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Database: UniProt
Entry: A0A1U7TCJ4_CARSF
LinkDB: A0A1U7TCJ4_CARSF
Original site: A0A1U7TCJ4_CARSF 
ID   A0A1U7TCJ4_CARSF        Unreviewed;       206 AA.
AC   A0A1U7TCJ4;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 39.
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   Name=SNAP25 {ECO:0000313|RefSeq:XP_008057769.1};
OS   Carlito syrichta (Philippine tarsier) (Tarsius syrichta).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Tarsiiformes; Tarsiidae;
OC   Carlito.
OX   NCBI_TaxID=1868482 {ECO:0000313|Proteomes:UP000189704, ECO:0000313|RefSeq:XP_008057769.1};
RN   [1] {ECO:0000313|RefSeq:XP_008057769.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: t-SNARE involved in the molecular regulation of
CC       neurotransmitter release. Plays an important role in the synaptic
CC       function of specific neuronal systems. Associates with proteins
CC       involved in vesicle docking and membrane fusion. Regulates plasma
CC       membrane recycling through its interaction with CENPF. Modulates the
CC       gating characteristics of the delayed rectifier voltage-dependent
CC       potassium channel KCNB1 in pancreatic beta cells.
CC       {ECO:0000256|RuleBase:RU369075}.
CC   -!- SUBUNIT: Part of the SNARE core complex containing SNAP25, VAMP2 and
CC       STX1A; this complex binds CPLX1. Found in a complex containing SYT1,
CC       SV2B and syntaxin-1. Found in a ternary complex with STX1A and VAMP8.
CC       Interacts with HSC70 and with SYT9, forming a complex with DNAJC5. The
CC       interaction with SYT9 is inhibited in presence of calcium. Isoform 1
CC       and isoform 2 interact with BLOC1S6. Interacts with CENPF. Interacts
CC       with EQTN. Interacts with HGS. Interacts with KCNB1 (via N-terminus);
CC       reduces the voltage-dependent potassium channel KCNB1 activity in
CC       pancreatic beta cells. Interacts with OTOF. Interacts with RIMS1.
CC       Interacts with SNAPIN. Interacts with STXBP6. Interacts with TRIM9.
CC       Interacts with ZDHHC13 (via ANK repeats). Interacts with ZDHHC17 (via
CC       ANK repeats). Associates with the BLOC-1 complex. Interacts with PLCL1
CC       (via C2 domain). Interacts with PRRT2; this interaction may impair the
CC       formation of the SNARE complex. Interacts with alpha-synuclein/SNCA.
CC       Interacts with PRPH2. Interacts with ROM1. Interacts with STX3.
CC       {ECO:0000256|RuleBase:RU369075}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004193,
CC       ECO:0000256|RuleBase:RU369075}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00004193}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC       {ECO:0000256|ARBA:ARBA00004635}. Photoreceptor inner segment
CC       {ECO:0000256|ARBA:ARBA00004437}. Synapse, synaptosome
CC       {ECO:0000256|RuleBase:RU369075}.
CC   -!- SIMILARITY: Belongs to the SNAP-25 family.
CC       {ECO:0000256|ARBA:ARBA00009480, ECO:0000256|RuleBase:RU003496}.
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DR   RefSeq; XP_008057769.1; XM_008059578.2.
DR   AlphaFoldDB; A0A1U7TCJ4; -.
DR   SMR; A0A1U7TCJ4; -.
DR   STRING; 1868482.ENSTSYP00000010269; -.
DR   Ensembl; ENSTSYT00000011196; ENSTSYP00000010269; ENSTSYG00000011194.
DR   GeneID; 103261977; -.
DR   KEGG; csyr:103261977; -.
DR   CTD; 6616; -.
DR   OMA; WKASEDG; -.
DR   OrthoDB; 388796at2759; -.
DR   Proteomes; UP000189704; Unplaced.
DR   GO; GO:0030424; C:axon; IEA:Ensembl.
DR   GO; GO:0031083; C:BLOC-1 complex; IEA:Ensembl.
DR   GO; GO:0005938; C:cell cortex; IEA:Ensembl.
DR   GO; GO:0005856; C:cytoskeleton; IEA:Ensembl.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell.
DR   GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR   GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl.
DR   GO; GO:0097470; C:ribbon synapse; IEA:Ensembl.
DR   GO; GO:0036477; C:somatodendritic compartment; IEA:Ensembl.
DR   GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl.
DR   GO; GO:0070032; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex; IEA:Ensembl.
DR   GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR   GO; GO:0005484; F:SNAP receptor activity; IEA:Ensembl.
DR   GO; GO:0017075; F:syntaxin-1 binding; IEA:Ensembl.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   GO; GO:0008306; P:associative learning; IEA:Ensembl.
DR   GO; GO:0098967; P:exocytic insertion of neurotransmitter receptor to postsynaptic membrane; IEA:Ensembl.
DR   GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR   GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
DR   GO; GO:0099590; P:neurotransmitter receptor internalization; IEA:Ensembl.
DR   GO; GO:0099525; P:presynaptic dense core vesicle exocytosis; IEA:Ensembl.
DR   GO; GO:0070201; P:regulation of establishment of protein localization; IEA:Ensembl.
DR   GO; GO:0010975; P:regulation of neuron projection development; IEA:Ensembl.
DR   CDD; cd15885; SNARE_SNAP25C; 1.
DR   CDD; cd15894; SNARE_SNAP25N; 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:UP000189704};
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"
SQ   SEQUENCE   206 AA;  23315 MW;  FBED2B082A4CB6A6 CRC64;
     MAEDADMRNE LEEMQRRADQ LADESLESTR RMLQLVEESK DAGIRTLVML DEQGEQLERI
     EEGMDQINKD MKEAEKNLTD LGKFCGLCVC PCNKLKSSDA YKKAWGNNQD GVVASQPARV
     VDEREQMAIS GGFIRRVTND ARENEMDENL EQVSGIIGNL RHMALDMGNE IDTQNRQIDR
     IMEKADSNKT RIDEANQRAT KMLGSG
//
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