ID SNP25_CHICK Reviewed; 206 AA.
AC P60878; P13795; P36974; P70557; P70558; Q8IXK3; Q96FM2; Q9BR45;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 27-MAR-2024, entry version 133.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=White leghorn; TISSUE=Retina;
RX PubMed=1992470; DOI=10.1073/pnas.88.3.785;
RA Catsicas S., Larhammar D., Blomqvist A.G., Sanna P.P., Milner R.J.,
RA Wilson M.C.;
RT "Expression of a conserved cell-type-specific protein in nerve terminals
RT coincides with synaptogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:785-789(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS 1 AND
RP 2).
RX PubMed=8377193; DOI=10.1006/jmbi.1993.1485;
RA Bark I.C.;
RT "Structure of the chicken gene for SNAP-25 reveals duplicated exon encoding
RT distinct isoforms of the protein.";
RL J. Mol. Biol. 233:67-76(1993).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Part of the SNARE core complex containing SNAP25, VAMP2 and
CC STX1A. This complex binds CPLX1. Interacts with TRIM9, RIMS1 and
CC SNAPIN. Binds STXBP6. Found in a ternary complex with STX1A and VAMP8.
CC Associates with the BLOC-1 complex. Isoform 1 and isoform 2 interact
CC with BLOC1S6 (By similarity). Interacts with alpha-synuclein/SNCA (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P60878; Q8AYS8: KCNMA1; NbExp=3; IntAct=EBI-1637031, EBI-1635766;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Cell membrane
CC {ECO:0000250|UniProtKB:P60881}. Note=Membrane association requires
CC palmitoylation. {ECO:0000250}.
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=P60878-1, P13795-1;
CC Sequence=Displayed;
CC Name=2; Synonyms=SNAP-25a;
CC IsoId=P60878-2, P13795-2;
CC Sequence=VSP_010018;
CC -!- PTM: Palmitoylated. Cys-85 appears to be the main site, and
CC palmitoylation is required for membrane association (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000305}.
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DR EMBL; M57957; AAA49072.1; -; mRNA.
DR EMBL; L09253; AAA49070.1; -; Genomic_DNA.
DR EMBL; L09254; AAA49070.1; JOINED; Genomic_DNA.
DR EMBL; L09257; AAA49070.1; JOINED; Genomic_DNA.
DR EMBL; L09259; AAA49070.1; JOINED; Genomic_DNA.
DR EMBL; L09251; AAA49070.1; JOINED; Genomic_DNA.
DR EMBL; L09258; AAA49070.1; JOINED; Genomic_DNA.
DR EMBL; L09250; AAA49070.1; JOINED; Genomic_DNA.
DR EMBL; L09253; AAA49071.1; -; Genomic_DNA.
DR EMBL; L09254; AAA49071.1; JOINED; Genomic_DNA.
DR EMBL; L09257; AAA49071.1; JOINED; Genomic_DNA.
DR EMBL; L09259; AAA49071.1; JOINED; Genomic_DNA.
DR EMBL; L09252; AAA49071.1; JOINED; Genomic_DNA.
DR EMBL; L09258; AAA49071.1; JOINED; Genomic_DNA.
DR EMBL; L09250; AAA49071.1; JOINED; Genomic_DNA.
DR PIR; A37861; A37861.
DR RefSeq; NP_990789.1; NM_205458.1.
DR RefSeq; XP_015138942.1; XM_015283456.1.
DR RefSeq; XP_015138943.1; XM_015283457.1.
DR AlphaFoldDB; P60878; -.
DR BMRB; P60878; -.
DR SMR; P60878; -.
DR BioGRID; 676693; 1.
DR IntAct; P60878; 1.
DR STRING; 9031.ENSGALP00000014636; -.
DR iPTMnet; P60878; -.
DR PaxDb; 9031-ENSGALP00000014636; -.
DR Ensembl; ENSGALT00000138067; ENSGALP00000080548; ENSGALG00000009003. [P60878-1]
DR Ensembl; ENSGALT00010044232.1; ENSGALP00010026310.1; ENSGALG00010018327.1. [P60878-1]
DR Ensembl; ENSGALT00010044242.1; ENSGALP00010026317.1; ENSGALG00010018327.1. [P60878-2]
DR Ensembl; ENSGALT00015016570; ENSGALP00015009419; ENSGALG00015006952. [P60878-1]
DR KEGG; gga:396444; -.
DR VEuPathDB; HostDB:geneid_396444; -.
DR eggNOG; KOG3065; Eukaryota.
DR GeneTree; ENSGT00950000182843; -.
DR HOGENOM; CLU_096939_0_0_1; -.
DR InParanoid; P60878; -.
DR OMA; GMIQINE; -.
DR OrthoDB; 388796at2759; -.
DR PhylomeDB; P60878; -.
DR Reactome; R-GGA-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-GGA-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-GGA-449836; Other interleukin signaling.
DR Reactome; R-GGA-6798695; Neutrophil degranulation.
DR PRO; PR:P60878; -.
DR Proteomes; UP000000539; Chromosome 3.
DR Bgee; ENSGALG00000009003; Expressed in cerebellum and 3 other cell types or tissues.
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:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0031201; C:SNARE complex; ISS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0017075; F:syntaxin-1 binding; IBA:GO_Central.
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:0006887; P:exocytosis; IBA:GO_Central.
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 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 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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Coiled coil; Lipoprotein; Membrane;
KW Palmitate; Phosphoprotein; Reference proteome; Repeat; Synapse;
KW Synaptosome.
FT CHAIN 1..206
FT /note="Synaptosomal-associated protein 25"
FT /id="PRO_0000213593"
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..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 138
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT LIPID 85
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 88
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 90
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 92
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 58..89
FT /note="ERIEEGMDQINKDMKEAEKNLTDLGKFCGLCV -> DRVEEGMNHINQDMKE
FT AEKNLKDLGKCCGLFI (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_010018"
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
//
