SYUA_PIG
ID SYUA_PIG Reviewed; 140 AA.
AC Q3I5G7;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Alpha-synuclein;
GN Name=SNCA;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Larsen K., Bendixen C.;
RT "Isolation of the porcine alpha-synuclein gene (SNCA) from cerebellum.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). This chaperone activity is
CC important to sustain normal SNARE-complex assembly during aging (By
CC similarity). Also plays a role in the regulation of the dopamine
CC neurotransmission by associating with the dopamine transporter (DAT1)
CC and thereby modulating its activity (By similarity).
CC {ECO:0000250|UniProtKB:P37840}.
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 (By similarity). Interacts with RPH3A and RAB3A (By
CC similarity). Interacts with SERF1A; this interaction promotes the
CC aggregation of SNCA (By similarity). Interacts with SEPTIN4 (By
CC similarity). {ECO:0000250|UniProtKB:O55042,
CC ECO:0000250|UniProtKB:P37377, ECO:0000250|UniProtKB:P37840}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P37840}.
CC Membrane {ECO:0000250|UniProtKB:P37840}. Nucleus
CC {ECO:0000250|UniProtKB:P37840}. Synapse {ECO:0000250|UniProtKB:P37840}.
CC Secreted {ECO:0000250|UniProtKB:P37840}. Cell projection, axon
CC {ECO:0000250|UniProtKB:O55042}. Note=Membrane-bound in dopaminergic
CC neurons (By similarity). Expressed and colocalized with SEPTIN4 in
CC dopaminergic axon terminals, especially at the varicosities (By
CC similarity). {ECO:0000250|UniProtKB:O55042,
CC ECO:0000250|UniProtKB:P37840}.
CC -!- PTM: Phosphorylated, predominantly on serine residues.
CC {ECO:0000250|UniProtKB:P37840}.
CC -!- PTM: Acetylation at Met-1 seems to be important for proper folding and
CC native oligomeric structure. {ECO:0000250|UniProtKB:P37840}.
CC -!- PTM: Ubiquitinated. The predominant conjugate is the diubiquitinated
CC form. {ECO:0000250|UniProtKB:P37377}.
CC -!- SIMILARITY: Belongs to the synuclein family. {ECO:0000305}.
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DR EMBL; DQ073395; AAZ23150.1; -; mRNA.
DR RefSeq; NP_001032222.1; NM_001037145.1.
DR RefSeq; XP_005667046.1; XM_005666989.2.
DR RefSeq; XP_005667047.1; XM_005666990.1.
DR RefSeq; XP_005667048.1; XM_005666991.2.
DR RefSeq; XP_013834472.1; XM_013979018.1.
DR RefSeq; XP_013834473.1; XM_013979019.1.
DR RefSeq; XP_013834474.1; XM_013979020.1.
DR RefSeq; XP_013834475.1; XM_013979021.1.
DR RefSeq; XP_013834476.1; XM_013979022.1.
DR RefSeq; XP_013834477.1; XM_013979023.1.
DR AlphaFoldDB; Q3I5G7; -.
DR IntAct; Q3I5G7; 1.
DR MINT; Q3I5G7; -.
DR STRING; 9823.ENSSSCP00000009812; -.
DR PaxDb; Q3I5G7; -.
DR PeptideAtlas; Q3I5G7; -.
DR PRIDE; Q3I5G7; -.
DR Ensembl; ENSSSCT00000010077; ENSSSCP00000009812; ENSSSCG00000009203.
DR Ensembl; ENSSSCT00005014538; ENSSSCP00005008658; ENSSSCG00005009534.
DR Ensembl; ENSSSCT00005014573; ENSSSCP00005008690; ENSSSCG00005009534.
DR Ensembl; ENSSSCT00005014602; ENSSSCP00005008712; ENSSSCG00005009534.
DR Ensembl; ENSSSCT00005014605; ENSSSCP00005008714; ENSSSCG00005009534.
DR Ensembl; ENSSSCT00015009339; ENSSSCP00015003727; ENSSSCG00015006869.
DR Ensembl; ENSSSCT00025097849; ENSSSCP00025042999; ENSSSCG00025071166.
DR Ensembl; ENSSSCT00030057605; ENSSSCP00030026173; ENSSSCG00030041450.
DR Ensembl; ENSSSCT00045041478; ENSSSCP00045028787; ENSSSCG00045024277.
DR Ensembl; ENSSSCT00050001298; ENSSSCP00050000342; ENSSSCG00050001043.
DR Ensembl; ENSSSCT00055060116; ENSSSCP00055048172; ENSSSCG00055030213.
DR Ensembl; ENSSSCT00060075237; ENSSSCP00060032494; ENSSSCG00060055210.
DR Ensembl; ENSSSCT00070030805; ENSSSCP00070025698; ENSSSCG00070015592.
DR Ensembl; ENSSSCT00070030816; ENSSSCP00070025706; ENSSSCG00070015592.
DR Ensembl; ENSSSCT00070030829; ENSSSCP00070025714; ENSSSCG00070015592.
DR Ensembl; ENSSSCT00070030833; ENSSSCP00070025718; ENSSSCG00070015592.
DR Ensembl; ENSSSCT00070030837; ENSSSCP00070025722; ENSSSCG00070015592.
DR GeneID; 641350; -.
DR KEGG; ssc:641350; -.
DR CTD; 6622; -.
DR VGNC; VGNC:93285; SNCA.
DR eggNOG; ENOG502S0Q7; Eukaryota.
DR GeneTree; ENSGT00950000183175; -.
DR HOGENOM; CLU_129378_1_0_1; -.
DR InParanoid; Q3I5G7; -.
DR OMA; VHGVTTX; -.
DR OrthoDB; 1544450at2759; -.
DR TreeFam; TF332776; -.
DR Proteomes; UP000008227; Chromosome 8.
DR Proteomes; UP000314985; Chromosome 8.
DR Bgee; ENSSSCG00000009203; Expressed in Ammon's horn and 41 other tissues.
DR ExpressionAtlas; Q3I5G7; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043679; C:axon terminus; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:1903136; F:cuprous ion binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0014059; P:regulation of dopamine secretion; IEA:InterPro.
DR GO; GO:1901214; P:regulation of neuron death; IBA:GO_Central.
DR GO; GO:0050808; P:synapse organization; IBA:GO_Central.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acetylation; Cell projection; Copper; Cytoplasm; Membrane; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Secreted; Synapse;
KW Ubl conjugation.
FT CHAIN 1..140
FT /note="Alpha-synuclein"
FT /id="PRO_0000184029"
FT REGION 98..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 COMPBIAS 116..140
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 87
FT /note="Phosphoserine"
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:0000250|UniProtKB:P37840"
SQ SEQUENCE 140 AA; 14520 MW; 175E2A66B448536C CRC64;
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVTTVAEKTK
EQVTNVGEAV VTGVTAVAQK TVEGAGSIAA ATGFGKKDQL GKNEEGAPQE GILEDMPVDP
DNEAYEMPSE EGYQDYEPEA
