ID   SNP25_TORMA             Reviewed;         210 AA.
AC   P36976;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Synaptosomal-associated protein 25;
DE            Short=SNAP-25;
DE   AltName: Full=Synaptosomal-associated 25 kDa protein;
GN   Name=snap25;
OS   Torpedo marmorata (Marbled electric ray).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC   Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Torpedo.
OX   NCBI_TaxID=7788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Electric lobe;
RX   PubMed=8226991; DOI=10.1016/s0021-9258(20)80540-7;
RA   Risinger C., Blomqvist A.G., Lundell I., Lambertsson A., Nassel D.,
RA   Pieribone V.A., Brodin L., Larhammar D.;
RT   "Evolutionary conservation of synaptosome-associated protein 25 kDa (SNAP-
RT   25) shown by Drosophila and Torpedo cDNA clones.";
RL   J. Biol. Chem. 268:24408-24414(1993).
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.
CC   -!- SUBCELLULAR LOCATION: Synapse, synaptosome {ECO:0000250}. Cell membrane
CC       {ECO:0000250|UniProtKB:P60881}. Note=Complexed with macromolecular
CC       elements of the nerve terminal.
CC   -!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000305}.
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DR   EMBL; L22020; AAA49284.1; -; mRNA.
DR   PIR; I50552; I50552.
DR   AlphaFoldDB; P36976; -.
DR   SMR; P36976; -.
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: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   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   2: Evidence at transcript level;
KW   Cell membrane; Coiled coil; Membrane; Repeat; Synapse; Synaptosome.
FT   CHAIN           1..210
FT                   /note="Synaptosomal-associated protein 25"
FT                   /id="PRO_0000213595"
FT   DOMAIN          23..85
FT                   /note="t-SNARE coiled-coil homology 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   DOMAIN          147..209
FT                   /note="t-SNARE coiled-coil homology 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   210 AA;  23653 MW;  58FE471A9234B8B1 CRC64;
     MENSVENSMD PRSEQEEMQR CADQITDESL ESTRRMLQLV EESKDAGIRT LVMLDEQGEQ
     LERIEEGMDQ INKDMKEAEK NLSDLGKCCG LCSCPCNKLK NFEAGGAYKK VWGNNQDGVV
     ASQPARVMDD REQMAMSGGY IRRITDDARE NEMEENLDQV GSIIGNLRHM ALDMSNEIGS
     QNAQIDRIVV KGDMNKARID EANKHATKML