SNP25_BOVIN
ID SNP25_BOVIN Reviewed; 206 AA.
AC Q17QQ3;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Synaptosomal-associated protein 25;
DE Short=SNAP-25;
DE AltName: Full=Synaptosomal-associated 25 kDa protein;
GN Name=SNAP25;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION) BY C.BOTULINUM NEUROTOXIN TYPE
RP C.
RC TISSUE=Chromaffin cell;
RX PubMed=8611567; DOI=10.1021/bi9519009;
RA Foran P., Lawrence G.W., Shone C.C., Foster K.A., Dolly J.O.;
RT "Botulinum neurotoxin C1 cleaves both syntaxin and SNAP-25 in intact and
RT permeabilized chromaffin cells: correlation with its blockade of
RT catecholamine release.";
RL Biochemistry 35:2630-2636(1996).
RN [3]
RP ASSOCIATION WITH THE BLOC-1 COMPLEX, AND INTERACTION WITH BLOC1S6.
RX PubMed=19546860; DOI=10.1038/mp.2009.58;
RA Ghiani C.A., Starcevic M., Rodriguez-Fernandez I.A., Nazarian R.,
RA Cheli V.T., Chan L.N., Malvar J.S., de Vellis J., Sabatti C.,
RA Dell'Angelica E.C.;
RT "The dysbindin-containing complex (BLOC-1) in brain: developmental
RT regulation, interaction with SNARE proteins and role in neurite
RT outgrowth.";
RL Mol. Psychiatry 15:204-215(2010).
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 (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P60881}.
CC -!- SUBUNIT: Part of the SNARE core complex containing SNAP25, VAMP2 and
CC STX1A; this complex binds CPLX1 (By similarity). Found in a complex
CC containing SYT1, SV2B and syntaxin-1 (By similarity). Found in a
CC ternary complex with STX1A and VAMP8 (By similarity). Interacts with
CC HSC70 and with SYT9, forming a complex with DNAJC5 (By similarity). The
CC interaction with SYT9 is inhibited in presence of calcium (By
CC similarity). Isoform 1 and isoform 2 interact with BLOC1S6
CC (PubMed:19546860). Interacts with CENPF (By similarity). Interacts with
CC EQTN (By similarity). Interacts with HGS (By similarity). Interacts
CC with KCNB1 (via N-terminus); reduces the voltage-dependent potassium
CC channel KCNB1 activity in pancreatic beta cells (By similarity).
CC Interacts with OTOF (By similarity). Interacts with RIMS1 (By
CC similarity). Interacts with SNAPIN (By similarity). Interacts with
CC STXBP6 (By similarity). Interacts with TRIM9 (By similarity). Interacts
CC with ZDHHC13 (via ANK repeats) (By similarity). Interacts with ZDHHC17
CC (via ANK repeats) (By similarity). Associates with the BLOC-1 complex
CC (PubMed:19546860). Interacts with PLCL1 (via C2 domain) (By
CC similarity). Interacts with PRRT2; this interaction may impair the
CC formation of the SNARE complex (By similarity). Interacts with alpha-
CC synuclein/SNCA (By similarity). Interacts with PRPH2 (By similarity).
CC Interacts with ROM1 (By similarity). Interacts with STX3 (By
CC similarity). {ECO:0000250|UniProtKB:P60879,
CC ECO:0000250|UniProtKB:P60881, ECO:0000269|PubMed:19546860}.
CC -!- INTERACTION:
CC Q17QQ3; P61763: STXBP1; NbExp=3; IntAct=EBI-7336080, EBI-7335973;
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 -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC neurotoxin BoNT/C; cleavage by BoNT/C inhibits neurotransmitter release
CC (PubMed:8611567). BoNT/C probably hydrolyzes the 198-Arg-|-Ala-199
CC bond. {ECO:0000305|PubMed:8611567}.
CC -!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC118237; AAI18238.1; -; mRNA.
DR RefSeq; NP_001069714.1; NM_001076246.1.
DR AlphaFoldDB; Q17QQ3; -.
DR SMR; Q17QQ3; -.
DR BioGRID; 197420; 1.
DR CORUM; Q17QQ3; -.
DR IntAct; Q17QQ3; 3.
DR MINT; Q17QQ3; -.
DR STRING; 9913.ENSBTAP00000010961; -.
DR iPTMnet; Q17QQ3; -.
DR PaxDb; Q17QQ3; -.
DR PRIDE; Q17QQ3; -.
DR Ensembl; ENSBTAT00000010961; ENSBTAP00000010961; ENSBTAG00000008323.
DR GeneID; 540853; -.
DR KEGG; bta:540853; -.
DR CTD; 6616; -.
DR VEuPathDB; HostDB:ENSBTAG00000008323; -.
DR VGNC; VGNC:35051; SNAP25.
DR eggNOG; KOG3065; Eukaryota.
DR GeneTree; ENSGT00950000182843; -.
DR HOGENOM; CLU_096939_0_0_1; -.
DR InParanoid; Q17QQ3; -.
DR OMA; WKASEDG; -.
DR OrthoDB; 1197028at2759; -.
DR TreeFam; TF315125; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000008323; Expressed in occipital lobe and 94 other tissues.
DR ExpressionAtlas; Q17QQ3; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0030426; C:growth cone; IDA:UniProtKB.
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; IDA:UniProtKB.
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 1: Evidence at protein 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_0000355578"
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 SITE 198..199
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type C (BoNT/C)"
FT /evidence="ECO:0000305|PubMed:8611567"
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
