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SYUA_SERCA
ID   SYUA_SERCA              Reviewed;         143 AA.
AC   Q91448;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Alpha-synuclein;
DE   AltName: Full=Synelfin;
GN   Name=SNCA;
OS   Serinus canaria (Island canary) (Fringilla canaria).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Fringillidae;
OC   Carduelinae; Serinus.
OX   NCBI_TaxID=9135;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=7646890; DOI=10.1016/0896-6273(95)90040-3;
RA   George J.M., Jin H., Woods W.S., Clayton D.F.;
RT   "Characterization of a novel protein regulated during the critical period
RT   for song learning in the zebra finch.";
RL   Neuron 15:361-372(1995).
CC   -!- FUNCTION: May be involved in the regulation of dopamine release and
CC       transport.
CC   -!- FUNCTION: May be involved in neuronal plasticity.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P37840}. Membrane
CC       {ECO:0000250|UniProtKB:P37840}. Nucleus {ECO:0000250|UniProtKB:P37840}.
CC       Synapse {ECO:0000250|UniProtKB:P37840}. Secreted
CC       {ECO:0000250|UniProtKB:P37840}.
CC   -!- TISSUE SPECIFICITY: Brain.
CC   -!- PTM: Acetylation at Met-1 seems to be important for proper folding and
CC       native oligomeric structure. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the synuclein family. {ECO:0000305}.
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DR   EMBL; L33860; AAA93538.1; -; mRNA.
DR   RefSeq; NP_001289028.1; NM_001302099.1.
DR   AlphaFoldDB; Q91448; -.
DR   Ensembl; ENSSCAT00000022424; ENSSCAP00000020085; ENSSCAG00000014487.
DR   GeneID; 103826045; -.
DR   KEGG; scan:103826045; -.
DR   CTD; 6622; -.
DR   GeneTree; ENSGT00950000183175; -.
DR   OMA; VHGVTTX; -.
DR   OrthoDB; 1544450at2759; -.
DR   Proteomes; UP000694409; Unassembled WGS sequence.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0043679; C:axon terminus; IEA:Ensembl.
DR   GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR   GO; GO:0016234; C:inclusion body; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0031092; C:platelet alpha granule membrane; IEA:Ensembl.
DR   GO; GO:0098794; C:postsynapse; IEA:GOC.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0099512; C:supramolecular fiber; IEA:Ensembl.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:Ensembl.
DR   GO; GO:0003779; F:actin binding; IEA:Ensembl.
DR   GO; GO:0043014; F:alpha-tubulin binding; IEA:Ensembl.
DR   GO; GO:0050544; F:arachidonic acid binding; IEA:Ensembl.
DR   GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR   GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR   GO; GO:1903136; F:cuprous ion binding; IEA:Ensembl.
DR   GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IEA:Ensembl.
DR   GO; GO:0070840; F:dynein complex binding; IEA:Ensembl.
DR   GO; GO:0008198; F:ferrous iron binding; IEA:Ensembl.
DR   GO; GO:0042393; F:histone binding; IEA:Ensembl.
DR   GO; GO:0030544; F:Hsp70 protein binding; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0019894; F:kinesin binding; IEA:Ensembl.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:Ensembl.
DR   GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
DR   GO; GO:0051219; F:phosphoprotein binding; IEA:Ensembl.
DR   GO; GO:0000149; F:SNARE binding; IEA:Ensembl.
DR   GO; GO:0048156; F:tau protein binding; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR   GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR   GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR   GO; GO:0071280; P:cellular response to copper ion; IEA:Ensembl.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl.
DR   GO; GO:0042416; P:dopamine biosynthetic process; IEA:Ensembl.
DR   GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:Ensembl.
DR   GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
DR   GO; GO:0001774; P:microglial cell activation; IEA:Ensembl.
DR   GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; IEA:Ensembl.
DR   GO; GO:0007006; P:mitochondrial membrane organization; IEA:Ensembl.
DR   GO; GO:1904715; P:negative regulation of chaperone-mediated autophagy; IEA:Ensembl.
DR   GO; GO:0051585; P:negative regulation of dopamine uptake involved in synaptic transmission; IEA:Ensembl.
DR   GO; GO:0045920; P:negative regulation of exocytosis; IEA:Ensembl.
DR   GO; GO:0035067; P:negative regulation of histone acetylation; IEA:Ensembl.
DR   GO; GO:0031115; P:negative regulation of microtubule polymerization; IEA:Ensembl.
DR   GO; GO:0032769; P:negative regulation of monooxygenase activity; IEA:Ensembl.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0051622; P:negative regulation of norepinephrine uptake; IEA:Ensembl.
DR   GO; GO:0010642; P:negative regulation of platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0051612; P:negative regulation of serotonin uptake; IEA:Ensembl.
DR   GO; GO:0070495; P:negative regulation of thrombin-activated receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0032410; P:negative regulation of transporter activity; IEA:Ensembl.
DR   GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0006638; P:neutral lipid metabolic process; IEA:Ensembl.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:Ensembl.
DR   GO; GO:0045807; P:positive regulation of endocytosis; IEA:Ensembl.
DR   GO; GO:0045921; P:positive regulation of exocytosis; IEA:Ensembl.
DR   GO; GO:1903284; P:positive regulation of glutathione peroxidase activity; IEA:Ensembl.
DR   GO; GO:1903285; P:positive regulation of hydrogen peroxide catabolic process; IEA:Ensembl.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
DR   GO; GO:0060732; P:positive regulation of inositol phosphate biosynthetic process; IEA:Ensembl.
DR   GO; GO:1901216; P:positive regulation of neuron death; IEA:Ensembl.
DR   GO; GO:0001956; P:positive regulation of neurotransmitter secretion; IEA:Ensembl.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR   GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IEA:Ensembl.
DR   GO; GO:0001921; P:positive regulation of receptor recycling; IEA:Ensembl.
DR   GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
DR   GO; GO:0035543; P:positive regulation of SNARE complex assembly; IEA:Ensembl.
DR   GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
DR   GO; GO:0051262; P:protein tetramerization; IEA:Ensembl.
DR   GO; GO:0031623; P:receptor internalization; IEA:Ensembl.
DR   GO; GO:0050812; P:regulation of acyl-CoA biosynthetic process; IEA:Ensembl.
DR   GO; GO:0014059; P:regulation of dopamine secretion; IEA:Ensembl.
DR   GO; GO:0014048; P:regulation of glutamate secretion; IEA:Ensembl.
DR   GO; GO:0040012; P:regulation of locomotion; IEA:Ensembl.
DR   GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
DR   GO; GO:0043030; P:regulation of macrophage activation; IEA:Ensembl.
DR   GO; GO:0010517; P:regulation of phospholipase activity; IEA:Ensembl.
DR   GO; GO:1905606; P:regulation of presynapse assembly; IEA:Ensembl.
DR   GO; GO:0022898; P:regulation of transmembrane transporter activity; IEA:Ensembl.
DR   GO; GO:0034341; P:response to interferon-gamma; IEA:Ensembl.
DR   GO; GO:0070555; P:response to interleukin-1; IEA:Ensembl.
DR   GO; GO:0010040; P:response to iron(II) ion; IEA:Ensembl.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR   GO; GO:0032026; P:response to magnesium ion; IEA:Ensembl.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR   GO; GO:0035493; P:SNARE complex assembly; IEA:Ensembl.
DR   GO; GO:0050808; P:synapse organization; IEA:Ensembl.
DR   GO; GO:0001963; P:synaptic transmission, dopaminergic; IEA:Ensembl.
DR   GO; GO:0048488; P:synaptic vesicle endocytosis; IEA:Ensembl.
DR   GO; GO:0016082; P:synaptic vesicle priming; IEA:Ensembl.
DR   GO; GO:0048489; P:synaptic vesicle transport; IEA:Ensembl.
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; Copper; Cytoplasm; Membrane; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Secreted; Synapse.
FT   CHAIN           1..143
FT                   /note="Alpha-synuclein"
FT                   /id="PRO_0000184033"
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          116..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..143
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"
SQ   SEQUENCE   143 AA;  14874 MW;  9C3AB9C9902C54A7 CRC64;
     MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSRTKEGVVH GVTTVAEKTK
     EQVSNVGGAV VTGVTAVAQK TVEGAGNIAA ATGLVKKDQL AKQNEEGFLQ EGMVNNTGAA
     VDPDNEAYEM PPEEEYQDYE PEA
 
 
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