SYUG_MOUSE
ID SYUG_MOUSE Reviewed; 123 AA.
AC Q9Z0F7;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Gamma-synuclein;
DE AltName: Full=Persyn;
GN Name=Sncg; Synonyms=Persyn;
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, AND CHARACTERIZATION.
RC STRAIN=CD-1; TISSUE=Embryonic ganglion;
RX PubMed=9801372; DOI=10.1523/jneurosci.18-22-09335.1998;
RA Buchman V.L., Hunter H.J., Pinon L.G., Thompson J., Privalova E.M.,
RA Ninkina N.N., Davies A.M.;
RT "Persyn, a member of the synuclein family, has a distinct pattern of
RT expression in the developing nervous system.";
RL J. Neurosci. 18:9335-9341(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=CD-1;
RX PubMed=10051410; DOI=10.1006/geno.1998.5674;
RA Alimova-Kost M.V., Ninkina N.N., Imreh S., Gnuchev N.V., Adu J.,
RA Davies A.M., Buchman V.L.;
RT "Genomic structure and chromosomal localization of the mouse persyn gene.";
RL Genomics 56:224-227(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 [4]
RP POSSIBLE FUNCTION IN SKIN.
RX PubMed=9925745; DOI=10.1006/excr.1998.4292;
RA Ninkina N.N., Privalova E.M., Pinon L.G., Davies A.M., Buchman V.L.;
RT "Developmentally regulated expression of persyn, a member of the synuclein
RT family, in skin.";
RL Exp. Cell Res. 246:308-311(1999).
RN [5]
RP INTERACTION WITH MYOC.
RX PubMed=16392033; DOI=10.1007/s10571-005-8471-4;
RA Surgucheva I., Park B.C., Yue B.Y., Tomarev S., Surguchov A.;
RT "Interaction of myocilin with gamma-synuclein affects its secretion and
RT aggregation.";
RL Cell. Mol. Neurobiol. 25:1009-1033(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, and Lung;
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 [7]
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: Plays a role in neurofilament network integrity. May be
CC involved in modulating axonal architecture during development and in
CC the adult. In vitro, increases the susceptibility of neurofilament-H to
CC calcium-dependent proteases. May also function in modulating the
CC keratin network in skin. Activates the MAPK and Elk-1 signal
CC transduction pathway (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: May be a centrosome-associated protein. Interacts with MYOC;
CC affects its secretion and its aggregation.
CC {ECO:0000269|PubMed:16392033}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}.
CC Note=Associated with centrosomes in several interphase cells. In
CC mitotic cells, localized to the poles of the spindle (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, particularly in the
CC substantia nigra. Also expressed in the corpus callosum, heart,
CC skeletal muscle, ovary, testis, colon and spleen. Weak expression in
CC pancreas, kidney and lung. Expressed predominantly in the cell bodies
CC and axons of primary sensory neurons, sympathetic neurons and
CC motoneurons.
CC -!- DEVELOPMENTAL STAGE: Developmentally expressed in primary sensory
CC neurons and motoneurons. In trigeminal ganglia, expression increases
CC between embryonic day 10 and day 12. High levels are maintained here
CC throughout later stages of development and in adulthood.
CC -!- PTM: Phosphorylated. Phosphorylation by GRK5 appears to occur on
CC residues distinct from the residue phosphorylated by other kinases (By
CC 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; AF017255; AAC98893.1; -; mRNA.
DR EMBL; AF099986; AAD19899.1; -; Genomic_DNA.
DR EMBL; AF099984; AAD19899.1; JOINED; Genomic_DNA.
DR EMBL; AF099985; AAD19899.1; JOINED; Genomic_DNA.
DR EMBL; BC028508; AAH28508.1; -; mRNA.
DR CCDS; CCDS26937.1; -.
DR RefSeq; NP_035560.1; NM_011430.3.
DR AlphaFoldDB; Q9Z0F7; -.
DR STRING; 10090.ENSMUSP00000023826; -.
DR iPTMnet; Q9Z0F7; -.
DR PhosphoSitePlus; Q9Z0F7; -.
DR SWISS-2DPAGE; Q9Z0F7; -.
DR jPOST; Q9Z0F7; -.
DR MaxQB; Q9Z0F7; -.
DR PaxDb; Q9Z0F7; -.
DR PRIDE; Q9Z0F7; -.
DR ProteomicsDB; 262922; -.
DR Antibodypedia; 2808; 464 antibodies from 41 providers.
DR DNASU; 20618; -.
DR Ensembl; ENSMUST00000023826; ENSMUSP00000023826; ENSMUSG00000023064.
DR GeneID; 20618; -.
DR KEGG; mmu:20618; -.
DR UCSC; uc007tau.2; mouse.
DR CTD; 6623; -.
DR MGI; MGI:1298397; Sncg.
DR VEuPathDB; HostDB:ENSMUSG00000023064; -.
DR eggNOG; ENOG502S3WF; Eukaryota.
DR GeneTree; ENSGT00950000183175; -.
DR HOGENOM; CLU_129378_0_0_1; -.
DR InParanoid; Q9Z0F7; -.
DR OMA; VPKAADQ; -.
DR OrthoDB; 1544450at2759; -.
DR PhylomeDB; Q9Z0F7; -.
DR TreeFam; TF332776; -.
DR BioGRID-ORCS; 20618; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Sncg; mouse.
DR PRO; PR:Q9Z0F7; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9Z0F7; protein.
DR Bgee; ENSMUSG00000023064; Expressed in facial nucleus and 196 other tissues.
DR ExpressionAtlas; Q9Z0F7; baseline and differential.
DR Genevisible; Q9Z0F7; MM.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0043014; F:alpha-tubulin binding; ISO:MGI.
DR GO; GO:0048487; F:beta-tubulin binding; ISO:MGI.
DR GO; GO:1903136; F:cuprous ion binding; IBA:GO_Central.
DR GO; GO:0008344; P:adult locomotory behavior; IGI:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; IGI:MGI.
DR GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
DR GO; GO:0009306; P:protein secretion; IDA:UniProtKB.
DR GO; GO:0014059; P:regulation of dopamine secretion; IGI:MGI.
DR GO; GO:1901214; P:regulation of neuron death; IBA:GO_Central.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; IGI:MGI.
DR GO; GO:0050808; P:synapse organization; IGI:MGI.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
DR InterPro; IPR001058; Synuclein.
DR InterPro; IPR002462; Synuclein_gamma.
DR PANTHER; PTHR13820; PTHR13820; 1.
DR Pfam; PF01387; Synuclein; 1.
DR PRINTS; PR01214; GSYNUCLEIN.
DR PRINTS; PR01211; SYNUCLEIN.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..123
FT /note="Gamma-synuclein"
FT /id="PRO_0000184039"
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 [EGSA]-K-T-K-[EQ]-[GQ]-
FT V-X(4)"
FT REGION 91..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63544"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63544"
FT MOD_RES 120
FT /note="Phosphoserine; by BARK1, CaMK2 and CK2"
FT /evidence="ECO:0000250|UniProtKB:O76070"
SQ SEQUENCE 123 AA; 13160 MW; DCB93C78F8071EE2 CRC64;
MDVFKKGFSI AKEGVVGAVE KTKQGVTEAA EKTKEGVMYV GTKTKENVVQ SVTSVAEKTK
EQANAVSEAV VSSVNTVANK TVEEAENIVV TTGVVRKEDL EPPAQDQEAK EQEENEEAKS
GED
