ID A0A4W5MZE4_9TELE Unreviewed; 530 AA.
AC A0A4W5MZE4;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 10-JUN-2026, entry version 29.
DE RecName: Full=Synapsin-1 {ECO:0000256|ARBA:ARBA00017852};
DE AltName: Full=Synapsin I {ECO:0000256|ARBA:ARBA00029646};
OS Hucho hucho (huchen).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Hucho.
OX NCBI_TaxID=62062 {ECO:0000313|Ensembl:ENSHHUP00000043228.1, ECO:0000313|Proteomes:UP000314982};
RN [1] {ECO:0000313|Ensembl:ENSHHUP00000043228.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSHHUP00000043228.1}
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; A0A4W5MZE4; -.
DR Ensembl; ENSHHUT00000044850.1; ENSHHUP00000043228.1; ENSHHUG00000026539.1.
DR GeneTree; ENSGT00940000156062; -.
DR Proteomes; UP000314982; Unassembled WGS sequence.
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:UP000314982};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT DOMAIN 83..164
FT /note="Synapsin pre-ATP-grasp"
FT /evidence="ECO:0000259|Pfam:PF02078"
FT DOMAIN 166..367
FT /note="Synapsin ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF02750"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..493
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 373..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..417
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..452
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..474
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 530 AA; 57850 MW; EF17ADBEF0B9A69C CRC64;
MNYLRRRLSD STFISNLPNG YMTDLQRPDP AQPPPPATAA PPKSPTVGST PPVTSPTPSP
APERKPQPSQ SSGAGFFTTC CVLGKKVHGD YDIKVEQAEF SEINVIAHAN GSCNVDMQVL
RNGTKVARSF KPDFVLIRQH AFSMTQNEDF RNLIIGLQYG GIPSINSLES IYNLCDKPWA
FAQLISTYRK LGAEKFPLIE QTFYPNYKDM VAMPTFPVVV KIGHAHSGVG KVRVDNHSKF
QDIASVVALT QTYTTTEPLI DSKYDIRIQK IGNDYKAYMR TSISGNWKTN TGSAMLEQVA
MTDRYKLWVD TCSVIFGGLD ICAVKAIHGK DGKDYITEVV GSSMPLVGEH QAEDRQLITD
MVVAKMKAVG RTATGSPNKP TTMQPSQPQS ASQGKPRPGG QGAQQPPPAQ PAKPAPPRQR
NSAPQLQPEF KAPPQASALP QPEPLAQPQN EPTTQAQGKD LSPEQSQPPV VEQPIAEEKA
QAHPSLNKSQ SLTNAFGLKE TSFFRTASED VAKAETMRNL RKSFASLFSD
//
