ID SYN1_CANLF Reviewed; 415 AA.
AC O62732;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=Synapsin-1;
DE AltName: Full=Synapsin I;
DE Flags: Fragment;
GN Name=SYN1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Shibuya H., Liu P.-C., O'Brien D.P., Johnson G.S.;
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Neuronal phosphoprotein that coats synaptic vesicles, and
CC binds to the cytoskeleton. Acts as a regulator of synaptic vesicles
CC trafficking, involved in the control of neurotransmitter release at the
CC pre-synaptic terminal (By similarity). Also involved in the regulation
CC of axon outgrowth and synaptogenesis (By similarity). The complex
CC formed with NOS1 and CAPON proteins is necessary for specific nitric-
CC oxid functions at a presynaptic level (By similarity).
CC {ECO:0000250|UniProtKB:O88935, ECO:0000250|UniProtKB:P09951,
CC ECO:0000250|UniProtKB:P17600}.
CC -!- SUBUNIT: Homodimer (By similarity). Can form oligomers with SYN2 (By
CC similarity). Interacts with CAPON. Forms a ternary complex with NOS1
CC (By similarity). Isoform Ib interacts with PRNP (By similarity).
CC {ECO:0000250|UniProtKB:O88935, ECO:0000250|UniProtKB:P09951,
CC ECO:0000250|UniProtKB:P17600}.
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000250|UniProtKB:O88935}. Golgi
CC apparatus {ECO:0000250|UniProtKB:O88935}. Presynapse
CC {ECO:0000250|UniProtKB:P17600}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle {ECO:0000250|UniProtKB:P09951}. Note=Dissociates from
CC synaptic vesicles and redistributes into the axon during action
CC potential firing, in a step that precedes fusion of vesicles with the
CC plasma membrane. Reclusters to presynapses after the cessation of
CC synaptic activity. {ECO:0000250|UniProtKB:P09951}.
CC -!- PTM: Substrate of different protein kinases. Phosphorylation promotes
CC synapsin-1 dissociation from synaptic vesicles, regulates its rate of
CC dispersion, and controls the kinetics of vesicle pool turnover and
CC neurotransmitter release. {ECO:0000250|UniProtKB:P09951,
CC ECO:0000250|UniProtKB:P17600}.
CC -!- SIMILARITY: Belongs to the synapsin family. {ECO:0000305}.
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DR EMBL; AF049588; AAC05207.1; -; Genomic_DNA.
DR AlphaFoldDB; O62732; -.
DR SMR; O62732; -.
DR STRING; 9615.ENSCAFP00000022325; -.
DR GlyCosmos; O62732; 3 sites, No reported glycans.
DR PaxDb; 9612-ENSCAFP00000022325; -.
DR eggNOG; KOG3895; Eukaryota.
DR InParanoid; O62732; -.
DR Proteomes; UP000002254; Unplaced.
DR Proteomes; UP000694429; Unplaced.
DR Proteomes; UP000694542; Unplaced.
DR Proteomes; UP000805418; Unplaced.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0007269; P:neurotransmitter secretion; IEA:InterPro.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR001359; Synapsin.
DR InterPro; IPR020898; Synapsin_ATP-bd_dom.
DR PANTHER; PTHR10841; SYNAPSIN; 1.
DR PANTHER; PTHR10841:SF24; SYNAPSIN-1; 1.
DR Pfam; PF02750; Synapsin_C; 1.
DR PRINTS; PR01368; SYNAPSIN.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
PE 3: Inferred from homology;
KW Actin-binding; Cell projection; Cytoplasmic vesicle; Glycoprotein;
KW Golgi apparatus; Methylation; Phosphoprotein; Reference proteome; Repeat;
KW Synapse.
FT CHAIN <1..>415
FT /note="Synapsin-1"
FT /id="PRO_0000183017"
FT REGION <1..148
FT /note="C; actin-binding and synaptic-vesicle binding"
FT REGION 146..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..383
FT /note="D; Pro-rich linker"
FT REGION 384..>415
FT /note="E"
FT COMPBIAS 146..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..214
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..284
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..358
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 40
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O88935"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88935"
FT MOD_RES 158
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88935"
FT MOD_RES 160
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O88935"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88935"
FT MOD_RES 164
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P09951"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88935"
FT MOD_RES 204
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88935"
FT MOD_RES 262
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88935"
FT MOD_RES 275
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88935"
FT MOD_RES 279
FT /note="Phosphoserine; by PDPK1"
FT /evidence="ECO:0000250|UniProtKB:P17599"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17600"
FT MOD_RES 284
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88935"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17599"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17599"
FT MOD_RES 350
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88935"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88935"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88935"
FT MOD_RES 406
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88935"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88935"
FT CARBOHYD 160
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 292
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 306
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 415
SQ SEQUENCE 415 AA; 43389 MW; E988E2026FC5361B CRC64;
AHSGMGKVKV DNQHDFQDIA SVVALTKTYA TAEPFIDAKY DVRVQKIGQN YKAYMRTSVS
GNWKTNTGSA MLEQIAMSDR YKLWVDTCSE IFGGLDICAV EALHGKDGRD HIIEVVGSSM
PLIGDHQDEY KQLIVELVVN KMAQALPRQQ QRDASPGRGS HSQTPSPGAL PLGRQTSQQP
SGPPAQQRPP PQGGPPQPGP GPQRQGPPLQ QRPPPQGQQH LSGLGPPAGS PLPQRLPSPT
SAPQQPVSQA QPLSQAQGRQ SRPVAGGPGA PPAARPPASP SPQRQAGPPQ ATRQTSVSGQ
APPKASGAPP SGQQRQGPPQ KPPGPAGPTR QASQAGPMPR TGPPTTQQPR PSGPGPAGRP
AKPQLAQKPS QDVPSPATAG GPPHPQLNKS QSLTNAFNLP EPAPPRPSLS QDEVK
//
