SYUG_RAT
ID SYUG_RAT Reviewed; 123 AA.
AC Q63544; Q6R2I0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Gamma-synuclein;
DE AltName: Full=Persyn;
DE AltName: Full=Sensory neuron synuclein;
GN Name=Sncg;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Spinal ganglion;
RX PubMed=7673161; DOI=10.1074/jbc.270.36.21264;
RA Akopian A.N., Wood N.;
RT "Peripheral nervous system-specific genes identified by subtractive cDNA
RT cloning.";
RL J. Biol. Chem. 270:21264-21270(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Brain;
RA Klugmann M., Leichtlein C.B., During M.J.;
RT "Gamma synuclein is expressed in the hippocampus of adult rats.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 81-96, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
RN [4]
RP TISSUE SPECIFICITY.
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67 AND SER-72, AND
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: 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 (By similarity).
CC {ECO:0000250}.
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: Specifically expressed in the peripheral nervous
CC system. High expression in motoneurons of the brainstem. Also found in
CC neurons of many other brain regions including the cerebellar cortex,
CC thalmus, hypothalamus and CA1, CA2, CA3 and CA4 regions of the
CC hippocampus. {ECO:0000269|PubMed:9801372}.
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 -!- SIMILARITY: Belongs to the synuclein family. {ECO:0000305}.
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DR EMBL; X86789; CAA60485.1; -; mRNA.
DR EMBL; AY518351; AAR99333.1; -; mRNA.
DR PIR; A57431; A57431.
DR RefSeq; NP_113876.1; NM_031688.1.
DR AlphaFoldDB; Q63544; -.
DR iPTMnet; Q63544; -.
DR PhosphoSitePlus; Q63544; -.
DR PaxDb; Q63544; -.
DR PRIDE; Q63544; -.
DR GeneID; 64347; -.
DR KEGG; rno:64347; -.
DR UCSC; RGD:70996; rat.
DR CTD; 6623; -.
DR RGD; 70996; Sncg.
DR eggNOG; ENOG502S3WF; Eukaryota.
DR InParanoid; Q63544; -.
DR OrthoDB; 1544450at2759; -.
DR PhylomeDB; Q63544; -.
DR PRO; PR:Q63544; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0043679; C:axon terminus; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0043014; F:alpha-tubulin binding; IDA:RGD.
DR GO; GO:0048487; F:beta-tubulin binding; IDA:RGD.
DR GO; GO:1903136; F:cuprous ion binding; IBA:GO_Central.
DR GO; GO:0008344; P:adult locomotory behavior; ISO:RGD.
DR GO; GO:0002118; P:aggressive behavior; IEP:RGD.
DR GO; GO:0071464; P:cellular response to hydrostatic pressure; IEP:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR GO; GO:1901215; P:negative regulation of neuron death; IMP:RGD.
DR GO; GO:0007422; P:peripheral nervous system development; NAS:RGD.
DR GO; GO:0009306; P:protein secretion; ISO:RGD.
DR GO; GO:0014059; P:regulation of dopamine secretion; ISO:RGD.
DR GO; GO:1901214; P:regulation of neuron death; IBA:GO_Central.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; ISO:RGD.
DR GO; GO:0042220; P:response to cocaine; IEP:RGD.
DR GO; GO:1904307; P:response to desipramine; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0050808; P:synapse organization; ISO:RGD.
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; Direct protein sequencing; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..123
FT /note="Gamma-synuclein"
FT /id="PRO_0000184040"
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 93..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:0007744|PubMed:22673903"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 120
FT /note="Phosphoserine; by BARK1, CaMK2 and CK2"
FT /evidence="ECO:0000250|UniProtKB:O76070"
FT CONFLICT 23
FT /note="K -> T (in Ref. 1; CAA60485)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="T -> A (in Ref. 1; CAA60485)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="K -> E (in Ref. 1; CAA60485)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 123 AA; 12976 MW; ED2B377A37FDEE59 CRC64;
MDVFKKGFSI AREGVVGAVE KTKQGVTEAA EKTKEGVMYV GTKTKGERGT SVTSVAEKTK
EQANAVSEAV VSSVNTVATK TVEEAENIVV TTGVVRKEDL EPPAQDQEAK EQEEGEEAKS
GGD
