ID A0A8C5D699_GOUWI Unreviewed; 469 AA.
AC A0A8C5D699;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 10-JUN-2026, entry version 22.
DE RecName: Full=Synapsin-1 {ECO:0000256|ARBA:ARBA00017852};
DE AltName: Full=Synapsin I {ECO:0000256|ARBA:ARBA00029646};
GN Name=syn2a {ECO:0000313|Ensembl:ENSGWIP00000002619.1};
OS Gouania willdenowi (Blunt-snouted clingfish) (Lepadogaster willdenowi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Blenniimorphae; Blenniiformes; Gobiesocoidei; Gobiesocidae;
OC Gobiesocinae; Gouania.
OX NCBI_TaxID=441366 {ECO:0000313|Ensembl:ENSGWIP00000002619.1, ECO:0000313|Proteomes:UP000694680};
RN [1] {ECO:0000313|Ensembl:ENSGWIP00000002619.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Wellcome Sanger Institute Data Sharing;
RL Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGWIP00000002619.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSGWIP00000002619.1}
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 RefSeq; XP_028309812.1; XM_028454011.1.
DR AlphaFoldDB; A0A8C5D699; -.
DR Ensembl; ENSGWIT00000002833.1; ENSGWIP00000002619.1; ENSGWIG00000001379.1.
DR GeneID; 114467596; -.
DR OrthoDB; 10249572at2759; -.
DR Proteomes; UP000694680; Chromosome 7.
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; IPR019735; Synapsin_CS.
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.
DR PROSITE; PS00416; SYNAPSIN_2; 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:UP000694680};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT DOMAIN 100..202
FT /note="Synapsin pre-ATP-grasp"
FT /evidence="ECO:0000259|Pfam:PF02078"
FT DOMAIN 204..406
FT /note="Synapsin ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF02750"
FT REGION 16..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..49
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 469 AA; 51620 MW; 4F0D52EEE0FF555C CRC64;
MNYLRRRLSD STFISNLPNG YISDLQRPDL AQPPPPASST TAKSPTAAGP TPPPATSPAP
EKKPQPTQST GAGFFSSITN VVKQTAASAG LVEQTQVKNP KKFKILLIID EPQQEWSKLF
RGKKVFGDYD IKVEQAEFNE INVMARANGT CNVNMQVVRN GSKVVRSFKP DFVLIRQHAF
SMTQNEDFRN LIIGLQYGGV QSINSIESIY NLCDKPWAFA QLINTYRKLG ADKFPLIEQT
FYPNYKEMVS MPSFPVVVKI GHAHSGMGKV KVDNHSKFQD IASVVALTQT YTTTEPLIDS
KYDIRIQKIG TDYKAYMRTS ISGNWKTNTG SAMLDQVAMT DRYKLWVDTC SEIFGGLEIC
AVKAIHGKDG KDYITEVVGS SMPLVGEHQA EDRQLIADMV LAKMNQVAEK EANAPQRATT
IQPSQGTGQK GENSDEPIKD GVGRPPQGCL QYILDCNGVA VGPKPVQAN
//
