SYUB_MOUSE
ID SYUB_MOUSE Reviewed; 133 AA.
AC Q91ZZ3;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Beta-synuclein;
GN Name=Sncb;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=11474193; DOI=10.1159/000056962;
RA Sopher B.L., Koszdin K.L., McClain M.E., Myrick S.B., Martinez R.A.,
RA Smith A.C., La Spada A.R.;
RT "Genomic organization, chromosome location, and expression analysis of
RT mouse beta-synuclein, a candidate for involvement in neurodegeneration.";
RL Cytogenet. Cell Genet. 93:117-123(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [3]
RP PROTEIN SEQUENCE OF 60-84, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Testis;
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 [5]
RP 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).
CC -!- FUNCTION: May be involved in neuronal plasticity. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the brain.
CC {ECO:0000269|PubMed:11474193}.
CC -!- PTM: Phosphorylated. Phosphorylation by G-protein coupled receptor
CC kinases (GRK) is more efficient than phosphorylation by CK1, CK2 and
CC CaM-kinase II (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Simultaneous knockout of SNCA, SNCB and SNCG
CC exhibit an age-dependent decrease in SNARE-complex assembly. Thus,
CC synucleins are required for maintaining normal SNARE-complex assembly
CC during aging in mice. {ECO:0000269|PubMed:20798282}.
CC -!- SIMILARITY: Belongs to the synuclein family. {ECO:0000305}.
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DR EMBL; AF348164; AAK83238.1; -; Genomic_DNA.
DR EMBL; AF348162; AAK83238.1; JOINED; Genomic_DNA.
DR EMBL; AF348163; AAK83238.1; JOINED; Genomic_DNA.
DR EMBL; BC019409; AAH19409.1; -; mRNA.
DR CCDS; CCDS36670.1; -.
DR RefSeq; NP_291088.1; NM_033610.2.
DR RefSeq; XP_006517078.1; XM_006517015.3.
DR RefSeq; XP_006517079.1; XM_006517016.3.
DR AlphaFoldDB; Q91ZZ3; -.
DR BMRB; Q91ZZ3; -.
DR BioGRID; 222330; 5.
DR STRING; 10090.ENSMUSP00000043074; -.
DR iPTMnet; Q91ZZ3; -.
DR PhosphoSitePlus; Q91ZZ3; -.
DR UCD-2DPAGE; Q91ZZ3; -.
DR MaxQB; Q91ZZ3; -.
DR PaxDb; Q91ZZ3; -.
DR PeptideAtlas; Q91ZZ3; -.
DR PRIDE; Q91ZZ3; -.
DR ProteomicsDB; 254759; -.
DR Antibodypedia; 3634; 368 antibodies from 40 providers.
DR DNASU; 104069; -.
DR Ensembl; ENSMUST00000036825; ENSMUSP00000043074; ENSMUSG00000034891.
DR Ensembl; ENSMUST00000134110; ENSMUSP00000116296; ENSMUSG00000034891.
DR GeneID; 104069; -.
DR KEGG; mmu:104069; -.
DR UCSC; uc007qpc.1; mouse.
DR CTD; 6620; -.
DR MGI; MGI:1889011; Sncb.
DR VEuPathDB; HostDB:ENSMUSG00000034891; -.
DR eggNOG; ENOG502S0N5; Eukaryota.
DR GeneTree; ENSGT00950000183175; -.
DR HOGENOM; CLU_129378_1_0_1; -.
DR InParanoid; Q91ZZ3; -.
DR OMA; AYDENQQ; -.
DR OrthoDB; 1544450at2759; -.
DR PhylomeDB; Q91ZZ3; -.
DR TreeFam; TF332776; -.
DR BioGRID-ORCS; 104069; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Sncb; mouse.
DR PRO; PR:Q91ZZ3; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q91ZZ3; protein.
DR Bgee; ENSMUSG00000034891; Expressed in dentate gyrus of hippocampal formation granule cell and 101 other tissues.
DR Genevisible; Q91ZZ3; MM.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0016234; C:inclusion body; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0099523; C:presynaptic cytosol; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0043014; F:alpha-tubulin binding; ISO:MGI.
DR GO; GO:0048487; F:beta-tubulin binding; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:1903136; F:cuprous ion binding; ISO:MGI.
DR GO; GO:0046914; F:transition metal ion binding; ISO:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IGI:MGI.
DR GO; GO:0042417; P:dopamine metabolic process; IGI:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IGI:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; IGI:MGI.
DR GO; GO:1901214; P:regulation of neuron death; IBA:GO_Central.
DR GO; GO:0050808; P:synapse organization; IGI:MGI.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:SynGO.
DR InterPro; IPR001058; Synuclein.
DR InterPro; IPR002461; Synuclein_beta.
DR PANTHER; PTHR13820; PTHR13820; 1.
DR PANTHER; PTHR13820:SF4; PTHR13820:SF4; 1.
DR Pfam; PF01387; Synuclein; 1.
DR PRINTS; PR01213; BSYNUCLEIN.
DR PRINTS; PR01211; SYNUCLEIN.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..133
FT /note="Beta-synuclein"
FT /id="PRO_0000286176"
FT REPEAT 20..30
FT /note="1"
FT REPEAT 31..41
FT /note="2"
FT REPEAT 42..55
FT /note="3; approximate"
FT REPEAT 56..66
FT /note="4"
FT REGION 20..66
FT /note="4 X 11 AA tandem repeats of [EGS]-K-T-K-[EQ]-[GQ]-V-
FT X(4)"
FT REGION 96..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..133
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 117
FT /note="Phosphoserine; by BARK1, CK2 and GRK5"
FT /evidence="ECO:0000250|UniProtKB:Q16143"
SQ SEQUENCE 133 AA; 14052 MW; 8274D8A6A0D8E4D5 CRC64;
MDVFMKGLSM AKEGVVAAAE KTKQGVTEAA EKTKEGVLYV GSKTSGVVQG VASVAEKTKE
QASHLGGAVF SGAGNIAAAT GLVKKEEFPT DLKPEEVAQE AAEEPLIEPL MEPEGESYED
SPQEEYQEYE PEA
