SYUA_RAT
ID SYUA_RAT Reviewed; 140 AA.
AC P37377; P37378; Q53YM9;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Alpha-synuclein;
GN Name=Snca;
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 ALTERNATIVE SPLICING.
RC TISSUE=Brain;
RX PubMed=1661825; DOI=10.1016/0169-328x(91)90043-w;
RA Maroteaux L., Scheller R.H.;
RT "The rat brain synucleins; family of proteins transiently associated with
RT neuronal membrane.";
RL Brain Res. Mol. Brain Res. 11:335-343(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SYN2), AND TISSUE SPECIFICITY.
RX PubMed=3411354; DOI=10.1523/jneurosci.08-08-02804.1988;
RA Maroteaux L., Campanelli J.T., Scheller R.H.;
RT "Synuclein: a neuron-specific protein localized to the nucleus and
RT presynaptic nerve terminal.";
RL J. Neurosci. 8:2804-2815(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SYN1).
RX PubMed=10582622; DOI=10.1046/j.1471-4159.1999.0732586.x;
RA Kholodilov N.G., Neystat M., Oo T.F., Lo S.E., Larsen K.E., Sulzer D.,
RA Burke R.E.;
RT "Increased expression of rat synuclein in the substantia nigra pars
RT compacta identified by mRNA differential display in a model of
RT developmental target injury.";
RL J. Neurochem. 73:2586-2599(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SYN1).
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=12665621; DOI=10.1073/pnas.0737182100;
RA Liang T., Spence J., Liu L., Strother W.N., Chang H.W., Ellison J.A.,
RA Lumeng L., Li T.K., Foroud T., Carr L.G.;
RT "Alpha-synuclein maps to a quantitative trait locus for alcohol preference
RT and is differentially expressed in alcohol-preferring and - nonpreferring
RT rats.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4690-4695(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SYN1).
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 [6]
RP PROTEIN SEQUENCE OF 33-97, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [7]
RP UBIQUITINATION, AND INTERACTION WITH UCHL1.
RX PubMed=12408865; DOI=10.1016/s0092-8674(02)01012-7;
RA Liu Y., Fallon L., Lashuel H.A., Liu Z., Lansbury P.T. Jr.;
RT "The UCH-L1 gene encodes two opposing enzymatic activities that affect
RT alpha-synuclein degradation and Parkinson's disease susceptibility.";
RL Cell 111:209-218(2002).
RN [8]
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: Neuronal protein that plays several roles in synaptic
CC activity such as regulation of synaptic vesicle trafficking and
CC subsequent neurotransmitter release (By similarity). Participates as a
CC monomer in synaptic vesicle exocytosis by enhancing vesicle priming,
CC fusion and dilation of exocytotic fusion pores (By similarity).
CC Mechanistically, acts by increasing local Ca(2+) release from
CC microdomains which is essential for the enhancement of ATP-induced
CC exocytosis (By similarity). Acts also as a molecular chaperone in its
CC multimeric membrane-bound state, assisting in the folding of synaptic
CC fusion components called SNAREs (Soluble NSF Attachment Protein
CC REceptors) at presynaptic plasma membrane in conjunction with cysteine
CC string protein-alpha/DNAJC5 (By similarity). This chaperone activity is
CC important to sustain normal SNARE-complex assembly during aging (By
CC similarity). Also plays a role in the regulation of the dopamine
CC neurotransmission by associating with the dopamine transporter (DAT1)
CC and thereby modulating its activity (By similarity).
CC {ECO:0000250|UniProtKB:P37840}.
CC -!- SUBUNIT: Soluble monomer. Homotetramer. A dynamic intracellular
CC population of tetramers and monomers coexists normally and the tetramer
CC plays an essential role in maintaining homeostasis (By similarity).
CC Interacts with UCHL1 (PubMed:12408865). Interacts with phospholipase D
CC and histones. Interacts (via N-terminus) with synphilin-1/SNCAIP; this
CC interaction promotes formation of SNCA inclusions in the cytoplasm.
CC Interacts with CALM1. Interacts with STXBP1; this interaction controls
CC SNCA self-replicating aggregation. Interacts with SNARE components
CC VAMP2 and SNAP25; these interactions allows SNARE complex assembly and
CC integrity (By similarity). Interacts with RPH3A and RAB3A (By
CC similarity). Interacts with SERF1A; this interaction promotes the
CC aggregation of SNCA (By similarity). Interacts with SEPTIN4 (By
CC similarity). {ECO:0000250|UniProtKB:O55042,
CC ECO:0000250|UniProtKB:P37840, ECO:0000269|PubMed:12408865}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P37840}.
CC Membrane {ECO:0000250|UniProtKB:P37840}. Nucleus
CC {ECO:0000250|UniProtKB:P37840}. Synapse {ECO:0000250|UniProtKB:P37840}.
CC Secreted {ECO:0000250|UniProtKB:P37840}. Cell projection, axon
CC {ECO:0000250|UniProtKB:O55042}. Note=Membrane-bound in dopaminergic
CC neurons (By similarity). Expressed and colocalized with SEPTIN4 in
CC dopaminergic axon terminals, especially at the varicosities (By
CC similarity). {ECO:0000250|UniProtKB:O55042,
CC ECO:0000250|UniProtKB:P37840}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=Syn1;
CC IsoId=P37377-1; Sequence=Displayed;
CC Name=Syn2;
CC IsoId=P37377-2; Sequence=VSP_006367;
CC Name=Syn3;
CC IsoId=P37377-3; Sequence=VSP_006365, VSP_006366;
CC -!- TISSUE SPECIFICITY: Found only in brain (hippocampus, brainstem and
CC cortex). Specifically expressed in neuronal cell bodies and synapses.
CC {ECO:0000269|PubMed:3411354}.
CC -!- PTM: Phosphorylated, predominantly on serine residues. Phosphorylated
CC on Tyr-125 upon osmotic stress. {ECO:0000250|UniProtKB:P37840}.
CC -!- PTM: Ubiquitinated. The predominant conjugate is the diubiquitinated
CC form. {ECO:0000269|PubMed:12408865}.
CC -!- PTM: Acetylation at Met-1 seems to be important for proper folding and
CC native oligomeric structure. {ECO:0000250|UniProtKB:P37840}.
CC -!- SIMILARITY: Belongs to the synuclein family. {ECO:0000305}.
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DR EMBL; S73007; AAB20688.1; -; mRNA.
DR EMBL; S73008; AAB20689.1; -; mRNA.
DR EMBL; S73009; AAB20690.1; -; mRNA.
DR EMBL; AF007758; AAC16026.1; -; mRNA.
DR EMBL; AY550005; AAS55694.1; -; mRNA.
DR EMBL; AY550006; AAS55695.1; -; mRNA.
DR EMBL; BC087682; AAH87682.1; -; mRNA.
DR PIR; B43959; B43959.
DR RefSeq; NP_062042.1; NM_019169.2. [P37377-1]
DR RefSeq; XP_006236653.1; XM_006236591.3. [P37377-2]
DR RefSeq; XP_017447989.1; XM_017592500.1. [P37377-2]
DR AlphaFoldDB; P37377; -.
DR BMRB; P37377; -.
DR BioGRID; 247897; 80.
DR IntAct; P37377; 3.
DR STRING; 10116.ENSRNOP00000040281; -.
DR iPTMnet; P37377; -.
DR PhosphoSitePlus; P37377; -.
DR World-2DPAGE; 0004:P37377; -.
DR PeptideAtlas; P37377; -.
DR PRIDE; P37377; -.
DR ABCD; P37377; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000039247; ENSRNOP00000030609; ENSRNOG00000008656. [P37377-1]
DR Ensembl; ENSRNOT00000110072; ENSRNOP00000081453; ENSRNOG00000008656. [P37377-2]
DR GeneID; 29219; -.
DR KEGG; rno:29219; -.
DR UCSC; RGD:3729; rat. [P37377-1]
DR CTD; 6622; -.
DR RGD; 3729; Snca.
DR GeneTree; ENSGT00950000183175; -.
DR HOGENOM; CLU_129378_1_0_1; -.
DR InParanoid; P37377; -.
DR OMA; VHGVTTX; -.
DR OrthoDB; 1544450at2759; -.
DR PhylomeDB; P37377; -.
DR TreeFam; TF332776; -.
DR PRO; PR:P37377; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000008656; Expressed in frontal cortex and 18 other tissues.
DR Genevisible; P37377; RN.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:RGD.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0043679; C:axon terminus; IDA:RGD.
DR GO; GO:0005938; C:cell cortex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:BHF-UCL.
DR GO; GO:0005856; C:cytoskeleton; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005576; C:extracellular region; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0016234; C:inclusion body; ISO:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:RGD.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:RGD.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005640; C:nuclear outer membrane; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0098793; C:presynapse; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0005840; C:ribosome; IDA:RGD.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
DR GO; GO:0099512; C:supramolecular fiber; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISO:RGD.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0003779; F:actin binding; ISO:RGD.
DR GO; GO:0043014; F:alpha-tubulin binding; ISO:RGD.
DR GO; GO:0050544; F:arachidonic acid binding; ISO:RGD.
DR GO; GO:0048487; F:beta-tubulin binding; IDA:RGD.
DR GO; GO:0005509; F:calcium ion binding; ISO:RGD.
DR GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR GO; GO:1903136; F:cuprous ion binding; ISO:RGD.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0070840; F:dynein complex binding; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR GO; GO:0008198; F:ferrous iron binding; ISO:RGD.
DR GO; GO:0042393; F:histone binding; ISO:RGD.
DR GO; GO:0030544; F:Hsp70 protein binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0019894; F:kinesin binding; ISO:RGD.
DR GO; GO:0000287; F:magnesium ion binding; ISO:RGD.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; ISO:RGD.
DR GO; GO:0043274; F:phospholipase binding; IPI:RGD.
DR GO; GO:0005543; F:phospholipid binding; IDA:RGD.
DR GO; GO:0051219; F:phosphoprotein binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; IDA:RGD.
DR GO; GO:0000149; F:SNARE binding; ISO:RGD.
DR GO; GO:0048156; F:tau protein binding; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; ISO:RGD.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0008344; P:adult locomotory behavior; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0048148; P:behavioral response to cocaine; IMP:RGD.
DR GO; GO:0071280; P:cellular response to copper ion; ISO:RGD.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEP:RGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR GO; GO:0042416; P:dopamine biosynthetic process; ISO:RGD.
DR GO; GO:0042417; P:dopamine metabolic process; ISO:RGD.
DR GO; GO:0060079; P:excitatory postsynaptic potential; ISO:RGD.
DR GO; GO:0006631; P:fatty acid metabolic process; ISO:RGD.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISO:RGD.
DR GO; GO:0061024; P:membrane organization; ISO:RGD.
DR GO; GO:0001774; P:microglial cell activation; ISO:RGD.
DR GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; ISO:RGD.
DR GO; GO:0007006; P:mitochondrial membrane organization; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:1904715; P:negative regulation of chaperone-mediated autophagy; ISO:RGD.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0045963; P:negative regulation of dopamine metabolic process; IMP:BHF-UCL.
DR GO; GO:0051585; P:negative regulation of dopamine uptake involved in synaptic transmission; ISO:RGD.
DR GO; GO:0045920; P:negative regulation of exocytosis; ISO:RGD.
DR GO; GO:0035067; P:negative regulation of histone acetylation; ISO:RGD.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; ISO:RGD.
DR GO; GO:0032769; P:negative regulation of monooxygenase activity; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD.
DR GO; GO:1901215; P:negative regulation of neuron death; IMP:RGD.
DR GO; GO:0051622; P:negative regulation of norepinephrine uptake; ISO:RGD.
DR GO; GO:0010642; P:negative regulation of platelet-derived growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:BHF-UCL.
DR GO; GO:0051612; P:negative regulation of serotonin uptake; ISO:RGD.
DR GO; GO:0070495; P:negative regulation of thrombin-activated receptor signaling pathway; ISO:RGD.
DR GO; GO:0032410; P:negative regulation of transporter activity; ISO:RGD.
DR GO; GO:0006638; P:neutral lipid metabolic process; ISO:RGD.
DR GO; GO:0006644; P:phospholipid metabolic process; ISO:RGD.
DR GO; GO:0045807; P:positive regulation of endocytosis; ISO:RGD.
DR GO; GO:0045921; P:positive regulation of exocytosis; ISO:RGD.
DR GO; GO:1903284; P:positive regulation of glutathione peroxidase activity; ISO:RGD.
DR GO; GO:1903285; P:positive regulation of hydrogen peroxide catabolic process; ISO:RGD.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISO:RGD.
DR GO; GO:0060732; P:positive regulation of inositol phosphate biosynthetic process; ISO:RGD.
DR GO; GO:1901216; P:positive regulation of neuron death; ISO:RGD.
DR GO; GO:0001956; P:positive regulation of neurotransmitter secretion; ISO:RGD.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:0001921; P:positive regulation of receptor recycling; ISO:RGD.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISO:RGD.
DR GO; GO:0035543; P:positive regulation of SNARE complex assembly; ISO:RGD.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; ISO:RGD.
DR GO; GO:0051259; P:protein complex oligomerization; ISO:RGD.
DR GO; GO:0031648; P:protein destabilization; ISO:RGD.
DR GO; GO:0051262; P:protein tetramerization; ISO:RGD.
DR GO; GO:0031623; P:receptor internalization; ISO:RGD.
DR GO; GO:0050812; P:regulation of acyl-CoA biosynthetic process; ISO:RGD.
DR GO; GO:0014059; P:regulation of dopamine secretion; ISO:RGD.
DR GO; GO:0014048; P:regulation of glutamate secretion; ISO:RGD.
DR GO; GO:0040012; P:regulation of locomotion; ISO:RGD.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISO:RGD.
DR GO; GO:0043030; P:regulation of macrophage activation; ISO:RGD.
DR GO; GO:1901214; P:regulation of neuron death; IGI:ParkinsonsUK-UCL.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; ISO:RGD.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; ISO:RGD.
DR GO; GO:0051621; P:regulation of norepinephrine uptake; ISO:RGD.
DR GO; GO:0010517; P:regulation of phospholipase activity; ISO:RGD.
DR GO; GO:1905606; P:regulation of presynapse assembly; ISO:RGD.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:0022898; P:regulation of transmembrane transporter activity; 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:0034341; P:response to interferon-gamma; ISO:RGD.
DR GO; GO:0070555; P:response to interleukin-1; ISO:RGD.
DR GO; GO:0010040; P:response to iron(II) ion; ISO:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISO:RGD.
DR GO; GO:0032026; P:response to magnesium ion; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:RGD.
DR GO; GO:0035493; P:SNARE complex assembly; ISO:RGD.
DR GO; GO:0050808; P:synapse organization; ISO:RGD.
DR GO; GO:0001963; P:synaptic transmission, dopaminergic; ISO:RGD.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; ISO:RGD.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; ISO:RGD.
DR GO; GO:0016082; P:synaptic vesicle priming; ISO:RGD.
DR GO; GO:0048489; P:synaptic vesicle transport; ISO:RGD.
DR InterPro; IPR001058; Synuclein.
DR InterPro; IPR002460; Synuclein_alpha.
DR PANTHER; PTHR13820; PTHR13820; 1.
DR PANTHER; PTHR13820:SF5; PTHR13820:SF5; 1.
DR Pfam; PF01387; Synuclein; 1.
DR PRINTS; PR01212; ASYNUCLEIN.
DR PRINTS; PR01211; SYNUCLEIN.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection; Copper; Cytoplasm;
KW Direct protein sequencing; Membrane; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Synapse;
KW Ubl conjugation.
FT CHAIN 1..140
FT /note="Alpha-synuclein"
FT /id="PRO_0000184031"
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 99..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..140
FT /note="Interaction with SERF1A"
FT /evidence="ECO:0000250|UniProtKB:P37840"
FT BINDING 2
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 50
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P37840"
FT MOD_RES 125
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000250|UniProtKB:P37840"
FT MOD_RES 129
FT /note="Phosphoserine; by PLK2"
FT /evidence="ECO:0000250|UniProtKB:P37840"
FT VAR_SEQ 42
FT /note="S -> R (in isoform Syn3)"
FT /evidence="ECO:0000305"
FT /id="VSP_006365"
FT VAR_SEQ 43..140
FT /note="Missing (in isoform Syn3)"
FT /evidence="ECO:0000305"
FT /id="VSP_006366"
FT VAR_SEQ 104..140
FT /note="EEGYPQEGILEDMPVDPSSEAYEMPSEEGYQDYEPEA -> YPMGECTNHPP
FT RLIALRVKSRYREHSWRPRKQLSLACVVMDPFLPT (in isoform Syn2)"
FT /evidence="ECO:0000303|PubMed:3411354"
FT /id="VSP_006367"
SQ SEQUENCE 140 AA; 14515 MW; 1FFD19CD3B9E636C CRC64;
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVTTVAEKTK
EQVTNVGGAV VTGVTAVAQK TVEGAGNIAA ATGFVKKDQM GKGEEGYPQE GILEDMPVDP
SSEAYEMPSE EGYQDYEPEA
