ID A0A9D3X563_9SAUR Unreviewed; 206 AA.
AC A0A9D3X563;
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=KIL84_017591 {ECO:0000313|EMBL:KAH1173752.1};
OS Mauremys mutica (yellowpond turtle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Geoemydidae; Geoemydinae; Mauremys.
OX NCBI_TaxID=74926 {ECO:0000313|EMBL:KAH1173752.1, ECO:0000313|Proteomes:UP000827986};
RN [1] {ECO:0000313|EMBL:KAH1173752.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MM-2020 {ECO:0000313|EMBL:KAH1173752.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAH1173752.1};
RA Gong S., Gao Y.;
RT "The genome of Mauremys mutica provides insights into the evolution of
RT semi-aquatic lifestyle.";
RL Submitted (SEP-2021) to the EMBL/GenBank/DDBJ databases.
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:KAH1173752.1}.
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DR EMBL; JAHDVG010000482; KAH1173752.1; -; Genomic_DNA.
DR OrthoDB; 19261at2759; -.
DR Proteomes; UP000827986; Unassembled WGS sequence.
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:UP000827986};
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 COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 206 AA; 23286 MW; D9FC91EB35894E09 CRC64;
MAEELDMRNE LEEMQRRADQ LADESLESTR RMLQLVEESK DAGIRTLVML DEQGEQLERI
EEGMDQINKD MKEAEKNLTD LGKFCGLCVC PCNKLKSSDA YKKAWGNNQD GVVASQPARV
VDEREQMAIS GGFIRRVTND DREGEMDENL EQVSGIIGNL RHMALDMGNE IDTQNRQIGR
IMEKADSNKT RIDDANQRAT KMLGSG
//