SNP25_RAT
ID SNP25_RAT Reviewed; 206 AA.
AC P60881; P13795; P36974; P70557; P70558; Q8IXK3; Q96FM2; Q9BR45;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Synaptosomal-associated protein 25;
DE Short=SNAP-25;
DE AltName: Full=Super protein;
DE Short=SUP;
DE AltName: Full=Synaptosomal-associated 25 kDa protein;
GN Name=Snap25; Synonyms=Snap;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA Kataoka M.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Cho A.R., You K.H.;
RT "Cloning of the SNAP-25 gene from a rat brain cDNA library.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-190 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10037470; DOI=10.1046/j.1471-4159.1999.0720988.x;
RA Madison D.L., Krueger W.H., Cheng D., Trapp B.D., Pfeiffer S.E.;
RT "SNARE complex proteins, including the cognate pair VAMP-2 and syntaxin-4,
RT are expressed in cultured oligodendrocytes.";
RL J. Neurochem. 72:988-998(1999).
RN [5]
RP PROTEIN SEQUENCE OF 46-69; 84-94; 104-119; 125-136 AND 143-161, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Diao W., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [6]
RP PALMITOYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=1281490; DOI=10.1523/jneurosci.12-12-04634.1992;
RA Hess D.T., Slater T.M., Wilson M.C., Skene J.H.P.;
RT "The 25 kDa synaptosomal-associated protein SNAP-25 is the major
RT methionine-rich polypeptide in rapid axonal transport and a major substrate
RT for palmitoylation in adult CNS.";
RL J. Neurosci. 12:4634-4641(1992).
RN [7]
RP FUNCTION, AND PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION) BY C.BOTULINUM
RP NEUROTOXIN TYPES A AND E.
RX PubMed=8243676; DOI=10.1016/0014-5793(93)80448-4;
RA Schiavo G., Santtuci A., Dasgupta B.R., Mehta P.P., Jontes J.,
RA Benfenati F., Wilson M.C., Montecucco C.;
RT "Botulinum neurotoxins serotypes A and E cleave SNAP-25 at distinct COOH-
RT terminal peptide bonds.";
RL FEBS Lett. 335:99-103(1993).
RN [8]
RP FUNCTION, AND PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION) BY C.BOTULINUM
RP NEUROTOXIN TYPES A AND E.
RX PubMed=8103915; DOI=10.1038/365160a0;
RA Blasi J., Chapman E.R., Link E., Binz T., Yamasaki S., De Camilli P.,
RA Suedhof T.C., Niemann H., Jahn R.;
RT "Botulinum neurotoxin A selectively cleaves the synaptic protein SNAP-25.";
RL Nature 365:160-163(1993).
RN [9]
RP PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION) BY C.BOTULINUM NEUROTOXIN TYPES
RP A AND E.
RX PubMed=8294407; DOI=10.1016/s0021-9258(17)42071-0;
RA Binz T., Blasi J., Yamasaki S., Baumeister A., Link E., Suedhof T.C.,
RA Jahn R., Niemann H.;
RT "Proteolysis of SNAP-25 by types E and A botulinal neurotoxins.";
RL J. Biol. Chem. 269:1617-1620(1994).
RN [10]
RP PHOSPHORYLATION AT THR-138 AND SER-187.
RX PubMed=12459461; DOI=10.1016/s0014-5793(02)03629-3;
RA Hepp R., Cabaniols J.-P., Roche P.A.;
RT "Differential phosphorylation of SNAP-25 in vivo by protein kinase C and
RT protein kinase A.";
RL FEBS Lett. 532:52-56(2002).
RN [11]
RP SUBCELLULAR LOCATION OF RNA TRANSCRIPTS.
RX PubMed=8738135; DOI=10.1016/0169-328x(95)00272-t;
RA Jacobsson G., Piehl F., Bark I.C., Zhang X., Meister B.;
RT "Differential subcellular localization of SNAP-25a and SNAP-25b RNA
RT transcripts in spinal motoneurons and plasticity in expression after nerve
RT injury.";
RL Brain Res. Mol. Brain Res. 37:49-62(1996).
RN [12]
RP INTERACTION WITH HGS.
RX PubMed=9039916; DOI=10.1038/385826a0;
RA Bean A.J., Seifert R., Chen Y.A., Sacks R., Scheller R.H.;
RT "Hrs-2 is an ATPase implicated in calcium-regulated secretion.";
RL Nature 385:826-829(1997).
RN [13]
RP IDENTIFICATION IN A TERNARY COMPLEX WITH STX1A AND VAMP8.
RX PubMed=10336434; DOI=10.1074/jbc.274.22.15440;
RA Fasshauer D., Antonin W., Margittai M., Pabst S., Jahn R.;
RT "Mixed and non-cognate SNARE complexes. Characterization of assembly and
RT biophysical properties.";
RL J. Biol. Chem. 274:15440-15446(1999).
RN [14]
RP INTERACTION WITH RIMS1.
RX PubMed=11438518; DOI=10.1074/jbc.m100929200;
RA Coppola T., Magnin-Luethi S., Perret-Menoud V., Gattesco S., Schiavo G.,
RA Regazzi R.;
RT "Direct interaction of the Rab3 effector RIM with Ca2+ channels, SNAP-25,
RT and synaptotagmin.";
RL J. Biol. Chem. 276:32756-32762(2001).
RN [15]
RP INTERACTION WITH STXBP6.
RX PubMed=12145319; DOI=10.1074/jbc.m204929200;
RA Scales S.J., Hesser B.A., Masuda E.S., Scheller R.H.;
RT "Amisyn, a novel syntaxin-binding protein that may regulate SNARE complex
RT assembly.";
RL J. Biol. Chem. 277:28271-28279(2002).
RN [16]
RP FUNCTION, INTERACTION WITH KCNB1, AND SUBCELLULAR LOCATION.
RX PubMed=12403834; DOI=10.1210/me.2002-0058;
RA MacDonald P.E., Wang G., Tsuk S., Dodo C., Kang Y., Tang L., Wheeler M.B.,
RA Cattral M.S., Lakey J.R., Salapatek A.M., Lotan I., Gaisano H.Y.;
RT "Synaptosome-associated protein of 25 kilodaltons modulates Kv2.1 voltage-
RT dependent K(+) channels in neuroendocrine islet beta-cells through an
RT interaction with the channel N terminus.";
RL Mol. Endocrinol. 16:2452-2461(2002).
RN [17]
RP INTERACTION WITH VAMP2.
RX PubMed=19196426; DOI=10.1111/j.1471-4159.2008.05849.x;
RA Ito H., Atsuzawa K., Morishita R., Usuda N., Sudo K., Iwamoto I.,
RA Mizutani K., Katoh-Semba R., Nozawa Y., Asano T., Nagata K.;
RT "Sept8 controls the binding of vesicle-associated membrane protein 2 to
RT synaptophysin.";
RL J. Neurochem. 108:867-880(2009).
RN [18]
RP INTERACTION WITH PLCL1, AND SUBCELLULAR LOCATION.
RX PubMed=23341457; DOI=10.1074/jbc.m112.419317;
RA Zhang Z., Takeuchi H., Gao J., Wang D., James D.J., Martin T.F., Hirata M.;
RT "PRIP (phospholipase C-related but catalytically inactive protein) inhibits
RT exocytosis by direct interactions with syntaxin 1 and SNAP-25 through its
RT C2 domain.";
RL J. Biol. Chem. 288:7769-7780(2013).
RN [19]
RP INTERACTION WITH ZDHHC17 AND ZDHHC13, AND MUTAGENESIS OF VAL-113; GLN-116
RP AND PRO-117.
RX PubMed=26198635; DOI=10.1074/jbc.m115.657668;
RA Lemonidis K., Sanchez-Perez M.C., Chamberlain L.H.;
RT "Identification of a novel sequence motif recognized by the ankyrin repeat
RT domain of zDHHC17/13 S-acyltransferases.";
RL J. Biol. Chem. 290:21939-21950(2015).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-83 AND 120-206 IN COMPLEX WITH
RP STX1A AND VAMP2.
RX PubMed=9759724; DOI=10.1038/26412;
RA Sutton R.B., Fasshauer D., Jahn R., Brunger A.T.;
RT "Crystal structure of a SNARE complex involved in synaptic exocytosis at
RT 2.4 A resolution.";
RL Nature 395:347-353(1998).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-83 IN COMPLEX WITH STX1A.
RX PubMed=11533035; DOI=10.1074/jbc.m106853200;
RA Misura K.M.S., Gonzalez L.C. Jr., May A.P., Scheller R.H., Weis W.I.;
RT "Crystal structure and biophysical properties of a complex between the N-
RT terminal SNARE region of SNAP25 and syntaxin 1a.";
RL J. Biol. Chem. 276:41301-41309(2001).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 7-83 AND 141-204 IN COMPLEX WITH
RP STX1A AND VAMP2.
RX PubMed=12496247; DOI=10.1074/jbc.m211889200;
RA Ernst J.A., Brunger A.T.;
RT "High resolution structure, stability, and synaptotagmin binding of a
RT truncated neuronal SNARE complex.";
RL J. Biol. Chem. 278:8630-8636(2003).
CC -!- FUNCTION: t-SNARE involved in the molecular regulation of
CC neurotransmitter release (PubMed:8243676, PubMed:8103915). May play an
CC important role in the synaptic function of specific neuronal systems.
CC Associates with proteins involved in vesicle docking and membrane
CC fusion. Regulates plasma membrane recycling through its interaction
CC with CENPF. Modulates the gating characteristics of the delayed
CC rectifier voltage-dependent potassium channel KCNB1 in pancreatic beta
CC cells (PubMed:12403834). {ECO:0000269|PubMed:12403834,
CC ECO:0000305|PubMed:8103915, ECO:0000305|PubMed:8243676}.
CC -!- SUBUNIT: Part of the SNARE core complex containing SNAP25, VAMP2 and
CC STX1A; this complex binds CPLX1 (PubMed:9759724, PubMed:12496247,
CC PubMed:19196426). Found in a complex containing SYT1, SV2B and
CC syntaxin-1 (By similarity). Found in a ternary complex with STX1A and
CC VAMP8 (PubMed:10336434). Interacts with HSC70 and with SYT9, forming a
CC complex with DNAJC5 (By similarity). The interaction with SYT9 is
CC inhibited in presence of calcium (By similarity). Isoform 1 and isoform
CC 2 interact with BLOC1S6 (By similarity). Interacts with CENPF (By
CC similarity). Interacts with EQTN (By similarity). Interacts with HGS
CC (PubMed:9039916). Interacts with KCNB1 (via N-terminus); reduces the
CC voltage-dependent potassium channel KCNB1 activity in pancreatic beta
CC cells (PubMed:12403834). Interacts with OTOF (By similarity). Interacts
CC with RIMS1 (PubMed:11438518). Interacts with SNAPIN (By similarity).
CC Interacts with STXBP6 (PubMed:12145319). Interacts with TRIM9 (By
CC similarity). Interacts with ZDHHC13 (via ANK repeats)
CC (PubMed:26198635). Interacts with ZDHHC17 (via ANK repeats)
CC (PubMed:26198635). Associates with the BLOC-1 complex (By similarity).
CC Interacts with PLCL1 (via C2 domain) (PubMed:23341457). Interacts with
CC PRRT2; this interaction may impair the formation of the SNARE complex
CC (By similarity). Interacts with alpha-synuclein/SNCA (By similarity).
CC Interacts with PRPH2 (By similarity). Interacts with ROM1 (By
CC similarity). Interacts with STX3 (By similarity).
CC {ECO:0000250|UniProtKB:P60879, ECO:0000269|PubMed:10336434,
CC ECO:0000269|PubMed:11438518, ECO:0000269|PubMed:12145319,
CC ECO:0000269|PubMed:12403834, ECO:0000269|PubMed:12496247,
CC ECO:0000269|PubMed:19196426, ECO:0000269|PubMed:23341457,
CC ECO:0000269|PubMed:26198635, ECO:0000269|PubMed:9039916,
CC ECO:0000269|PubMed:9759724}.
CC -!- INTERACTION:
CC P60881; P47709: Rph3a; NbExp=4; IntAct=EBI-1027214, EBI-1027524;
CC P60881; Q9QXY2: Srcin1; NbExp=3; IntAct=EBI-1027214, EBI-1394088;
CC P60881; P32851: Stx1a; NbExp=29; IntAct=EBI-1027214, EBI-539720;
CC P60881; Q08849: Stx3; NbExp=4; IntAct=EBI-1027214, EBI-8311156;
CC P60881; P21707: Syt1; NbExp=24; IntAct=EBI-1027214, EBI-458098;
CC P60881-2; P32851: Stx1a; NbExp=6; IntAct=EBI-15685612, EBI-539720;
CC P60881-2; P63045: Vamp2; NbExp=4; IntAct=EBI-15685612, EBI-520880;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P60879}. Cell membrane
CC {ECO:0000269|PubMed:12403834, ECO:0000269|PubMed:23341457}; Lipid-
CC anchor {ECO:0000250|UniProtKB:P60879}. Synapse, synaptosome
CC {ECO:0000269|PubMed:1281490}. Photoreceptor inner segment
CC {ECO:0000250|UniProtKB:P60879}. Note=Membrane association requires
CC palmitoylation (By similarity). Expressed throughout cytoplasm,
CC concentrating at the perinuclear region (By similarity). Colocalizes
CC with KCNB1 at the cell membrane (PubMed:12403834). Colocalizes with
CC PLCL1 at the cell membrane (PubMed:23341457).
CC {ECO:0000250|UniProtKB:P60879, ECO:0000269|PubMed:12403834,
CC ECO:0000269|PubMed:1281490, ECO:0000269|PubMed:23341457}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Isoforms differ by the usage of two alternative homologous
CC exons (5a and 5b) which code for positions 56 to 94 and differ only
CC in 9 positions out of 39.;
CC Name=1; Synonyms=SNAP-25b;
CC IsoId=P60881-1, P13795-1;
CC Sequence=Displayed;
CC Name=2; Synonyms=SNAP-25a;
CC IsoId=P60881-2, P13795-2;
CC Sequence=VSP_010020;
CC -!- PTM: Palmitoylated. Cys-85 appears to be the main site, and
CC palmitoylation is required for membrane association (By similarity).
CC {ECO:0000250|UniProtKB:P60879}.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC neurotoxin type A (BoNT/A, botA) which hydrolyzes the 197-Gln-|-Arg-198
CC bond and inhibits neurotransmitter release (PubMed:8243676,
CC PubMed:8103915). {ECO:0000269|PubMed:8243676,
CC ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915}.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC neurotoxin type E (BoNT/E) which hydrolyzes the 180-Arg-|-Ile-181 bond
CC and inhibits neurotransmitter release (PubMed:8243676, PubMed:8103915).
CC {ECO:0000269|PubMed:8243676, ECO:0000269|PubMed:8294407,
CC ECO:0000305|PubMed:8103915}.
CC -!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000305}.
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DR EMBL; AB003991; BAA20151.1; -; mRNA.
DR EMBL; AB003992; BAA20152.1; -; mRNA.
DR EMBL; AF245227; AAF81202.1; -; mRNA.
DR EMBL; U56262; AAA99826.1; -; mRNA.
DR EMBL; BC087699; AAH87699.1; -; mRNA.
DR EMBL; U56261; AAA99825.1; -; mRNA.
DR RefSeq; NP_001257504.1; NM_001270575.1. [P60881-2]
DR RefSeq; NP_001257505.1; NM_001270576.1. [P60881-2]
DR RefSeq; NP_112253.1; NM_030991.3. [P60881-1]
DR PDB; 1JTH; X-ray; 2.00 A; A/C=1-82.
DR PDB; 1N7S; X-ray; 1.45 A; C=7-83, D=141-204.
DR PDB; 1SFC; X-ray; 2.40 A; C/G/K=1-83, D/H/L=120-206.
DR PDB; 1URQ; X-ray; 2.00 A; C=7-83, D=142-204.
DR PDB; 3HD7; X-ray; 3.40 A; C/G=7-83, D/H=141-204.
DR PDB; 3IPD; X-ray; 4.80 A; C/G=7-83, D/H=141-204.
DR PDB; 3J96; EM; 7.60 A; M=17-204.
DR PDB; 3J97; EM; 7.80 A; M=7-204.
DR PDB; 3J98; EM; 8.40 A; M=17-204.
DR PDB; 3J99; EM; 8.20 A; M=17-204.
DR PDB; 5CCG; X-ray; 3.50 A; C/I=7-83, D/J=141-204.
DR PDB; 5CCH; X-ray; 3.60 A; C=7-83, D=141-204.
DR PDB; 5CCI; X-ray; 4.10 A; C=7-83, D=141-204.
DR PDB; 5KJ7; X-ray; 3.50 A; C/I=9-83, D/J=141-204.
DR PDB; 5KJ8; X-ray; 4.10 A; C/I=9-83, D/J=141-204.
DR PDB; 5LOB; X-ray; 3.30 A; D/F=7-82, E/G=141-203.
DR PDB; 5LOW; X-ray; 2.80 A; D/F/K/M=7-82, E/G/L/N=141-203.
DR PDB; 5W5C; X-ray; 1.85 A; C=7-83, D=141-204.
DR PDB; 5W5D; X-ray; 2.50 A; C=7-83, D=141-204.
DR PDB; 6IP1; EM; 3.90 A; C=1-100, D=126-206.
DR PDB; 6MDM; EM; 4.40 A; H=1-204.
DR PDB; 6MDN; EM; 4.40 A; H=1-204.
DR PDB; 6MDO; EM; 3.90 A; H=1-204.
DR PDB; 6MDP; EM; 3.80 A; H=1-204.
DR PDB; 6MTI; EM; 10.40 A; C/G/K/O/S/W=7-83, D/H/L/P/T/X=141-204.
DR PDB; 6WVW; X-ray; 2.11 A; C/G=10-83, D/H=141-204.
DR PDBsum; 1JTH; -.
DR PDBsum; 1N7S; -.
DR PDBsum; 1SFC; -.
DR PDBsum; 1URQ; -.
DR PDBsum; 3HD7; -.
DR PDBsum; 3IPD; -.
DR PDBsum; 3J96; -.
DR PDBsum; 3J97; -.
DR PDBsum; 3J98; -.
DR PDBsum; 3J99; -.
DR PDBsum; 5CCG; -.
DR PDBsum; 5CCH; -.
DR PDBsum; 5CCI; -.
DR PDBsum; 5KJ7; -.
DR PDBsum; 5KJ8; -.
DR PDBsum; 5LOB; -.
DR PDBsum; 5LOW; -.
DR PDBsum; 5W5C; -.
DR PDBsum; 5W5D; -.
DR PDBsum; 6IP1; -.
DR PDBsum; 6MDM; -.
DR PDBsum; 6MDN; -.
DR PDBsum; 6MDO; -.
DR PDBsum; 6MDP; -.
DR PDBsum; 6MTI; -.
DR PDBsum; 6WVW; -.
DR AlphaFoldDB; P60881; -.
DR SMR; P60881; -.
DR BioGRID; 247095; 14.
DR CORUM; P60881; -.
DR DIP; DIP-29205N; -.
DR IntAct; P60881; 27.
DR MINT; P60881; -.
DR ChEMBL; CHEMBL1075243; -.
DR iPTMnet; P60881; -.
DR PhosphoSitePlus; P60881; -.
DR SwissPalm; P60881; -.
DR World-2DPAGE; 0004:P60881; -.
DR jPOST; P60881; -.
DR PRIDE; P60881; -.
DR Ensembl; ENSRNOT00000007998; ENSRNOP00000007998; ENSRNOG00000006037. [P60881-2]
DR Ensembl; ENSRNOT00000080581; ENSRNOP00000072612; ENSRNOG00000006037. [P60881-1]
DR GeneID; 25012; -.
DR KEGG; rno:25012; -.
DR UCSC; RGD:3728; rat.
DR CTD; 6616; -.
DR RGD; 3728; Snap25.
DR eggNOG; KOG3065; Eukaryota.
DR GeneTree; ENSGT00950000182843; -.
DR InParanoid; P60881; -.
DR OrthoDB; 1197028at2759; -.
DR PhylomeDB; P60881; -.
DR Reactome; R-RNO-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-RNO-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-RNO-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-449836; Other interleukin signaling.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-888590; GABA synthesis, release, reuptake and degradation.
DR EvolutionaryTrace; P60881; -.
DR PRO; PR:P60881; -.
DR Proteomes; UP000002494; Chromosome 3.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:RGD.
DR GO; GO:0099026; C:anchored component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0044295; C:axonal growth cone; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005856; C:cytoskeleton; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005768; C:endosome; IDA:RGD.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISO:RGD.
DR GO; GO:0030175; C:filopodium; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030426; C:growth cone; IDA:HGNC-UCL.
DR GO; GO:0043229; C:intracellular organelle; IDA:RGD.
DR GO; GO:0030027; C:lamellipodium; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:HGNC-UCL.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0098794; C:postsynapse; ISO:RGD.
DR GO; GO:0048787; C:presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:0042734; C:presynaptic membrane; ISO:RGD.
DR GO; GO:0031201; C:SNARE complex; IDA:HGNC-UCL.
DR GO; GO:0036477; C:somatodendritic compartment; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; ISO:RGD.
DR GO; GO:0070044; C:synaptobrevin 2-SNAP-25-syntaxin-1a complex; IDA:RGD.
DR GO; GO:0070032; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex; IDA:MGI.
DR GO; GO:0070033; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex; IDA:RGD.
DR GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
DR GO; GO:0005802; C:trans-Golgi network; ISO:RGD.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:RGD.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0017022; F:myosin binding; IPI:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:RGD.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IDA:RGD.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0017075; F:syntaxin-1 binding; IDA:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:RGD.
DR GO; GO:0008306; P:associative learning; ISO:RGD.
DR GO; GO:0007409; P:axonogenesis; IEP:RGD.
DR GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; IDA:RGD.
DR GO; GO:0016197; P:endosomal transport; IDA:RGD.
DR GO; GO:0098967; P:exocytic insertion of neurotransmitter receptor to postsynaptic membrane; ISO:RGD.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0030252; P:growth hormone secretion; IEP:RGD.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0007616; P:long-term memory; IMP:RGD.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISO:RGD.
DR GO; GO:0030182; P:neuron differentiation; IEP:RGD.
DR GO; GO:0099590; P:neurotransmitter receptor internalization; ISO:RGD.
DR GO; GO:0007269; P:neurotransmitter secretion; ISO:RGD.
DR GO; GO:0046887; P:positive regulation of hormone secretion; IMP:RGD.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IEP:RGD.
DR GO; GO:0070201; P:regulation of establishment of protein localization; ISO:RGD.
DR GO; GO:0010975; P:regulation of neuron projection development; IMP:ParkinsonsUK-UCL.
DR GO; GO:0051963; P:regulation of synapse assembly; IEP:RGD.
DR GO; GO:0030431; P:sleep; IDA:RGD.
DR GO; GO:0035493; P:SNARE complex assembly; IMP:CAFA.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IDA:SynGO.
DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IBA:GO_Central.
DR GO; GO:0016082; P:synaptic vesicle priming; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR InterPro; IPR039077; SNAP-25.
DR InterPro; IPR000928; SNAP-25_dom.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19305:SF5; PTHR19305:SF5; 1.
DR Pfam; PF00835; SNAP-25; 1.
DR SMART; SM00397; t_SNARE; 2.
DR PROSITE; PS50192; T_SNARE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Reference proteome; Repeat; Synapse; Synaptosome.
FT CHAIN 1..206
FT /note="Synaptosomal-associated protein 25"
FT /id="PRO_0000213592"
FT DOMAIN 19..81
FT /note="t-SNARE coiled-coil homology 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT DOMAIN 140..202
FT /note="t-SNARE coiled-coil homology 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 1..75
FT /note="Interaction with CENPF"
FT /evidence="ECO:0000250"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..120
FT /note="Interaction with ZDHHC13 and ZDHHC17"
FT /evidence="ECO:0000269|PubMed:26198635"
FT REGION 111..120
FT /note="Interaction with ZDHHC17"
FT /evidence="ECO:0000250|UniProtKB:P60880"
FT SITE 180..181
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type E (BoNT/E)"
FT /evidence="ECO:0000269|PubMed:8243676,
FT ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915"
FT SITE 197..198
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type A (BoNT/A, botA)"
FT /evidence="ECO:0000269|PubMed:8243676,
FT ECO:0000269|PubMed:8294407, ECO:0000305|PubMed:8103915"
FT MOD_RES 138
FT /note="Phosphothreonine; by PKC and PKA"
FT /evidence="ECO:0000269|PubMed:12459461"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60879"
FT MOD_RES 187
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:12459461"
FT LIPID 85
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P60879"
FT LIPID 88
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P60879"
FT LIPID 90
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P60879"
FT LIPID 92
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P60879"
FT VAR_SEQ 58..89
FT /note="ERIEEGMDQINKDMKEAEKNLTDLGKFCGLCV -> DRVEEGMNHINQDMKE
FT AEKNLKDLGKCCGLFI (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1, ECO:0000303|Ref.2"
FT /id="VSP_010020"
FT MUTAGEN 113
FT /note="V->A: Inhibits interaction with ZDHHC13 and
FT ZDHHC17."
FT /evidence="ECO:0000269|PubMed:26198635"
FT MUTAGEN 116
FT /note="Q->A: Inhibits interaction with ZDHHC13 and
FT ZDHHC17."
FT /evidence="ECO:0000269|PubMed:26198635"
FT MUTAGEN 117
FT /note="P->A: Inhibits interaction with ZDHHC13 and
FT ZDHHC17."
FT /evidence="ECO:0000269|PubMed:26198635"
FT HELIX 7..82
FT /evidence="ECO:0007829|PDB:1N7S"
FT HELIX 142..201
FT /evidence="ECO:0007829|PDB:1N7S"
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
