ID A0A674A3V6_SALTR Unreviewed; 614 AA.
AC A0A674A3V6;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 25.
DE RecName: Full=Synapsin-1 {ECO:0000256|ARBA:ARBA00017852};
DE AltName: Full=Synapsin I {ECO:0000256|ARBA:ARBA00029646};
GN Name=SYN2 {ECO:0000313|Ensembl:ENSSTUP00000053730.1};
GN Synonyms=LOC115166143 {ECO:0000313|Ensembl:ENSSTUP00000053730.1};
OS Salmo trutta (Brown trout).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8032 {ECO:0000313|Ensembl:ENSSTUP00000053730.1, ECO:0000313|Proteomes:UP000472277};
RN [1] {ECO:0000313|Ensembl:ENSSTUP00000053730.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSSTUP00000053730.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) 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; A0A674A3V6; -.
DR Ensembl; ENSSTUT00000056164.1; ENSSTUP00000053730.1; ENSSTUG00000019732.1.
DR GeneTree; ENSGT00940000156062; -.
DR Proteomes; UP000472277; Chromosome 28.
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:UP000472277};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT DOMAIN 103..204
FT /note="Synapsin pre-ATP-grasp"
FT /evidence="ECO:0000259|Pfam:PF02078"
FT DOMAIN 206..408
FT /note="Synapsin ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF02750"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..44
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..56
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..475
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..503
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..538
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..559
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 614 AA; 67459 MW; 698EA3EC08774977 CRC64;
MNYLRRRLSD STFISNLPNG YMTDLQRPDP AQPPPPATAA PPKSPTVGST PSVTSPTPSP
APERKPQPSQ SSGAGFFSSI TNVVKQTAAS AGLVEQSTVT TPKKFKILLV IDEPQQEWAK
LFRGKKVHGD YDIKVEQAEF SEINVIAHAN GSCNVDMQVL RNGTKVARSF KPDFVLIRQH
AFSMTQNEDF RNLIIGLQYG GIPSINSLES IYNLCDKPWA FAQLISTYRK LGAEKFPLIE
QTFYPNYKDM VAMPTFPIVV KIGHAHSGVG KVRVDNHSKF QDIASVVALT QTYTTTEPLI
DSKYDIRIQK IGNDYKAYMR TSISGNWKTN TGSAMLEQVA MTDRYKLWVD NCSVIFGGLD
ICAVKAIHGK DGKDYITEVV GSSMPLVGEH QAEDRQLITD MVVAKMNQAV GRTPTGSPNR
PTTMQPSQVW LFLVLKLGGR VEPQSPRPDP KSTPKASAKD SCQRPTPTTQ QPQPQSASQG
KPRPGGLRAQ QTPPAQPAKP APPRQRNSAP QLQPEFKAPP QASALPQPEP LAQPQNEPTT
QAQQKDLNPE QSQPPVVEQP TVICSDKTFG FLQISLTNAF GLKETSFFRT ASEDVAKAET
MRNLRKSFAS LFSD
//
