SYN_HELPO
ID SYN_HELPO Reviewed; 496 AA.
AC Q6QM28;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Synapsin {ECO:0000312|EMBL:AAS45543.1};
DE Short=helSyn {ECO:0000303|PubMed:17726061};
GN Name=SYN {ECO:0000303|PubMed:20159961};
OS Helix pomatia (Roman snail) (Edible snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Eupulmonata; Stylommatophora;
OC Helicina; Helicoidea; Helicidae; Helix.
OX NCBI_TaxID=6536;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAS45543.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION
RP AT SER-9, AND MUTAGENESIS OF SER-9.
RC TISSUE=Nervous system {ECO:0000269|PubMed:17726061};
RX PubMed=17726061; DOI=10.1242/jcs.012005;
RA Fiumara F., Milanese C., Corradi A., Giovedi S., Leitinger G., Menegon A.,
RA Montarolo P.G., Benfenati F., Ghirardi M.;
RT "Phosphorylation of synapsin domain A is required for post-tetanic
RT potentiation.";
RL J. Cell Sci. 120:3228-3237(2007).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-36 AND SER-42, AND
RP MUTAGENESIS OF SER-36 AND SER-42.
RX PubMed=20159961; DOI=10.1242/jcs.056846;
RA Giachello C.N., Fiumara F., Giacomini C., Corradi A., Milanese C.,
RA Ghirardi M., Benfenati F., Montarolo P.G.;
RT "MAPK/Erk-dependent phosphorylation of synapsin mediates formation of
RT functional synapses and short-term homosynaptic plasticity.";
RL J. Cell Sci. 123:881-893(2010).
CC -!- FUNCTION: Neuronal phosphoprotein that coats synaptic vesicles. Plays a
CC role in the establishment of functional synaptic connections and in the
CC regulation of their activity-dependent short-term plasticity.
CC {ECO:0000269|PubMed:17726061, ECO:0000269|PubMed:20159961}.
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:17726061,
CC ECO:0000269|PubMed:20159961}. Cell projection
CC {ECO:0000269|PubMed:17726061, ECO:0000269|PubMed:20159961}.
CC Note=Localized in the contact area between the pre- and postsynaptic
CC cells and in varicose structures along presynaptic neurites projecting
CC onto the postsynaptic cell. {ECO:0000269|PubMed:17726061,
CC ECO:0000269|PubMed:20159961}.
CC -!- PTM: Ser-9 is likely to be phosphorylated by CaMK1/4 and/or PKA. It is
CC probable that the phosphorylation plays a role in short-term synaptic
CC enhancement (STE). Ser-36 and/or Ser-42 are likely to be phosphorylated
CC by MAPK; the phosphorylation may play a dual role in regulating both
CC functional synapse formation and their activity-dependent short-term
CC plasticity. {ECO:0000269|PubMed:17726061, ECO:0000269|PubMed:20159961}.
CC -!- SIMILARITY: Belongs to the synapsin family. {ECO:0000255}.
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DR EMBL; AY533823; AAS45543.1; -; mRNA.
DR AlphaFoldDB; Q6QM28; -.
DR SMR; Q6QM28; -.
DR iPTMnet; Q6QM28; -.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0008021; C:synaptic vesicle; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0007269; P:neurotransmitter secretion; IEA:InterPro.
DR Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR001359; Synapsin.
DR InterPro; IPR020898; Synapsin_ATP-bd_dom.
DR InterPro; IPR020897; Synapsin_pre-ATP-grasp_dom.
DR Pfam; PF02078; Synapsin; 1.
DR Pfam; PF02750; Synapsin_C; 1.
DR PRINTS; PR01368; SYNAPSIN.
DR SUPFAM; SSF52440; SSF52440; 1.
PE 1: Evidence at protein level;
KW Cell projection; Phosphoprotein; Synapse.
FT CHAIN 1..496
FT /note="Synapsin"
FT /id="PRO_0000423430"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..464
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphoserine; by PKA, CaMK1 and CaMK4"
FT /evidence="ECO:0000269|PubMed:17726061"
FT MOD_RES 36
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000269|PubMed:20159961"
FT MOD_RES 42
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000269|PubMed:20159961"
FT MUTAGEN 9
FT /note="S->A: Impairs post-tetanic potentiation (PTP) at
FT synapses."
FT /evidence="ECO:0000269|PubMed:17726061"
FT MUTAGEN 36
FT /note="S->A: Decreased phosphorylation and more clustered
FT distribution pattern; when associated with A-42."
FT /evidence="ECO:0000269|PubMed:20159961"
FT MUTAGEN 36
FT /note="S->D: Diffused and uniform distribution pattern;
FT when associated with E-42."
FT /evidence="ECO:0000269|PubMed:20159961"
FT MUTAGEN 42
FT /note="S->A: Decreased phosphorylation and more clustered
FT distribution pattern; when associated with A-36."
FT /evidence="ECO:0000269|PubMed:20159961"
FT MUTAGEN 42
FT /note="S->E: Diffused and uniform distribution pattern;
FT when associated with D-36."
FT /evidence="ECO:0000269|PubMed:20159961"
SQ SEQUENCE 496 AA; 54417 MW; 98CAACD9210B14C1 CRC64;
MNFLRRRFSS GDLQGEANEK EDPPNVGILN FKKGPSPSAP NSPSKSASPA TIGQKLFSGT
VGVKPVSKDR YKTLLVIDGQ HTDWSKYFKG KKLFGDWDVK VEQAEFSELN LASNSETGTT
VEIQAIRNGN KTTRSLKPDF LLIRQHVRDA KVDWRHLLLG FRYGGVPSIN SLTAEFNFLD
KPWVFAQLID IQKRLSKDVF PLIDQTYFSN HEEMLNSPKF PLVVKIGHAH RGLGKIKVDN
VQTLEDLASV MATMSSYATT EPFIDSKYDI HVQKIGTNYK AYLRKSIAGN WKANTGSAML
EQIPMDERFK LWADECSQLF GGLDVVSVEA IQGKDGRDHI IEVNGSSMAL LGEAQEEDRR
LISEMVMAKM QMMCKPAQQP LSKASSSQSI TPQANGAQKP VLAASPSRQA QGRPLDTSAQ
ATPGQARGPP SSGGLPGVSN SQTPLSNQPS HLSNPPPQPF PTSTSGPQGL PRMASKDEED
TMKNLRKTFA GIFGDV
