GenomeNet

Database: UniProt
Entry: A0A9D3T7Q5_MEGAT
LinkDB: A0A9D3T7Q5_MEGAT
Original site: A0A9D3T7Q5_MEGAT 
ID   A0A9D3T7Q5_MEGAT        Unreviewed;       206 AA.
AC   A0A9D3T7Q5;
DT   03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2023, sequence version 1.
DT   18-JUN-2025, entry version 11.
DE   RecName: Full=Multifunctional fusion protein {ECO:0000256|RuleBase:RU003496, ECO:0000256|RuleBase:RU369075};
DE   Includes:
DE     RecName: Full=Synaptosomal-associated protein 25 {ECO:0000256|RuleBase:RU369075};
DE              Short=SNAP-25 {ECO:0000256|RuleBase:RU369075};
DE   Includes:
DE     RecName: Full=Synaptosomal-associated protein {ECO:0000256|RuleBase:RU003496};
GN   ORFNames=MATL_G00157110 {ECO:0000313|EMBL:KAG7465772.1};
OS   Megalops atlanticus (Tarpon) (Clupea gigantea).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Elopiformes; Megalopidae; Megalops.
OX   NCBI_TaxID=7932 {ECO:0000313|EMBL:KAG7465772.1, ECO:0000313|Proteomes:UP001046870};
RN   [1] {ECO:0000313|EMBL:KAG7465772.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YG-15Mar2019-1 {ECO:0000313|EMBL:KAG7465772.1};
RC   TISSUE=Brain {ECO:0000313|EMBL:KAG7465772.1};
RA   Zahm M., Roques C., Cabau C., Klopp C., Donnadieu C., Jouanno E.,
RA   Lampietro C., Louis A., Herpin A., Echchiki A., Berthelot C., Parey E.,
RA   Roest-Crollius H., Braasch I., Postlethwait J., Bobe J., Montfort J.,
RA   Bouchez O., Begum T., Mejri S., Adams A., Chen W.-J., Guiguen Y.;
RL   Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play an important role in the synaptic function of
CC       specific neuronal systems. Associates with proteins involved in vesicle
CC       docking and membrane fusion. {ECO:0000256|ARBA:ARBA00053144}.
CC   -!- FUNCTION: Plays an important role in the synaptic function of specific
CC       neuronal systems. Associates with proteins involved in vesicle docking
CC       and membrane fusion. {ECO:0000256|RuleBase:RU369075}.
CC   -!- SUBCELLULAR LOCATION: Synapse, synaptosome
CC       {ECO:0000256|RuleBase:RU369075}. Cell membrane
CC       {ECO:0000256|RuleBase:RU369075}.
CC   -!- SIMILARITY: Belongs to the SNAP-25 family.
CC       {ECO:0000256|ARBA:ARBA00009480, ECO:0000256|RuleBase:RU003496}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAG7465772.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JAFDVH010000013; KAG7465772.1; -; Genomic_DNA.
DR   OrthoDB; 19261at2759; -.
DR   Proteomes; UP001046870; Chromosome 13.
DR   GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0070032; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex; IEA:TreeGrafter.
DR   GO; GO:0005484; F:SNAP receptor activity; IEA:TreeGrafter.
DR   GO; GO:0017075; F:syntaxin-1 binding; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IEA:TreeGrafter.
DR   GO; GO:0016082; P:synaptic vesicle priming; IEA:TreeGrafter.
DR   CDD; cd15885; SNARE_SNAP25C; 1.
DR   CDD; cd15894; SNARE_SNAP25N; 1.
DR   FunFam; 1.20.5.110:FF:000007; Synaptosomal-associated protein; 1.
DR   FunFam; 1.20.5.110:FF:000009; Synaptosomal-associated protein; 1.
DR   Gene3D; 1.20.5.110; -; 2.
DR   InterPro; IPR000928; SNAP-25_dom.
DR   InterPro; IPR039077; SNAP-25_N_SNARE_chord.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   PANTHER; PTHR19305; SYNAPTOSOMAL ASSOCIATED PROTEIN; 1.
DR   PANTHER; PTHR19305:SF5; SYNAPTOSOMAL-ASSOCIATED PROTEIN 25; 1.
DR   Pfam; PF00835; SNAP-25; 1.
DR   SMART; SM00397; t_SNARE; 2.
DR   SUPFAM; SSF58038; SNARE fusion complex; 2.
DR   PROSITE; PS50192; T_SNARE; 2.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|RuleBase:RU369075};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU369075};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU369075};
KW   Reference proteome {ECO:0000313|Proteomes:UP001046870};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU369075};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018, ECO:0000256|RuleBase:RU369075};
KW   Synaptosome {ECO:0000256|ARBA:ARBA00022599, ECO:0000256|RuleBase:RU369075}.
FT   DOMAIN          19..81
FT                   /note="T-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50192"
FT   DOMAIN          140..202
FT                   /note="T-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50192"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          50..77
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..11
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   206 AA;  23160 MW;  CFDABAB07A10F4EA CRC64;
     MADDTDMRNE LADMQQRADQ LADESLESTR RMLQLVEESK DAGIRTLVML DEQGEQLERI
     EEGMDQINKD MKEAEKNLTD LGKFCGLCSC PCNKLKGSDA YKKAWGNNQD GVVASQPARV
     VDEREQMAIS GGFIRRVTDD ARENEMDENL EQVGGIIGNL RHMALDMGNE IDTQNRQIDR
     IMEKADSNKT RIDEANQRAT KMLGSG
//
DBGET integrated database retrieval system