SYUA_MOUSE
ID SYUA_MOUSE Reviewed; 140 AA.
AC O55042; Q3U130; Q9CXF8; Q9EQC3; Q9QUR3;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Alpha-synuclein;
DE AltName: Full=Non-A beta component of AD amyloid;
DE AltName: Full=Non-A4 component of amyloid precursor;
DE Short=NACP;
GN Name=Snca; Synonyms=Syn;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9648883; DOI=10.1046/j.1471-4159.1998.71010338.x;
RA Hsu L.J., Mallory M., Xia Y., Veinbergs I., Hashimoto M., Yoshimoto M.,
RA Thal L.J., Saitoh T., Masliah E.;
RT "Expression pattern of synucleins (non-Abeta component of Alzheimer's
RT disease amyloid precursor protein/alpha-synuclein) during murine brain
RT development.";
RL J. Neurochem. 71:338-344(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=ICR;
RX PubMed=9601701; DOI=10.1097/00001756-199804200-00051;
RA Hong L., Ko H.W., Gwag B.J., Joe E., Lee S., Kim Y.T., Suh Y.-H.;
RT "The cDNA cloning and ontogeny of mouse alpha-synuclein.";
RL NeuroReport 9:1239-1243(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and Sv129/Ola; TISSUE=Brain;
RA Fog J.U., Kallunki P.;
RT "Genomic cloning of the mouse alpha-synuclein and analysis of the
RT promoter.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=11156617; DOI=10.1101/gr.165801;
RA Touchman J.W., Dehejia A., Chiba-Falek O., Cabin D.E., Schwartz J.R.,
RA Orrison B.M., Polymeropoulos M.H., Nussbaum R.L.;
RT "Human and mouse alpha-synuclein genes: comparative genomic sequence
RT analysis and identification of a novel gene regulatory element.";
RL Genome Res. 11:78-86(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Liver, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54.
RC STRAIN=129/SvJ;
RX PubMed=12732244; DOI=10.1016/s0306-4522(03)00036-8;
RA Schlueter O.M., Fornai F., Alessandri M.G., Takamori S., Geppert M.,
RA Jahn R., Suedhof T.C.;
RT "Role of alpha-synuclein in 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-
RT induced parkinsonism in mice.";
RL Neuroscience 118:985-1002(2003).
RN [8]
RP PROTEIN SEQUENCE OF 61-96, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [9]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=10707987; DOI=10.1016/s0896-6273(00)80886-7;
RA Abeliovich A., Schmitz Y., Farinas I., Choi-Lundberg D., Ho W.H.,
RA Castillo P.E., Shinsky N., Verdugo J.M., Armanini M., Ryan A., Hynes M.,
RA Phillips H., Sulzer D., Rosenthal A.;
RT "Mice lacking alpha-synuclein display functional deficits in the
RT nigrostriatal dopamine system.";
RL Neuron 25:239-252(2000).
RN [10]
RP INTERACTION WITH SEPTIN4, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17296554; DOI=10.1016/j.neuron.2007.01.019;
RA Ihara M., Yamasaki N., Hagiwara A., Tanigaki A., Kitano A., Hikawa R.,
RA Tomimoto H., Noda M., Takanashi M., Mori H., Hattori N., Miyakawa T.,
RA Kinoshita M.;
RT "Sept4, a component of presynaptic scaffold and Lewy bodies, is required
RT for the suppression of alpha-synuclein neurotoxicity.";
RL Neuron 53:519-533(2007).
RN [11]
RP PHOSPHORYLATION AT SER-129.
RX PubMed=19004816; DOI=10.1074/jbc.c800206200;
RA Inglis K.J., Chereau D., Brigham E.F., Chiou S.S., Schobel S., Frigon N.L.,
RA Yu M., Caccavello R.J., Nelson S., Motter R., Wright S., Chian D.,
RA Santiago P., Soriano F., Ramos C., Powell K., Goldstein J.M., Babcock M.,
RA Yednock T., Bard F., Basi G.S., Sham H., Chilcote T.J., McConlogue L.,
RA Griswold-Prenner I., Anderson J.P.;
RT "Polo-like kinase 2 (PLK2) phosphorylates alpha-synuclein at serine 129 in
RT central nervous system.";
RL J. Biol. Chem. 284:2598-2602(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP FUNCTION, INTERACTION WITH VAMP2 AND SNAP25, AND DISRUPTION PHENOTYPE.
RX PubMed=20798282; DOI=10.1126/science.1195227;
RA Burre J., Sharma M., Tsetsenis T., Buchman V., Etherton M.R., Suedhof T.C.;
RT "Alpha-synuclein promotes SNARE-complex assembly in vivo and in vitro.";
RL Science 329:1663-1667(2010).
RN [14]
RP FUNCTION, AND SUBUNIT.
RX PubMed=25246573; DOI=10.1073/pnas.1416598111;
RA Burre J., Sharma M., Suedhof T.C.;
RT "alpha-Synuclein assembles into higher-order multimers upon membrane
RT binding to promote SNARE complex formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E4274-E4283(2014).
RN [15]
RP INTERACTION WITH SERF1A, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=31034892; DOI=10.1016/j.jmb.2019.04.031;
RA Merle D.A., Witternigg A., Tam-Amersdorfer C., Hartlmueller C.,
RA Spreitzer E., Schrank E., Wagner-Lichtenegger S., Werzer O., Zangger K.,
RA Kungl A.J., Madl T., Meyer N.H., Falsone S.F.;
RT "Increased Aggregation Tendency of Alpha-Synuclein in a Fully Disordered
RT Protein Complex.";
RL J. Mol. Biol. 431:2581-2598(2019).
CC -!- FUNCTION: Neuronal protein that plays several roles in synaptic
CC activity such as regulation of synaptic vesicle trafficking and
CC subsequent neurotransmitter release (By similarity). Participates as a
CC monomer in synaptic vesicle exocytosis by enhancing vesicle priming,
CC fusion and dilation of exocytotic fusion pores (By similarity).
CC Mechanistically, acts by increasing local Ca(2+) release from
CC microdomains which is essential for the enhancement of ATP-induced
CC exocytosis (By similarity). Acts also as a molecular chaperone in its
CC multimeric membrane-bound state, assisting in the folding of synaptic
CC fusion components called SNAREs (Soluble NSF Attachment Protein
CC REceptors) at presynaptic plasma membrane in conjunction with cysteine
CC string protein-alpha/DNAJC5 (PubMed:20798282, PubMed:25246573). This
CC chaperone activity is important to sustain normal SNARE-complex
CC assembly during aging (By similarity). Also plays a role in the
CC regulation of the dopamine neurotransmission by associating with the
CC dopamine transporter (DAT1) and thereby modulating its activity (By
CC similarity). {ECO:0000250|UniProtKB:P37840,
CC ECO:0000269|PubMed:20798282, ECO:0000269|PubMed:25246573}.
CC -!- SUBUNIT: Soluble monomer. Homotetramer. A dynamic intracellular
CC population of tetramers and monomers coexists normally and the tetramer
CC plays an essential role in maintaining homeostasis (By similarity).
CC Interacts with UCHL1 (By similarity). Interacts with phospholipase D
CC and histones. Interacts (via N-terminus) with synphilin-1/SNCAIP; this
CC interaction promotes formation of SNCA inclusions in the cytoplasm.
CC Interacts with CALM1. Interacts with STXBP1; this interaction controls
CC SNCA self-replicating aggregation. Interacts with SNARE components
CC VAMP2 and SNAP25; these interactions allows SNARE complex assembly and
CC integrity (PubMed:20798282, PubMed:25246573). Interacts with RPH3A and
CC RAB3A (By similarity). Interacts with SERF1A; this interaction promotes
CC the aggregation of SNCA (By similarity). Interacts with SEPTIN4
CC (PubMed:17296554). {ECO:0000250|UniProtKB:P37377,
CC ECO:0000250|UniProtKB:P37840, ECO:0000269|PubMed:17296554,
CC ECO:0000269|PubMed:20798282, ECO:0000269|PubMed:25246573}.
CC -!- INTERACTION:
CC O55042; P00520: Abl1; NbExp=2; IntAct=EBI-2310271, EBI-914519;
CC O55042; P55258: Rab8a; NbExp=2; IntAct=EBI-2310271, EBI-398411;
CC O55042; Q61327: Slc6a3; NbExp=5; IntAct=EBI-2310271, EBI-7839708;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:31034892}. Membrane
CC {ECO:0000250|UniProtKB:P37840}. Nucleus {ECO:0000250|UniProtKB:P37840}.
CC Synapse {ECO:0000250|UniProtKB:P37840}. Secreted
CC {ECO:0000250|UniProtKB:P37840}. Cell projection, axon
CC {ECO:0000269|PubMed:17296554}. Note=Membrane-bound in dopaminergic
CC neurons (By similarity). Expressed and colocalized with SEPTIN4 in
CC dopaminergic axon terminals, especially at the varicosities
CC (PubMed:17296554). {ECO:0000250|UniProtKB:P37840,
CC ECO:0000269|PubMed:17296554}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O55042-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O55042-2; Sequence=VSP_025018, VSP_025019;
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level)
CC (PubMed:31034892). Expressed in the striatum (at protein level)
CC (PubMed:17296554). Highly expressed in presynaptic terminals in the
CC central nervous system (PubMed:10707987). {ECO:0000269|PubMed:10707987,
CC ECO:0000269|PubMed:17296554, ECO:0000269|PubMed:31034892}.
CC -!- PTM: Phosphorylated, predominantly on serine residues. Phosphorylated
CC on Tyr-125 upon osmotic stress. {ECO:0000250|UniProtKB:P37840}.
CC -!- PTM: Ubiquitinated. The predominant conjugate is the diubiquitinated
CC form. {ECO:0000250|UniProtKB:P37377}.
CC -!- PTM: Acetylation at Met-1 seems to be important for proper folding and
CC native oligomeric structure. {ECO:0000250|UniProtKB:P37840}.
CC -!- DISRUPTION PHENOTYPE: Snca-deficient mice are viable and fertile,
CC possess intact brain architecture but exhibit decreased striatal
CC dopamin content and amphetamine sensitivity (PubMed:10707987).
CC Simultaneous knockout of SNCA, SNCB and SNCG exhibit an age-dependent
CC decrease in SNARE-complex assembly. Thus, synucleins are required for
CC maintaining normal SNARE-complex assembly during aging in mice
CC (PubMed:20798282). {ECO:0000269|PubMed:10707987,
CC ECO:0000269|PubMed:20798282}.
CC -!- SIMILARITY: Belongs to the synuclein family. {ECO:0000305}.
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DR EMBL; AF044672; AAC00521.1; -; mRNA.
DR EMBL; AF033261; AAD11254.1; -; mRNA.
DR EMBL; AF179273; AAD56908.1; -; mRNA.
DR EMBL; AF179272; AAD56907.1; -; Genomic_DNA.
DR EMBL; AF179268; AAD56907.1; JOINED; Genomic_DNA.
DR EMBL; AF179269; AAD56907.1; JOINED; Genomic_DNA.
DR EMBL; AF179270; AAD56907.1; JOINED; Genomic_DNA.
DR EMBL; AF179271; AAD56907.1; JOINED; Genomic_DNA.
DR EMBL; AF163865; AAG30304.1; -; Genomic_DNA.
DR EMBL; AK014472; BAB29375.1; -; mRNA.
DR EMBL; AK156316; BAE33670.1; -; mRNA.
DR EMBL; BC046764; AAH46764.1; -; mRNA.
DR EMBL; AF277451; AAG44833.1; -; Genomic_DNA.
DR CCDS; CCDS20201.1; -. [O55042-1]
DR RefSeq; NP_001035916.1; NM_001042451.2. [O55042-1]
DR RefSeq; NP_033247.1; NM_009221.2. [O55042-1]
DR AlphaFoldDB; O55042; -.
DR BMRB; O55042; -.
DR BioGRID; 203365; 34.
DR CORUM; O55042; -.
DR IntAct; O55042; 10.
DR MINT; O55042; -.
DR STRING; 10090.ENSMUSP00000109907; -.
DR iPTMnet; O55042; -.
DR PhosphoSitePlus; O55042; -.
DR CPTAC; non-CPTAC-3949; -.
DR MaxQB; O55042; -.
DR PaxDb; O55042; -.
DR PeptideAtlas; O55042; -.
DR PRIDE; O55042; -.
DR ProteomicsDB; 254757; -. [O55042-1]
DR ProteomicsDB; 254758; -. [O55042-2]
DR ABCD; O55042; 1 sequenced antibody.
DR Antibodypedia; 14688; 3113 antibodies from 55 providers.
DR DNASU; 20617; -.
DR Ensembl; ENSMUST00000114268; ENSMUSP00000109907; ENSMUSG00000025889. [O55042-1]
DR Ensembl; ENSMUST00000163779; ENSMUSP00000126067; ENSMUSG00000025889. [O55042-1]
DR GeneID; 20617; -.
DR KEGG; mmu:20617; -.
DR UCSC; uc009cdn.2; mouse. [O55042-1]
DR UCSC; uc009cdp.2; mouse. [O55042-2]
DR CTD; 6622; -.
DR MGI; MGI:1277151; Snca.
DR VEuPathDB; HostDB:ENSMUSG00000025889; -.
DR eggNOG; ENOG502S0Q7; Eukaryota.
DR GeneTree; ENSGT00950000183175; -.
DR HOGENOM; CLU_129378_1_0_1; -.
DR InParanoid; O55042; -.
DR OMA; VHGVTTX; -.
DR OrthoDB; 1544450at2759; -.
DR PhylomeDB; O55042; -.
DR TreeFam; TF332776; -.
DR BioGRID-ORCS; 20617; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Snca; mouse.
DR PRO; PR:O55042; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; O55042; protein.
DR Bgee; ENSMUSG00000025889; Expressed in dentate gyrus of hippocampal formation granule cell and 227 other tissues.
DR Genevisible; O55042; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0043679; C:axon terminus; IDA:UniProtKB.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0016234; C:inclusion body; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; IMP:ParkinsonsUK-UCL.
DR GO; GO:0005640; C:nuclear outer membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0031092; C:platelet alpha granule membrane; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005840; C:ribosome; ISO:MGI.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
DR GO; GO:0099512; C:supramolecular fiber; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0043014; F:alpha-tubulin binding; ISO:MGI.
DR GO; GO:0050544; F:arachidonic acid binding; IDA:MGI.
DR GO; GO:0048487; F:beta-tubulin binding; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:1903136; F:cuprous ion binding; ISO:MGI.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0070840; F:dynein complex binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0008198; F:ferrous iron binding; ISO:MGI.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR GO; GO:0019894; F:kinesin binding; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0016491; F:oxidoreductase activity; ISO:MGI.
DR GO; GO:0043274; F:phospholipase binding; ISO:MGI.
DR GO; GO:0005543; F:phospholipid binding; ISO:MGI.
DR GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0000149; F:SNARE binding; ISO:MGI.
DR GO; GO:0048156; F:tau protein binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0008344; P:adult locomotory behavior; IGI:MGI.
DR GO; GO:0048148; P:behavioral response to cocaine; ISO:MGI.
DR GO; GO:0071280; P:cellular response to copper ion; ISO:MGI.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IGI:MGI.
DR GO; GO:0042416; P:dopamine biosynthetic process; IMP:MGI.
DR GO; GO:0042417; P:dopamine metabolic process; IGI:MGI.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IMP:MGI.
DR GO; GO:0006631; P:fatty acid metabolic process; IMP:MGI.
DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI.
DR GO; GO:0061024; P:membrane organization; IMP:MGI.
DR GO; GO:0001774; P:microglial cell activation; IMP:MGI.
DR GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; IMP:MGI.
DR GO; GO:0007006; P:mitochondrial membrane organization; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:1904715; P:negative regulation of chaperone-mediated autophagy; ISO:MGI.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0045963; P:negative regulation of dopamine metabolic process; ISO:MGI.
DR GO; GO:0051585; P:negative regulation of dopamine uptake involved in synaptic transmission; ISO:MGI.
DR GO; GO:0045920; P:negative regulation of exocytosis; ISO:MGI.
DR GO; GO:0035067; P:negative regulation of histone acetylation; ISO:MGI.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; ISO:MGI.
DR GO; GO:0032769; P:negative regulation of monooxygenase activity; ISO:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IGI:MGI.
DR GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
DR GO; GO:0051622; P:negative regulation of norepinephrine uptake; ISO:MGI.
DR GO; GO:0010642; P:negative regulation of platelet-derived growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0051612; P:negative regulation of serotonin uptake; ISO:MGI.
DR GO; GO:0070495; P:negative regulation of thrombin-activated receptor signaling pathway; ISO:MGI.
DR GO; GO:0032410; P:negative regulation of transporter activity; ISO:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
DR GO; GO:0007269; P:neurotransmitter secretion; IDA:MGI.
DR GO; GO:0006638; P:neutral lipid metabolic process; IMP:MGI.
DR GO; GO:0006644; P:phospholipid metabolic process; IMP:MGI.
DR GO; GO:0045807; P:positive regulation of endocytosis; ISO:MGI.
DR GO; GO:0045921; P:positive regulation of exocytosis; ISO:MGI.
DR GO; GO:1903284; P:positive regulation of glutathione peroxidase activity; ISO:MGI.
DR GO; GO:1903285; P:positive regulation of hydrogen peroxide catabolic process; ISO:MGI.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISO:MGI.
DR GO; GO:0060732; P:positive regulation of inositol phosphate biosynthetic process; ISO:MGI.
DR GO; GO:1901216; P:positive regulation of neuron death; ISO:MGI.
DR GO; GO:0001956; P:positive regulation of neurotransmitter secretion; IDA:MGI.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:BHF-UCL.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0001921; P:positive regulation of receptor recycling; ISO:MGI.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISO:MGI.
DR GO; GO:0035543; P:positive regulation of SNARE complex assembly; ISO:MGI.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; IMP:MGI.
DR GO; GO:0051259; P:protein complex oligomerization; IDA:UniProtKB.
DR GO; GO:0031648; P:protein destabilization; ISO:MGI.
DR GO; GO:0051262; P:protein tetramerization; ISO:MGI.
DR GO; GO:0031623; P:receptor internalization; ISO:MGI.
DR GO; GO:0050812; P:regulation of acyl-CoA biosynthetic process; IDA:MGI.
DR GO; GO:0014059; P:regulation of dopamine secretion; IGI:MGI.
DR GO; GO:0014048; P:regulation of glutamate secretion; IMP:MGI.
DR GO; GO:0040012; P:regulation of locomotion; IMP:MGI.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:MGI.
DR GO; GO:0043030; P:regulation of macrophage activation; IMP:MGI.
DR GO; GO:1901214; P:regulation of neuron death; ISO:MGI.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IMP:MGI.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; IMP:MGI.
DR GO; GO:0051621; P:regulation of norepinephrine uptake; ISO:MGI.
DR GO; GO:0010517; P:regulation of phospholipase activity; ISO:MGI.
DR GO; GO:1905606; P:regulation of presynapse assembly; ISO:MGI.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IMP:ParkinsonsUK-UCL.
DR GO; GO:0022898; P:regulation of transmembrane transporter activity; ISO:MGI.
DR GO; GO:0034341; P:response to interferon-gamma; ISO:MGI.
DR GO; GO:0070555; P:response to interleukin-1; ISO:MGI.
DR GO; GO:0010040; P:response to iron(II) ion; ISO:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:MGI.
DR GO; GO:0032026; P:response to magnesium ion; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
DR GO; GO:0035493; P:SNARE complex assembly; IDA:UniProtKB.
DR GO; GO:0050808; P:synapse organization; IGI:MGI.
DR GO; GO:0001963; P:synaptic transmission, dopaminergic; IMP:MGI.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:SynGO.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; ISO:MGI.
DR GO; GO:0016082; P:synaptic vesicle priming; ISO:MGI.
DR GO; GO:0048489; P:synaptic vesicle transport; IMP:MGI.
DR InterPro; IPR001058; Synuclein.
DR InterPro; IPR002460; Synuclein_alpha.
DR PANTHER; PTHR13820; PTHR13820; 1.
DR PANTHER; PTHR13820:SF5; PTHR13820:SF5; 1.
DR Pfam; PF01387; Synuclein; 1.
DR PRINTS; PR01212; ASYNUCLEIN.
DR PRINTS; PR01211; SYNUCLEIN.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection; Copper; Cytoplasm;
KW Direct protein sequencing; Membrane; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Synapse;
KW Ubl conjugation.
FT CHAIN 1..140
FT /note="Alpha-synuclein"
FT /id="PRO_0000184026"
FT REPEAT 20..30
FT /note="1"
FT REPEAT 31..41
FT /note="2"
FT REPEAT 42..56
FT /note="3; approximate"
FT REPEAT 57..67
FT /note="4"
FT REGION 20..67
FT /note="4 X 11 AA tandem repeats of [EGS]-K-T-K-[EQ]-[GQ]-V-
FT X(4)"
FT REGION 99..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..140
FT /note="Interaction with SERF1A"
FT /evidence="ECO:0000250|UniProtKB:P37840"
FT BINDING 2
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P37840"
FT MOD_RES 125
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000250|UniProtKB:P37840"
FT MOD_RES 129
FT /note="Phosphoserine; by PLK2"
FT /evidence="ECO:0000269|PubMed:19004816"
FT VAR_SEQ 103..121
FT /note="GEEGYPQEGILEDMPVDPG -> VWLPVLCSVITLDTMSLHA (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025018"
FT VAR_SEQ 122..140
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025019"
FT CONFLICT 58
FT /note="K -> T (in Ref. 1; AAC00521)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 140 AA; 14485 MW; 1FFD19D7E15E636C CRC64;
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVTTVAEKTK
EQVTNVGGAV VTGVTAVAQK TVEGAGNIAA ATGFVKKDQM GKGEEGYPQE GILEDMPVDP
GSEAYEMPSE EGYQDYEPEA
