ID   SYUB_BOVIN              Reviewed;         134 AA.
AC   P33567;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Beta-synuclein;
DE   AltName: Full=14 kDa brain-specific protein;
DE   AltName: Full=Phosphoneuroprotein 14;
DE            Short=PNP 14;
GN   Name=SNCB;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Brain;
RX   PubMed=8223629; DOI=10.1111/j.1432-1033.1993.tb18337.x;
RA   Nakajo S., Tsukada K., Omata K., Nakamura Y., Nakaya K.;
RT   "A new brain-specific 14-kDa protein is a phosphoprotein. Its complete
RT   amino acid sequence and evidence for phosphorylation.";
RL   Eur. J. Biochem. 217:1057-1063(1993).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Brain;
RX   PubMed=2230807; DOI=10.1111/j.1471-4159.1990.tb05792.x;
RA   Nakajo S., Omata K., Aiuchi T., Shibayama T., Okahashi I., Ochiai H.,
RA   Nakai Y., Nakaya K., Nakamura Y.;
RT   "Purification and characterization of a novel brain-specific 14-kDa
RT   protein.";
RL   J. Neurochem. 55:2031-2038(1990).
CC   -!- FUNCTION: May be involved in neuronal plasticity.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Specifically present in synapses around neurons but
CC       not in glial cells.
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   -!- SIMILARITY: Belongs to the synuclein family. {ECO:0000305}.
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DR   PIR; A60218; A60218.
DR   PIR; S39046; S39046.
DR   AlphaFoldDB; P33567; -.
DR   BMRB; P33567; -.
DR   STRING; 9913.ENSBTAP00000012928; -.
DR   PaxDb; P33567; -.
DR   eggNOG; ENOG502S0N5; Eukaryota.
DR   InParanoid; P33567; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0043679; C:axon terminus; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR   GO; GO:1903136; F:cuprous ion binding; IBA:GO_Central.
DR   GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
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; 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..134
FT                   /note="Beta-synuclein"
FT                   /id="PRO_0000184034"
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          97..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..134
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         118
FT                   /note="Phosphoserine; by BARK1, CK2 and GRK5"
FT                   /evidence="ECO:0000250|UniProtKB:Q16143"
SQ   SEQUENCE   134 AA;  14277 MW;  484FA01A01979966 CRC64;
     MDVFMKGLSM AKEGVVAAAE KTKQGVTEAA EKTKEGVLYV GSKTKEGVVQ GVASVAEKTK
     EQASHLGGAV FSGAGNIAAA TGLVKKEEFP TDLKPEEVAQ EAAEEPLIEP LMEPEGESYE
     EQPQEEYQEY EPEA