ID   SYUG_HUMAN              Reviewed;         127 AA.
AC   O76070; O15104; Q96P61;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 2.
DT   12-OCT-2022, entry version 193.
DE   RecName: Full=Gamma-synuclein;
DE   AltName: Full=Breast cancer-specific gene 1 protein;
DE   AltName: Full=Persyn;
DE   AltName: Full=Synoretin;
DE            Short=SR;
GN   Name=SNCG; Synonyms=BCSG1, PERSYN, PRSN;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Mammary cancer;
RX   PubMed=9044857;
RA   Ji H., Liu Y.E., Jia T., Wang M., Liu J., Xiao G., Joseph B.K., Rosen C.,
RA   Shi Y.E.;
RT   "Identification of a breast cancer-specific gene, BCSG1, by direct
RT   differential cDNA sequencing.";
RL   Cancer Res. 57:759-764(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   PubMed=9700196; DOI=10.1093/hmg/7.9.1417;
RA   Ninkina N.N., Alimova-Kost M.V., Paterson J.W.E., Delaney L., Cohen B.B.,
RA   Imreh S., Gnuchev N.V., Davies A.M., Buchman V.L.;
RT   "Organization, expression and polymorphism of the human persyn gene.";
RL   Hum. Mol. Genet. 7:1417-1424(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-110.
RX   PubMed=9737786; DOI=10.1007/s004390050792;
RA   Lavedan C., Leroy E., Dehejia A., Buchholtz S., Dutra A., Nussbaum R.L.,
RA   Polymeropoulos M.H.;
RT   "Identification, localization and characterization of the human gamma-
RT   synuclein gene.";
RL   Hum. Genet. 103:106-112(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Han C., Zhang B., Peng X., Yuan J., Qiang B.;
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-110.
RC   TISSUE=Colon;
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   [6]
RP   PHOSPHORYLATION AT SER-124 BY BARK1; CAMK2 AND CK2.
RX   PubMed=10852916; DOI=10.1074/jbc.m003542200;
RA   Pronin A.N., Morris A.J., Surguchov A., Benovic J.L.;
RT   "Synucleins are a novel class of substrates for G protein-coupled receptor
RT   kinases.";
RL   J. Biol. Chem. 275:26515-26522(2000).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=11746666; DOI=10.1002/cm.1035;
RA   Surguchov A., Palazzo R.E., Surgucheva I.;
RT   "Gamma synuclein: subcellular localization in neuronal and non-neuronal
RT   cells and effect on signal transduction.";
RL   Cell Motil. Cytoskeleton 49:218-228(2001).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
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 (By similarity). May also function in
CC       modulating the keratin network in skin. Activates the MAPK and Elk-1
CC       signal transduction pathway (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: May be a centrosome-associated protein. Interacts with MYOC;
CC       affects its secretion and its aggregation (By similarity).
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       O76070; P54274: TERF1; NbExp=2; IntAct=EBI-1053810, EBI-710997;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC       {ECO:0000269|PubMed:11746666}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000269|PubMed:11746666}. Cytoplasm,
CC       cytoskeleton, spindle {ECO:0000269|PubMed:11746666}. Note=Associated
CC       with centrosomes in several interphase cells. In mitotic cells,
CC       localized to the poles of the spindle.
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.
CC   -!- PTM: Phosphorylated. Phosphorylation by GRK5 appears to occur on
CC       residues distinct from the residue phosphorylated by other kinases.
CC       {ECO:0000269|PubMed:10852916}.
CC   -!- SIMILARITY: Belongs to the synuclein family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/SNCGID42343ch10q23.html";
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF010126; AAB64109.1; -; mRNA.
DR   EMBL; AF037207; AAC36586.1; -; Genomic_DNA.
DR   EMBL; AF017256; AAC36550.1; -; mRNA.
DR   EMBL; AF044311; AAC27738.1; -; Genomic_DNA.
DR   EMBL; AF411524; AAL05870.1; -; mRNA.
DR   EMBL; BC014098; AAH14098.1; -; mRNA.
DR   CCDS; CCDS7380.1; -.
DR   RefSeq; NP_001317049.1; NM_001330120.1.
DR   RefSeq; NP_003078.2; NM_003087.2.
DR   AlphaFoldDB; O76070; -.
DR   BMRB; O76070; -.
DR   BioGRID; 112507; 65.
DR   IntAct; O76070; 5.
DR   STRING; 9606.ENSP00000361087; -.
DR   TCDB; 1.C.77.1.3; the synuclein (synuclein) family.
DR   GlyGen; O76070; 9 sites, 1 O-linked glycan (9 sites).
DR   iPTMnet; O76070; -.
DR   PhosphoSitePlus; O76070; -.
DR   BioMuta; SNCG; -.
DR   CPTAC; CPTAC-133; -.
DR   CPTAC; CPTAC-1459; -.
DR   CPTAC; CPTAC-1460; -.
DR   CPTAC; CPTAC-1461; -.
DR   CPTAC; CPTAC-708; -.
DR   EPD; O76070; -.
DR   jPOST; O76070; -.
DR   MassIVE; O76070; -.
DR   PaxDb; O76070; -.
DR   PeptideAtlas; O76070; -.
DR   PRIDE; O76070; -.
DR   ProteomicsDB; 50372; -.
DR   ABCD; O76070; 1 sequenced antibody.
DR   Antibodypedia; 2808; 465 antibodies from 40 providers.
DR   CPTC; O76070; 3 antibodies.
DR   DNASU; 6623; -.
DR   Ensembl; ENST00000372017.4; ENSP00000361087.3; ENSG00000173267.14.
DR   GeneID; 6623; -.
DR   KEGG; hsa:6623; -.
DR   MANE-Select; ENST00000372017.4; ENSP00000361087.3; NM_003087.3; NP_003078.2.
DR   CTD; 6623; -.
DR   DisGeNET; 6623; -.
DR   GeneCards; SNCG; -.
DR   HGNC; HGNC:11141; SNCG.
DR   HPA; ENSG00000173267; Tissue enhanced (adrenal gland, brain).
DR   MIM; 602998; gene.
DR   neXtProt; NX_O76070; -.
DR   OpenTargets; ENSG00000173267; -.
DR   PharmGKB; PA35989; -.
DR   VEuPathDB; HostDB:ENSG00000173267; -.
DR   eggNOG; ENOG502S3WF; Eukaryota.
DR   GeneTree; ENSGT00950000183175; -.
DR   HOGENOM; CLU_129378_0_0_1; -.
DR   InParanoid; O76070; -.
DR   OMA; VPKAADQ; -.
DR   OrthoDB; 1544450at2759; -.
DR   PhylomeDB; O76070; -.
DR   TreeFam; TF332776; -.
DR   PathwayCommons; O76070; -.
DR   SignaLink; O76070; -.
DR   SIGNOR; O76070; -.
DR   BioGRID-ORCS; 6623; 8 hits in 1072 CRISPR screens.
DR   ChiTaRS; SNCG; human.
DR   GeneWiki; Gamma-synuclein; -.
DR   GenomeRNAi; 6623; -.
DR   Pharos; O76070; Tbio.
DR   PRO; PR:O76070; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; O76070; protein.
DR   Bgee; ENSG00000173267; Expressed in right adrenal gland cortex and 144 other tissues.
DR   ExpressionAtlas; O76070; baseline and differential.
DR   Genevisible; O76070; HS.
DR   GO; GO:0043679; C:axon terminus; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:1903136; F:cuprous ion binding; IBA:GO_Central.
DR   GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR   GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0009306; P:protein secretion; IEA:Ensembl.
DR   GO; GO:0014059; P:regulation of dopamine secretion; IEA:Ensembl.
DR   GO; GO:1901214; P:regulation of neuron death; IBA:GO_Central.
DR   GO; GO:0046928; P:regulation of neurotransmitter secretion; IEA:Ensembl.
DR   GO; GO:0050808; P:synapse organization; IBA:GO_Central.
DR   GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
DR   DisProt; DP00630; -.
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..127
FT                   /note="Gamma-synuclein"
FT                   /id="PRO_0000184038"
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          96..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..127
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         124
FT                   /note="Phosphoserine; by BARK1, CaMK2 and CK2"
FT                   /evidence="ECO:0000269|PubMed:10852916"
FT   VARIANT         110
FT                   /note="E -> V (in dbSNP:rs9864)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:9737786"
FT                   /id="VAR_007455"
FT   CONFLICT        13
FT                   /note="E -> K (in Ref. 1; AAB64109)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        17
FT                   /note="G -> D (in Ref. 4; AAL05870)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        68
FT                   /note="E -> K (in Ref. 1; AAB64109)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   127 AA;  13331 MW;  F183DEF302DBE688 CRC64;
     MDVFKKGFSI AKEGVVGAVE KTKQGVTEAA EKTKEGVMYV GAKTKENVVQ SVTSVAEKTK
     EQANAVSEAV VSSVNTVATK TVEEAENIAV TSGVVRKEDL RPSAPQQEGE ASKEKEEVAE
     EAQSGGD
//