SNP25_MACMU
ID SNP25_MACMU Reviewed; 206 AA.
AC P60877; P13795; P36974; P70557; P70558; Q8IXK3; Q96FM2; Q9BR45;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Synaptosomal-associated protein 25;
DE Short=SNAP-25;
DE AltName: Full=Synaptosomal-associated 25 kDa protein;
GN Name=SNAP25;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hippocampus;
RA Jensen M.J., Smith L.A.;
RL Submitted (MAR-2000) 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.
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 PLCL1 (via C2
CC domain) (By similarity). Interacts with PRRT2; this interaction may
CC impair the formation of the SNARE complex (By similarity). Interacts
CC with alpha-synuclein/SNCA (By similarity). Interacts with PRPH2 (By
CC similarity). Interacts with ROM1 (By similarity). Interacts with STX3
CC (By similarity). {ECO:0000250|UniProtKB:P60879,
CC ECO:0000250|UniProtKB:P60881, 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 -!- 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; AF240770; AAF64477.1; -; mRNA.
DR RefSeq; NP_001028036.1; NM_001032864.1.
DR RefSeq; XP_015004823.1; XM_015149337.1.
DR AlphaFoldDB; P60877; -.
DR BMRB; P60877; -.
DR SMR; P60877; -.
DR STRING; 9544.ENSMMUP00000014487; -.
DR Ensembl; ENSMMUT00000015467; ENSMMUP00000014487; ENSMMUG00000011064.
DR Ensembl; ENSMMUT00000065548; ENSMMUP00000053161; ENSMMUG00000011064.
DR Ensembl; ENSMMUT00000085469; ENSMMUP00000071592; ENSMMUG00000011064.
DR Ensembl; ENSMMUT00000085731; ENSMMUP00000066077; ENSMMUG00000011064.
DR Ensembl; ENSMMUT00000087428; ENSMMUP00000063084; ENSMMUG00000011064.
DR Ensembl; ENSMMUT00000097476; ENSMMUP00000079299; ENSMMUG00000011064.
DR Ensembl; ENSMMUT00000100536; ENSMMUP00000075790; ENSMMUG00000011064.
DR Ensembl; ENSMMUT00000103515; ENSMMUP00000062488; ENSMMUG00000011064.
DR GeneID; 574204; -.
DR KEGG; mcc:574204; -.
DR CTD; 6616; -.
DR VEuPathDB; HostDB:ENSMMUG00000011064; -.
DR VGNC; VGNC:77663; SNAP25.
DR eggNOG; KOG3065; Eukaryota.
DR GeneTree; ENSGT00950000182843; -.
DR HOGENOM; CLU_096939_0_0_1; -.
DR InParanoid; P60877; -.
DR OMA; WKASEDG; -.
DR TreeFam; TF315125; -.
DR Proteomes; UP000006718; Chromosome 10.
DR Bgee; ENSMMUG00000011064; Expressed in prefrontal cortex and 21 other tissues.
DR ExpressionAtlas; P60877; baseline.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0031083; C:BLOC-1 complex; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:Ensembl.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; 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:UniProtKB-SubCell.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell.
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:0019905; F:syntaxin binding; 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: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 GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
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; Cytoplasm; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Reference proteome; Repeat; Synapse; Synaptosome.
FT CHAIN 1..206
FT /note="Synaptosomal-associated protein 25"
FT /id="PRO_0000213588"
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..23
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"
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
