ID   SNP25_RABIT             Reviewed;          54 AA.
AC   P55820;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 85.
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;
DE   Flags: Fragments;
GN   Name=SNAP25; Synonyms=SNAP;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC   STRAIN=New Zealand white; TISSUE=Eye, and Spinal cord;
RX   PubMed=1941090; DOI=10.1523/jneurosci.11-11-03412.1991;
RA   Loewy A., Liu W.-S., Baitinger C., Willard M.B.;
RT   "The major 35S-methionine-labeled rapidly transported protein
RT   (superprotein) is identical to SNAP-25, a protein of synaptic terminals.";
RL   J. Neurosci. 11:3412-3421(1991).
CC   -!- FUNCTION: t-SNARE involved in the molecular regulation of
CC       neurotransmitter release. May play 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:0000250|UniProtKB:P60881}.
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 (By similarity). Found in a ternary complex with
CC       STX1A and VAMP8 (By similarity). Interacts with HSC70 and with SYT9,
CC       forming a complex with DNAJC5 (By similarity). The interaction with
CC       SYT9 is inhibited in presence of calcium (By similarity). Isoform 1 and
CC       isoform 2 interact with BLOC1S6. Interacts with CENPF. Interacts with
CC       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 (By similarity). Interacts with alpha-
CC       synuclein/SNCA (By similarity). Interacts with PRPH2 (By similarity).
CC       Interacts with ROM1 (By similarity). Interacts with STX3 (By
CC       similarity). {ECO:0000250|UniProtKB:P60879,
CC       ECO:0000250|UniProtKB:P60881}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC       {ECO:0000250|UniProtKB:P60879}. Cell membrane
CC       {ECO:0000250|UniProtKB:P60881}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P60879}. Synapse, synaptosome
CC       {ECO:0000250|UniProtKB:P60879}. Photoreceptor inner segment
CC       {ECO:0000250|UniProtKB:P60879}. Note=Membrane association requires
CC       palmitoylation. Expressed throughout cytoplasm, concentrating at the
CC       perinuclear region. Colocalizes with KCNB1 at the cell membrane (By
CC       similarity). Colocalizes with PLCL1 at the cell membrane (By
CC       similarity). {ECO:0000250|UniProtKB:P60879,
CC       ECO:0000250|UniProtKB:P60881}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000305}.
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DR   PIR; A44823; A44823.
DR   PIR; C44823; C44823.
DR   PIR; F44823; F44823.
DR   eggNOG; KOG3065; Eukaryota.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031201; C:SNARE complex; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0017075; F:syntaxin-1 binding; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   InterPro; IPR039077; SNAP-25.
DR   PANTHER; PTHR19305:SF5; PTHR19305:SF5; 2.
PE   1: Evidence at protein level;
KW   Cell membrane; Cytoplasm; Direct protein sequencing; Lipoprotein; Membrane;
KW   Reference proteome; Synapse; Synaptosome.
FT   CHAIN           1..54
FT                   /note="Synaptosomal-associated protein 25"
FT                   /id="PRO_0000213591"
FT   NON_CONS        29..30
FT                   /evidence="ECO:0000305"
FT   NON_CONS        45..46
FT                   /evidence="ECO:0000305"
FT   NON_CONS        49..50
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
SQ   SEQUENCE   54 AA;  6065 MW;  00014F740FEB29C5 CRC64;
     MLQLVEESSK DAGIRXLVML DEQGEQLERV VDEREQMAIS GGFIRIMEKM LGSG