ID   SN25A_CARAU             Reviewed;         204 AA.
AC   P36977;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Synaptosomal-associated protein 25-A;
DE            Short=SNAP-25A;
DE   AltName: Full=Synaptosome-associated protein 25.1;
DE            Short=SNAP-25.1;
GN   Name=snap25a; Synonyms=snap25.1;
OS   Carassius auratus (Goldfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Carassius.
OX   NCBI_TaxID=7957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RX   PubMed=8248151; DOI=10.1073/pnas.90.22.10598;
RA   Risinger C., Larhammar D.;
RT   "Multiple loci for synapse protein SNAP-25 in the tetraploid goldfish.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:10598-10602(1993).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=9843147;
RX   DOI=10.1002/(sici)1097-4547(19981201)54:5<563::aid-jnr1>3.0.co;2-7;
RA   Risinger C., Salaneck E., Soederberg C., Gates M., Postlethwait J.H.,
RA   Larhammar D.;
RT   "Cloning of two loci for synapse protein Snap25 in zebrafish: comparison of
RT   paralogous linkage groups suggests loss of one locus in the mammalian
RT   lineage.";
RL   J. Neurosci. Res. 54:563-573(1998).
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; L22973; AAA16537.1; -; mRNA.
DR   PIR; I50480; I50480.
DR   AlphaFoldDB; P36977; -.
DR   BMRB; P36977; -.
DR   SMR; P36977; -.
DR   Ensembl; ENSCART00000012656; ENSCARP00000012009; ENSCARG00000005536.
DR   Proteomes; UP000515129; Genome assembly.
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; Reference proteome; Repeat; Synapse;
KW   Synaptosome.
FT   CHAIN           1..204
FT                   /note="Synaptosomal-associated protein 25-A"
FT                   /id="PRO_0000213596"
FT   DOMAIN          19..81
FT                   /note="t-SNARE coiled-coil homology 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   DOMAIN          138..200
FT                   /note="t-SNARE coiled-coil homology 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   204 AA;  22843 MW;  458BBECFCFC09189 CRC64;
     MAEDADMRNE LSDMQQRADQ LADESLESTR RMLQLVEESK DAGIRTLVML DEQGEQLERI
     EEGMDQINKD MKDAEKNLND LGKFCGLCSC PCNKMKSGGS KAWGNNQDGV VASQPARVVD
     EREQMAISGG FIRRVTDDAR ENEMDENLEQ VGGIIGNLRH MALDMGNEID TQNRQIDRIM
     EKADSNKTRI DEANQRATKM LGSG