vesicle

Inferred from electronic annotation. Source: Ensembl

terminal bouton

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionarachidonic acid binding

Inferred from direct assay PubMed 16734431. Source: MGI

calcium ion binding

Inferred from electronic annotation. Source: Ensembl

copper ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

cysteine-type endopeptidase inhibitor activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

ferrous iron binding

Inferred from electronic annotation. Source: Ensembl

histone binding

Inferred from direct assay PubMed 16959795. Source: UniProtKB

identical protein binding

Inferred from direct assay PubMed 10978144. Source: MGI

magnesium ion binding

Inferred from electronic annotation. Source: Ensembl

oxidoreductase activity

Inferred from electronic annotation. Source: Ensembl

phospholipid binding

Inferred from electronic annotation. Source: Ensembl

zinc ion binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Slc6a3Q613275EBI-2310271,EBI-7839708
YwhahP685102EBI-2310271,EBI-444641

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O55042-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O55042-2)

The sequence of this isoform differs from the canonical sequence as follows:
     103-121: GEEGYPQEGILEDMPVDPG → VWLPVLCSVITLDTMSLHA
     122-140: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 140140Alpha-synuclein
PRO_0000184026

Regions

Repeat20 – 30111
Repeat31 – 41112
Repeat42 – 56153; approximate
Repeat57 – 67114
Region20 – 67484 X 11 AA tandem repeats of [EGS]-K-T-K-[EQ]-[GQ]-V-X(4)

Sites

Metal binding21Copper By similarity
Metal binding501Copper By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue1251Phosphotyrosine; by FYN By similarity
Modified residue1291Phosphoserine; by PLK2 Ref.9

Natural variations

Alternative sequence103 – 12119GEEGY…PVDPG → VWLPVLCSVITLDTMSLHA in isoform 2.
VSP_025018
Alternative sequence122 – 14019Missing in isoform 2.
VSP_025019

Experimental info

Sequence conflict581K → T in AAC00521. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 27, 2001. Version 2.
Checksum: 1FFD19D7E15E636C

FASTA14014,485
        10         20         30         40         50         60 
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVTTVAEKTK 

        70         80         90        100        110        120 
EQVTNVGGAV VTGVTAVAQK TVEGAGNIAA ATGFVKKDQM GKGEEGYPQE GILEDMPVDP 

       130        140 
GSEAYEMPSE EGYQDYEPEA 

« Hide

Isoform 2 [UniParc].

Checksum: 03CAFC4944C78D63
Show »

FASTA12112,345

References

« Hide 'large scale' references
[1]"Expression pattern of synucleins (non-Abeta component of Alzheimer's disease amyloid precursor protein/alpha-synuclein) during murine brain development."
Hsu L.J., Mallory M., Xia Y., Veinbergs I., Hashimoto M., Yoshimoto M., Thal L.J., Saitoh T., Masliah E.
J. Neurochem. 71:338-344(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"The cDNA cloning and ontogeny of mouse alpha-synuclein."
Hong L., Ko H.W., Gwag B.J., Joe E., Lee S., Kim Y.T., Suh Y.-H.
NeuroReport 9:1239-1243(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: ICR.
[3]"Genomic cloning of the mouse alpha-synuclein and analysis of the promoter."
Fog J.U., Kallunki P.
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
Strain: C57BL/6J and Sv129/Ola.
Tissue: Brain.
[4]"Human and mouse alpha-synuclein genes: comparative genomic sequence analysis and identification of a novel gene regulatory element."
Touchman J.W., Dehejia A., Chiba-Falek O., Cabin D.E., Schwartz J.R., Orrison B.M., Polymeropoulos M.H., Nussbaum R.L.
Genome Res. 11:78-86(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/SvJ.
[5]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6J and NOD.
Tissue: Liver and Spleen.
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6.
Tissue: Brain.
[7]"Role of alpha-synuclein in 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced parkinsonism in mice."
Schlueter O.M., Fornai F., Alessandri M.G., Takamori S., Geppert M., Jahn R., Suedhof T.C.
Neuroscience 118:985-1002(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54.
Strain: 129/SvJ.
[8]Lubec G., Klug S.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 61-96, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Hippocampus.
[9]"Polo-like kinase 2 (PLK2) phosphorylates alpha-synuclein at serine 129 in central nervous system."
Inglis K.J., Chereau D., Brigham E.F., Chiou S.S., Schobel S., Frigon N.L., Yu M., Caccavello R.J., Nelson S., Motter R., Wright S., Chian D., Santiago P., Soriano F., Ramos C., Powell K., Goldstein J.M., Babcock M. expand/collapse author list , Yednock T., Bard F., Basi G.S., Sham H., Chilcote T.J., McConlogue L., Griswold-Prenner I., Anderson J.P.
J. Biol. Chem. 284:2598-2602(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-129.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF044672 mRNA. Translation: AAC00521.1.
AF033261 mRNA. Translation: AAD11254.1.
AF179273 mRNA. Translation: AAD56908.1.
AF179272 expand/collapse EMBL AC list , AF179268, AF179269, AF179270, AF179271 Genomic DNA. Translation: AAD56907.1.
AF163865 Genomic DNA. Translation: AAG30304.1.
AK014472 mRNA. Translation: BAB29375.1.
AK156316 mRNA. Translation: BAE33670.1.
BC046764 mRNA. Translation: AAH46764.1.
AF277451 Genomic DNA. Translation: AAG44833.1.
RefSeqNP_001035916.1. NM_001042451.2.
NP_033247.1. NM_009221.2.
UniGeneMm.17484.

3D structure databases

ProteinModelPortalO55042.
SMRO55042. Positions 1-140.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203365. 17 interactions.
IntActO55042. 5 interactions.
MINTMINT-2736846.

PTM databases

PhosphoSiteO55042.

Proteomic databases

PaxDbO55042.
PRIDEO55042.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000114268; ENSMUSP00000109907; ENSMUSG00000025889. [O55042-1]
ENSMUST00000163779; ENSMUSP00000126067; ENSMUSG00000025889. [O55042-1]
GeneID20617.
KEGGmmu:20617.
UCSCuc009cdn.1. mouse. [O55042-1]
uc009cdp.1. mouse. [O55042-2]

Organism-specific databases

CTD6622.
MGIMGI:1277151. Snca.

Phylogenomic databases

eggNOGNOG44393.
GeneTreeENSGT00390000016161.
HOGENOMHOG000008691.
HOVERGENHBG000481.
InParanoidO55042.
KOK04528.
OMASEAYEMP.
OrthoDBEOG7034KG.
PhylomeDBO55042.
TreeFamTF332776.

Gene expression databases

BgeeO55042.
CleanExMM_SNCA.
GenevestigatorO55042.

Family and domain databases

Gene3D1.10.287.700. 1 hit.
InterProIPR001058. Synuclein.
IPR002460. Synuclein_alpha.
[Graphical view]
PANTHERPTHR13820. PTHR13820. 1 hit.
PfamPF01387. Synuclein. 1 hit.
[Graphical view]
PRINTSPR01212. ASYNUCLEIN.
PR01211. SYNUCLEIN.
ProtoNetSearch...

Other

NextBio298995.
PMAP-CutDBO55042.
PROO55042.
SOURCESearch...

Entry information

Entry nameSYUA_MOUSE
AccessionPrimary (citable) accession number: O55042
Secondary accession number(s): Q3U130 expand/collapse secondary AC list , Q9CXF8, Q9EQC3, Q9QUR3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: April 27, 2001
Last modified: April 16, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot