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Alpha-synuclein

 SYUA_RAT                Reviewed;         140 AA.
P37377; P37378; Q53YM9;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
01-OCT-1994, sequence version 1.
18-JUL-2018, entry version 152.
RecName: Full=Alpha-synuclein;
Name=Snca;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
TISSUE=Brain;
PubMed=1661825; DOI=10.1016/0169-328X(91)90043-W;
Maroteaux L., Scheller R.H.;
"The rat brain synucleins; family of proteins transiently associated
with neuronal membrane.";
Brain Res. Mol. Brain Res. 11:335-343(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SYN2).
PubMed=3411354;
Maroteaux L., Campanelli J.T., Scheller R.H.;
"Synuclein: a neuron-specific protein localized to the nucleus and
presynaptic nerve terminal.";
J. Neurosci. 8:2804-2815(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SYN1).
PubMed=10582622; DOI=10.1046/j.1471-4159.1999.0732586.x;
Kholodilov N.G., Neystat M., Oo T.F., Lo S.E., Larsen K.E., Sulzer D.,
Burke R.E.;
"Increased expression of rat synuclein in the substantia nigra pars
compacta identified by mRNA differential display in a model of
developmental target injury.";
J. Neurochem. 73:2586-2599(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SYN1).
STRAIN=Wistar; TISSUE=Brain;
PubMed=12665621; DOI=10.1073/pnas.0737182100;
Liang T., Spence J., Liu L., Strother W.N., Chang H.W., Ellison J.A.,
Lumeng L., Li T.K., Foroud T., Carr L.G.;
"Alpha-synuclein maps to a quantitative trait locus for alcohol
preference and is differentially expressed in alcohol-preferring and
- nonpreferring rats.";
Proc. Natl. Acad. Sci. U.S.A. 100:4690-4695(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SYN1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 33-97, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
Lubec G., Chen W.-Q.;
Submitted (APR-2007) to UniProtKB.
[7]
UBIQUITINATION, AND INTERACTION WITH UCHL1.
PubMed=12408865; DOI=10.1016/S0092-8674(02)01012-7;
Liu Y., Fallon L., Lashuel H.A., Liu Z., Lansbury P.T. Jr.;
"The UCH-L1 gene encodes two opposing enzymatic activities that affect
alpha-synuclein degradation and Parkinson's disease susceptibility.";
Cell 111:209-218(2002).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: May be involved in the regulation of dopamine release
and transport.
-!- SUBUNIT: Interacts with UCHL1. {ECO:0000269|PubMed:12408865}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:P37840}. Membrane
{ECO:0000250|UniProtKB:P37840}. Nucleus
{ECO:0000250|UniProtKB:P37840}. Cell junction, synapse
{ECO:0000250|UniProtKB:P37840}. Secreted
{ECO:0000250|UniProtKB:P37840}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Additional isoforms seem to exist.;
Name=Syn1;
IsoId=P37377-1; Sequence=Displayed;
Name=Syn2;
IsoId=P37377-2; Sequence=VSP_006367;
Name=Syn3;
IsoId=P37377-3; Sequence=VSP_006365, VSP_006366;
-!- TISSUE SPECIFICITY: Found only in brain (hippocampus, brainstem
and cortex). Specifically expressed in neuronal cell bodies and
synapses.
-!- PTM: Phosphorylated, predominantly on serine residues.
Phosphorylated on Tyr-125 upon osmotic stress (By similarity).
{ECO:0000250}.
-!- PTM: Ubiquitinated. The predominant conjugate is the
diubiquitinated form. {ECO:0000269|PubMed:12408865}.
-!- PTM: Acetylation at Met-1 seems to be important for proper folding
and native oligomeric structure. {ECO:0000250}.
-!- SIMILARITY: Belongs to the synuclein family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; S73007; AAB20688.1; -; mRNA.
EMBL; S73008; AAB20689.1; -; mRNA.
EMBL; S73009; AAB20690.1; -; mRNA.
EMBL; AF007758; AAC16026.1; -; mRNA.
EMBL; AY550005; AAS55694.1; -; mRNA.
EMBL; AY550006; AAS55695.1; -; mRNA.
EMBL; BC087682; AAH87682.1; -; mRNA.
PIR; B43959; B43959.
RefSeq; NP_062042.1; NM_019169.2. [P37377-1]
RefSeq; XP_006236653.1; XM_006236591.3. [P37377-2]
RefSeq; XP_017447989.1; XM_017592500.1. [P37377-2]
UniGene; Rn.1827; -.
ProteinModelPortal; P37377; -.
SMR; P37377; -.
BioGrid; 247897; 79.
IntAct; P37377; 3.
iPTMnet; P37377; -.
PhosphoSitePlus; P37377; -.
World-2DPAGE; 0004:P37377; -.
PeptideAtlas; P37377; -.
PRIDE; P37377; -.
Ensembl; ENSRNOT00000039247; ENSRNOP00000030609; ENSRNOG00000008656. [P37377-1]
GeneID; 29219; -.
KEGG; rno:29219; -.
UCSC; RGD:3729; rat. [P37377-1]
CTD; 6622; -.
RGD; 3729; Snca.
GeneTree; ENSGT00390000016161; -.
HOGENOM; HOG000008691; -.
HOVERGEN; HBG000481; -.
InParanoid; P37377; -.
KO; K04528; -.
OMA; SEAYEMP; -.
OrthoDB; EOG091G11PA; -.
PhylomeDB; P37377; -.
TreeFam; TF332776; -.
PRO; PR:P37377; -.
Proteomes; UP000002494; Chromosome 4.
Bgee; ENSRNOG00000008656; -.
Genevisible; P37377; RN.
GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
GO; GO:0043679; C:axon terminus; IDA:RGD.
GO; GO:0005938; C:cell cortex; IEA:Ensembl.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
GO; GO:0030426; C:growth cone; IDA:RGD.
GO; GO:0016234; C:inclusion body; IEA:Ensembl.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:RGD.
GO; GO:0005758; C:mitochondrial intermembrane space; IDA:RGD.
GO; GO:0005759; C:mitochondrial matrix; IDA:RGD.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005640; C:nuclear outer membrane; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0031092; C:platelet alpha granule membrane; IEA:Ensembl.
GO; GO:0098794; C:postsynapse; IEA:GOC.
GO; GO:0098793; C:presynapse; IDA:RGD.
GO; GO:0005840; C:ribosome; IDA:RGD.
GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
GO; GO:0099512; C:supramolecular fiber; IEA:Ensembl.
GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
GO; GO:0043195; C:terminal bouton; IDA:RGD.
GO; GO:0003779; F:actin binding; IEA:Ensembl.
GO; GO:0043014; F:alpha-tubulin binding; IEA:Ensembl.
GO; GO:0050544; F:arachidonic acid binding; IEA:Ensembl.
GO; GO:0048487; F:beta-tubulin binding; IDA:RGD.
GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
GO; GO:1903136; F:cuprous ion binding; IEA:Ensembl.
GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IEA:Ensembl.
GO; GO:0070840; F:dynein complex binding; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IPI:RGD.
GO; GO:0008198; F:ferrous iron binding; IEA:Ensembl.
GO; GO:0042393; F:histone binding; IEA:Ensembl.
GO; GO:0030544; F:Hsp70 protein binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
GO; GO:0019894; F:kinesin binding; IEA:Ensembl.
GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0016491; F:oxidoreductase activity; IEA:Ensembl.
GO; GO:0043274; F:phospholipase binding; IPI:RGD.
GO; GO:0005543; F:phospholipid binding; IDA:RGD.
GO; GO:0051219; F:phosphoprotein binding; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
GO; GO:0047485; F:protein N-terminus binding; IDA:RGD.
GO; GO:0048156; F:tau protein binding; IEA:Ensembl.
GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0048148; P:behavioral response to cocaine; IMP:RGD.
GO; GO:0071280; P:cellular response to copper ion; IEA:Ensembl.
GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEP:RGD.
GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl.
GO; GO:0042416; P:dopamine biosynthetic process; IEA:Ensembl.
GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl.
GO; GO:0006631; P:fatty acid metabolic process; IEA:Ensembl.
GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
GO; GO:0001774; P:microglial cell activation; IEA:Ensembl.
GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; IEA:Ensembl.
GO; GO:0007006; P:mitochondrial membrane organization; IEA:Ensembl.
GO; GO:1904715; P:negative regulation of chaperone-mediated autophagy; IEA:Ensembl.
GO; GO:0045963; P:negative regulation of dopamine metabolic process; IMP:BHF-UCL.
GO; GO:0051585; P:negative regulation of dopamine uptake involved in synaptic transmission; IEA:Ensembl.
GO; GO:0045920; P:negative regulation of exocytosis; IEA:Ensembl.
GO; GO:0035067; P:negative regulation of histone acetylation; IEA:Ensembl.
GO; GO:0031115; P:negative regulation of microtubule polymerization; IEA:Ensembl.
GO; GO:0032769; P:negative regulation of monooxygenase activity; IEA:Ensembl.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD.
GO; GO:1901215; P:negative regulation of neuron death; IMP:RGD.
GO; GO:0051622; P:negative regulation of norepinephrine uptake; IEA:Ensembl.
GO; GO:0010642; P:negative regulation of platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:BHF-UCL.
GO; GO:0051612; P:negative regulation of serotonin uptake; IEA:Ensembl.
GO; GO:0070495; P:negative regulation of thrombin-activated receptor signaling pathway; IEA:Ensembl.
GO; GO:0032410; P:negative regulation of transporter activity; IEA:Ensembl.
GO; GO:0006638; P:neutral lipid metabolic process; IEA:Ensembl.
GO; GO:0006644; P:phospholipid metabolic process; IEA:Ensembl.
GO; GO:0045807; P:positive regulation of endocytosis; IEA:Ensembl.
GO; GO:1903284; P:positive regulation of glutathione peroxidase activity; IEA:Ensembl.
GO; GO:1903285; P:positive regulation of hydrogen peroxide catabolic process; IEA:Ensembl.
GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
GO; GO:0060732; P:positive regulation of inositol phosphate biosynthetic process; IEA:Ensembl.
GO; GO:1901216; P:positive regulation of neuron death; IEA:Ensembl.
GO; GO:0001956; P:positive regulation of neurotransmitter secretion; IEA:Ensembl.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IEA:Ensembl.
GO; GO:0001921; P:positive regulation of receptor recycling; IEA:Ensembl.
GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
GO; GO:0031623; P:receptor internalization; IEA:Ensembl.
GO; GO:0050812; P:regulation of acyl-CoA biosynthetic process; IEA:Ensembl.
GO; GO:0014059; P:regulation of dopamine secretion; IEA:Ensembl.
GO; GO:0014048; P:regulation of glutamate secretion; IEA:Ensembl.
GO; GO:0040012; P:regulation of locomotion; IEA:Ensembl.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
GO; GO:0043030; P:regulation of macrophage activation; IEA:Ensembl.
GO; GO:1901214; P:regulation of neuron death; IGI:ParkinsonsUK-UCL.
GO; GO:0010517; P:regulation of phospholipase activity; IEA:Ensembl.
GO; GO:1905606; P:regulation of presynapse assembly; IEA:Ensembl.
GO; GO:0022898; P:regulation of transmembrane transporter activity; IEA:Ensembl.
GO; GO:0042220; P:response to cocaine; IEP:RGD.
GO; GO:1904307; P:response to desipramine; IEP:RGD.
GO; GO:0034341; P:response to interferon-gamma; IEA:Ensembl.
GO; GO:0070555; P:response to interleukin-1; IEA:Ensembl.
GO; GO:0010040; P:response to iron(II) ion; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0032026; P:response to magnesium ion; IEA:Ensembl.
GO; GO:0050808; P:synapse organization; IEA:Ensembl.
GO; GO:0001963; P:synaptic transmission, dopaminergic; IEA:Ensembl.
GO; GO:0048488; P:synaptic vesicle endocytosis; IEA:Ensembl.
GO; GO:0048489; P:synaptic vesicle transport; IEA:Ensembl.
InterPro; IPR001058; Synuclein.
InterPro; IPR002460; Synuclein_alpha.
PANTHER; PTHR13820; PTHR13820; 1.
PANTHER; PTHR13820:SF5; PTHR13820:SF5; 1.
Pfam; PF01387; Synuclein; 1.
PRINTS; PR01212; ASYNUCLEIN.
PRINTS; PR01211; SYNUCLEIN.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell junction; Complete proteome;
Copper; Cytoplasm; Direct protein sequencing; Membrane; Metal-binding;
Nucleus; Phosphoprotein; Reference proteome; Repeat; Secreted;
Synapse; Ubl conjugation.
CHAIN 1 140 Alpha-synuclein.
/FTId=PRO_0000184031.
REPEAT 20 30 1.
REPEAT 31 41 2.
REPEAT 42 56 3; approximate.
REPEAT 57 67 4.
REGION 20 67 4 X 11 AA tandem repeats of [EGS]-K-T-K-
[EQ]-[GQ]-V-X(4).
METAL 2 2 Copper. {ECO:0000250}.
METAL 50 50 Copper. {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P37840}.
MOD_RES 125 125 Phosphotyrosine; by FYN.
{ECO:0000250|UniProtKB:P37840}.
MOD_RES 129 129 Phosphoserine; by PLK2.
{ECO:0000250|UniProtKB:P37840}.
VAR_SEQ 42 42 S -> R (in isoform Syn3). {ECO:0000305}.
/FTId=VSP_006365.
VAR_SEQ 43 140 Missing (in isoform Syn3). {ECO:0000305}.
/FTId=VSP_006366.
VAR_SEQ 104 140 EEGYPQEGILEDMPVDPSSEAYEMPSEEGYQDYEPEA ->
YPMGECTNHPPRLIALRVKSRYREHSWRPRKQLSLACVVMD
PFLPT (in isoform Syn2).
{ECO:0000303|PubMed:3411354}.
/FTId=VSP_006367.
SEQUENCE 140 AA; 14515 MW; 1FFD19CD3B9E636C CRC64;
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVTTVAEKTK
EQVTNVGGAV VTGVTAVAQK TVEGAGNIAA ATGFVKKDQM GKGEEGYPQE GILEDMPVDP
SSEAYEMPSE EGYQDYEPEA


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