SYUG_BOVIN
ID SYUG_BOVIN Reviewed; 127 AA.
AC Q9NZ50; Q1RMG7; Q9N187;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Gamma-synuclein;
DE AltName: Full=Synoretin;
DE Short=SR;
GN Name=SNCG;
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 NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=10192768; DOI=10.1006/mcne.1999.0735;
RA Surguchov A., Surgucheva I., Solessio E., Baehr W.;
RT "Synoretin: a new protein belonging to the synuclein family.";
RL Mol. Cell. Neurosci. 13:95-103(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION BY G-PROTEIN COUPLED RECEPTOR KINASES.
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 [4]
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).
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. {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 -!- 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: Predominantly expressed in retina (predominantly in
CC outer nuclear layer, also in inner segment of photoreceptor cells, some
CC individual cells located in the inner nuclear layer, inner plexiform
CC layer and in nerve fiber layer). Also found in brain and heart.
CC -!- PTM: Phosphorylated by BARK1 and GRK5. {ECO:0000269|PubMed:10852916}.
CC -!- SIMILARITY: Belongs to the synuclein family. {ECO:0000305}.
CC -!- CAUTION: Was originally (PubMed:10192768) thought to correspond to a
CC new class of synuclein. In fact, it is ortholog of the human gamma-
CC synuclein. {ECO:0000305|PubMed:10192768}.
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DR EMBL; AF219257; AAF32342.1; -; mRNA.
DR EMBL; BC114910; AAI14911.1; -; mRNA.
DR RefSeq; NP_776611.1; NM_174186.2.
DR AlphaFoldDB; Q9NZ50; -.
DR STRING; 9913.ENSBTAP00000004571; -.
DR PaxDb; Q9NZ50; -.
DR PRIDE; Q9NZ50; -.
DR Ensembl; ENSBTAT00000004571; ENSBTAP00000004571; ENSBTAG00000003515.
DR GeneID; 281494; -.
DR KEGG; bta:281494; -.
DR CTD; 6623; -.
DR VEuPathDB; HostDB:ENSBTAG00000003515; -.
DR VGNC; VGNC:35062; SNCG.
DR eggNOG; ENOG502S3WF; Eukaryota.
DR GeneTree; ENSGT00950000183175; -.
DR HOGENOM; CLU_129378_0_0_1; -.
DR InParanoid; Q9NZ50; -.
DR OMA; VPKAADQ; -.
DR OrthoDB; 1544450at2759; -.
DR TreeFam; TF332776; -.
DR Proteomes; UP000009136; Chromosome 28.
DR Bgee; ENSBTAG00000003515; Expressed in retina and 83 other tissues.
DR ExpressionAtlas; Q9NZ50; baseline.
DR GO; GO:0043679; C:axon terminus; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:1901214; P:regulation of neuron death; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
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; 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_0000184037"
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 99..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..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"
FT /evidence="ECO:0000250|UniProtKB:O76070"
FT CONFLICT 11
FT /note="A -> V (in Ref. 2; AAI14911)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 127 AA; 13253 MW; 4271F507830C917D CRC64;
MDVFKKGFSI AKEGVVGAVE KTKQGVTEAA EKTKEGVMYV GAKTKEGVVQ SVTSVAEKTK
EQANAVSEAV VSSVNTVATK TVEEVENIAV TSGVVHKEAL KQPVPSQEDE AAKAEEQVAE
ETKSGGD
