ID A0A3P8T6V2_AMPPE Unreviewed; 452 AA.
AC A0A3P8T6V2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 10-JUN-2026, entry version 35.
DE RecName: Full=Synapsin-1 {ECO:0000256|ARBA:ARBA00017852};
DE AltName: Full=Synapsin I {ECO:0000256|ARBA:ARBA00029646};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000020099.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000020099.1}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000020099.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JAN-2026) to UniProtKB.
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. Also involved in the regulation of axon
CC outgrowth and synaptogenesis. The complex formed with NOS1 and CAPON
CC proteins is necessary for specific nitric-oxid functions at a
CC presynaptic level. {ECO:0000256|ARBA:ARBA00060129}.
CC -!- SUBUNIT: Homodimer. Can form oligomers with SYN2. Interacts with CAPON.
CC Forms a ternary complex with NOS1. Isoform Ib interacts with PRNP.
CC {ECO:0000256|ARBA:ARBA00046960}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
CC {ECO:0000256|ARBA:ARBA00004398}. Golgi apparatus
CC {ECO:0000256|ARBA:ARBA00004555}. Presynapse
CC {ECO:0000256|ARBA:ARBA00034106}.
CC -!- SIMILARITY: Belongs to the synapsin family.
CC {ECO:0000256|ARBA:ARBA00008243}.
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DR AlphaFoldDB; A0A3P8T6V2; -.
DR STRING; 161767.ENSAPEP00000020099; -.
DR Ensembl; ENSAPET00000020640.1; ENSAPEP00000020099.1; ENSAPEG00000014339.1.
DR GeneTree; ENSGT00940000156062; -.
DR OMA; CCEIFGG; -.
DR Proteomes; UP000265080; Chromosome 8.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:TreeGrafter.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0007269; P:neurotransmitter secretion; IEA:InterPro.
DR FunFam; 3.30.1490.20:FF:000008; Synapsin I; 1.
DR FunFam; 3.30.470.20:FF:000011; Synapsin I; 1.
DR FunFam; 3.40.50.20:FF:000008; Synapsin III; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
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; IPR019736; Synapsin_P_site.
DR InterPro; IPR020897; Synapsin_pre-ATP-grasp_dom.
DR PANTHER; PTHR10841; SYNAPSIN; 1.
DR PANTHER; PTHR10841:SF26; SYNAPSIN IIA; 1.
DR Pfam; PF02078; Synapsin; 1.
DR Pfam; PF02750; Synapsin_C; 1.
DR Pfam; PF10581; Synapsin_N; 1.
DR PRINTS; PR01368; SYNAPSIN.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS00415; SYNAPSIN_1; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000265080};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT DOMAIN 99..200
FT /note="Synapsin pre-ATP-grasp"
FT /evidence="ECO:0000259|Pfam:PF02078"
FT DOMAIN 202..397
FT /note="Synapsin ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF02750"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 452 AA; 49866 MW; DF454FCA809D486D CRC64;
MNYLRRRLSD STFISNLPNG YMTDLQRPDP AQPPPPASTT PAKSPTAGPT PPATSPAPER
KPQPAQSTGV GFFSSITNVV KQTAASAGLV EQTQVTTPKK FKILFVIDEP TQEWAKLFRG
KKIHGDYDIK VEQAEFNEIN VVAHANGTCM VNMQVYRNGT KVVRSFKPDF VLIRQHAFSM
TQNEDFRNLI IGLQYGGVPS INSLESIYNL CDKPWAFAQL INTFRKLGAD KFPLIEQTFY
PNYKEMVSMP SFPVVVKIGH AHSGIGKVKV DNHSKFQDIA SVVALTQTYT TTEPLIDSKY
DIRIQKIGTD YKAYMRTSIS GNWKSNTGSA MLEQVAMTDR YKLWVDTCSE IFGGLDICAV
KAIHGKDGRD YITEVVGSAM PLVGEHQAED RQLITDMEAN APQRPTTIQP SQKGEITGEP
TKNGTGRPPQ GCLQYILDCN GVAVGPKPVQ AN
//
