SNP25_PONAB
ID SNP25_PONAB Reviewed; 206 AA.
AC Q5NVG5; Q5NVK3; Q5R505; Q5R690; Q5R6U7;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Synaptosomal-associated protein 25;
DE Short=SNAP-25;
DE AltName: Full=Synaptosomal-associated 25 kDa protein;
GN Name=SNAP25;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250,
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. Found in a ternary complex with STX1A and VAMP8
CC (By similarity). Interacts with HSC70 and with SYT9, forming a complex
CC with DNAJC5 (By similarity). The interaction with SYT9 is inhibited in
CC presence of calcium (By similarity). Isoform 1 and isoform 2 interact
CC with BLOC1S6. Interacts with CENPF. Interacts with EQTN. Interacts with
CC HGS. Interacts with KCNB1 (via N-terminus); reduces the voltage-
CC dependent potassium channel KCNB1 activity in pancreatic beta cells.
CC Interacts with OTOF. Interacts with RIMS1. Interacts with SNAPIN.
CC Interacts with STXBP6. Interacts with TRIM9. Interacts with ZDHHC13
CC (via ANK repeats). Interacts with ZDHHC17 (via ANK repeats). Associates
CC with the BLOC-1 complex (By similarity). Interacts with HSC70 and with
CC SYT9, forming a complex with DNAJC5 (By similarity). The interaction
CC with SYT9 is inhibited in presence of calcium (By similarity).
CC Interacts with PLCL1 (via C2 domain) (By similarity). 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:0000250|UniProtKB:P60881,
CC ECO:0000250|UniProtKB:Q17QQ3}.
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 -!- 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=Q5NVG5-1; Sequence=Displayed;
CC Name=2; Synonyms=SNAP-25a;
CC IsoId=Q5NVG5-2; Sequence=VSP_017743;
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 -!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000305}.
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DR EMBL; CR860387; CAH92513.1; -; mRNA.
DR EMBL; CR860604; CAH92726.1; -; mRNA.
DR EMBL; CR861080; CAH93161.1; -; mRNA.
DR EMBL; CR926023; CAI29660.1; -; mRNA.
DR EMBL; CR926071; CAI29698.1; -; mRNA.
DR RefSeq; NP_001127109.1; NM_001133637.1. [Q5NVG5-1]
DR RefSeq; NP_001128960.1; NM_001135488.1. [Q5NVG5-2]
DR AlphaFoldDB; Q5NVG5; -.
DR SMR; Q5NVG5; -.
DR STRING; 9601.ENSPPYP00000011970; -.
DR PRIDE; Q5NVG5; -.
DR Ensembl; ENSPPYT00000044529; ENSPPYP00000037298; ENSPPYG00000010705. [Q5NVG5-2]
DR GeneID; 100174149; -.
DR GeneID; 100189930; -.
DR KEGG; pon:100189930; -.
DR CTD; 6616; -.
DR eggNOG; KOG3065; Eukaryota.
DR GeneTree; ENSGT00950000182843; -.
DR InParanoid; Q5NVG5; -.
DR Proteomes; UP000001595; Chromosome 20.
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 GO; GO:0006887; P:exocytosis; IEA:UniProt.
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 Alternative splicing; Cell membrane; Coiled coil; Cytoplasm; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Reference proteome; Repeat; Synapse;
KW Synaptosome.
FT CHAIN 1..206
FT /note="Synaptosomal-associated protein 25"
FT /id="PRO_0000229768"
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..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 111..120
FT /note="Interaction with ZDHHC17"
FT /evidence="ECO:0000250|UniProtKB:P60880"
FT MOD_RES 138
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P60879"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60879"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60879"
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="ERIEEGMDQINKDMKEAEKNSTDLGKFCGLCV -> DRVEEGMNHINQDMKE
FT AEKNLKDLGKCCGLFI (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_017743"
SQ SEQUENCE 206 AA; 23289 MW; F1DE39982A4CA436 CRC64;
MAEDADMRNE LEEMQRRADQ LADESLESTR RMLQLVEESK DAGIRTLVML DEQGEQLERI
EEGMDQINKD MKEAEKNSTD LGKFCGLCVC PCNKLKSSDA YKKAWGNNQD GVVASQPARV
VDEREQMAIS GGFIRRVTND ARENEMDENL EQVSGIIGNL RHMALDMGNE IDTQNRQIDR
IMEKADSNKT RIDEANQRAT KMLGSG
