SYUB_RAT
ID SYUB_RAT Reviewed; 137 AA.
AC Q63754; Q5PPN9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Beta-synuclein;
DE AltName: Full=Phosphoneuroprotein 14;
DE Short=PNP 14;
GN Name=Sncb;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Brain;
RX PubMed=1402909; DOI=10.1111/j.1471-4159.1992.tb10991.x;
RA Tobe T., Nakajo S., Tanaka A., Mitoya A., Omata K., Nakaya K., Tomita M.,
RA Nakamura Y.;
RT "Cloning and characterization of the cDNA encoding a novel brain-specific
RT 14-kDa protein.";
RL J. Neurochem. 59:1624-1629(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-134.
RC TISSUE=Brain;
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 33-43 AND 46-85, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP PHOSPHORYLATION BY CAM-KINASE II.
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May be involved in neuronal plasticity.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in brain.
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. {ECO:0000269|PubMed:8223629}.
CC -!- SIMILARITY: Belongs to the synuclein family. {ECO:0000305}.
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DR EMBL; D17764; BAA04610.1; -; mRNA.
DR EMBL; BC087579; AAH87579.1; -; mRNA.
DR RefSeq; NP_542955.2; NM_080777.2.
DR RefSeq; XP_006253656.1; XM_006253594.2.
DR AlphaFoldDB; Q63754; -.
DR BMRB; Q63754; -.
DR BioGRID; 250205; 2.
DR IntAct; Q63754; 1.
DR STRING; 10116.ENSRNOP00000024357; -.
DR iPTMnet; Q63754; -.
DR PhosphoSitePlus; Q63754; -.
DR SwissPalm; Q63754; -.
DR World-2DPAGE; 0004:Q63754; -.
DR jPOST; Q63754; -.
DR PaxDb; Q63754; -.
DR PRIDE; Q63754; -.
DR GeneID; 113893; -.
DR KEGG; rno:113893; -.
DR UCSC; RGD:70992; rat.
DR CTD; 6620; -.
DR RGD; 70992; Sncb.
DR eggNOG; ENOG502S0N5; Eukaryota.
DR InParanoid; Q63754; -.
DR OrthoDB; 1544450at2759; -.
DR PhylomeDB; Q63754; -.
DR TreeFam; TF332776; -.
DR PRO; PR:Q63754; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0043679; C:axon terminus; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0016234; C:inclusion body; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0099523; C:presynaptic cytosol; IDA:SynGO.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0043014; F:alpha-tubulin binding; IDA:RGD.
DR GO; GO:0048487; F:beta-tubulin binding; IDA:RGD.
DR GO; GO:0005509; F:calcium ion binding; ISO:RGD.
DR GO; GO:1903136; F:cuprous ion binding; ISO:RGD.
DR GO; GO:0046914; F:transition metal ion binding; ISO:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR GO; GO:0042417; P:dopamine metabolic process; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:1901214; P:regulation of neuron death; IBA:GO_Central.
DR GO; GO:0050808; P:synapse organization; ISO:RGD.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; ISO:RGD.
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..137
FT /note="Beta-synuclein"
FT /id="PRO_0000184036"
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 88..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..127
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 137 AA; 14504 MW; 678C6CB84FA01A03 CRC64;
MDVFMKGLSM AKEGVVAAAE KTKQGVTEAA EKTKEGVLYV GSKTKEGVVQ GVASVAEKTK
EQASHLGGAV FSGAGNIAAA TGLVKKEEFP TDLKPEEVAQ EAAEEPLIEP LMEPEGESYE
DSPQEEYQEY EPEAKGP
