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SNP25_DROME
ID   SNP25_DROME             Reviewed;         212 AA.
AC   P36975; F3YD56; Q5LJU6; Q7PLV2;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 166.
DE   RecName: Full=Synaptosomal-associated protein 25;
DE            Short=SNAP-25;
DE   AltName: Full=Synaptosomal-associated 25 kDa protein;
GN   Name=Snap25; ORFNames=CG40452;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND TISSUE SPECIFICITY.
RC   TISSUE=Head;
RX   PubMed=8226991; DOI=10.1016/s0021-9258(20)80540-7;
RA   Risinger C., Blomqvist A.G., Lundell I., Lambertsson A., Nassel D.,
RA   Pieribone V.A., Brodin L., Larhammar D.;
RT   "Evolutionary conservation of synaptosome-associated protein 25 kDa (SNAP-
RT   25) shown by Drosophila and Torpedo cDNA clones.";
RL   J. Biol. Chem. 268:24408-24414(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9272858; DOI=10.1016/s0378-1119(97)00106-6;
RA   Risinger C., Deitcher D.L., Lundell I., Schwarz T.L., Larhammar D.;
RT   "Complex gene organization of synaptic protein SNAP-25 in Drosophila
RT   melanogaster.";
RL   Gene 194:169-177(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [4]
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC   STRAIN=Berkeley; TISSUE=Head;
RA   Stapleton M., Booth B., Carlson J.W., Chavez C., Frise E., George R.A.,
RA   Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Synapse, synaptosome {ECO:0000250}.
CC       Note=Complexed with macromolecular elements of the nerve terminal.
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A;
CC         IsoId=P36975-1; Sequence=Displayed;
CC       Name=C;
CC         IsoId=P36975-3; Sequence=VSP_054454;
CC   -!- TISSUE SPECIFICITY: Exclusively found in brain and ganglia.
CC       {ECO:0000269|PubMed:8226991}.
CC   -!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000305}.
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DR   EMBL; L22021; AAA16059.1; -; mRNA.
DR   EMBL; U81153; AAB39757.1; -; Genomic_DNA.
DR   EMBL; U81147; AAB39757.1; JOINED; Genomic_DNA.
DR   EMBL; U81148; AAB39757.1; JOINED; Genomic_DNA.
DR   EMBL; U81149; AAB39757.1; JOINED; Genomic_DNA.
DR   EMBL; U81150; AAB39757.1; JOINED; Genomic_DNA.
DR   EMBL; U81151; AAB39757.1; JOINED; Genomic_DNA.
DR   EMBL; U81152; AAB39757.1; JOINED; Genomic_DNA.
DR   EMBL; AE014296; EAA46071.2; -; Genomic_DNA.
DR   EMBL; AE014296; EAL24571.2; -; Genomic_DNA.
DR   EMBL; BT023789; AAZ41798.1; -; mRNA.
DR   EMBL; BT126217; AEB22096.1; -; mRNA.
DR   RefSeq; NP_001036641.1; NM_001043176.2. [P36975-1]
DR   RefSeq; NP_001036642.2; NM_001043177.3. [P36975-3]
DR   AlphaFoldDB; P36975; -.
DR   SMR; P36975; -.
DR   BioGRID; 78209; 27.
DR   DIP; DIP-23273N; -.
DR   STRING; 7227.FBpp0110435; -.
DR   SwissPalm; P36975; -.
DR   PaxDb; P36975; -.
DR   PeptideAtlas; P36975; -.
DR   PRIDE; P36975; -.
DR   DNASU; 3355084; -.
DR   EnsemblMetazoa; FBtr0111143; FBpp0110435; FBgn0011288. [P36975-1]
DR   EnsemblMetazoa; FBtr0304625; FBpp0293167; FBgn0011288. [P36975-3]
DR   GeneID; 3355084; -.
DR   KEGG; dme:Dmel_CG40452; -.
DR   CTD; 6616; -.
DR   FlyBase; FBgn0011288; Snap25.
DR   VEuPathDB; VectorBase:FBgn0011288; -.
DR   eggNOG; KOG3065; Eukaryota.
DR   GeneTree; ENSGT00950000182843; -.
DR   HOGENOM; CLU_096939_0_0_1; -.
DR   InParanoid; P36975; -.
DR   OMA; WKASEDG; -.
DR   PhylomeDB; P36975; -.
DR   Reactome; R-DME-181429; Serotonin Neurotransmitter Release Cycle.
DR   Reactome; R-DME-181430; Norepinephrine Neurotransmitter Release Cycle.
DR   Reactome; R-DME-199992; trans-Golgi Network Vesicle Budding.
DR   Reactome; R-DME-210500; Glutamate Neurotransmitter Release Cycle.
DR   Reactome; R-DME-212676; Dopamine Neurotransmitter Release Cycle.
DR   Reactome; R-DME-264642; Acetylcholine Neurotransmitter Release Cycle.
DR   Reactome; R-DME-449836; Other interleukin signaling.
DR   Reactome; R-DME-6798695; Neutrophil degranulation.
DR   Reactome; R-DME-888590; GABA synthesis, release, reuptake and degradation.
DR   Reactome; R-DME-8980692; RHOA GTPase cycle.
DR   Reactome; R-DME-9013026; RHOB GTPase cycle.
DR   Reactome; R-DME-9013149; RAC1 GTPase cycle.
DR   Reactome; R-DME-9035034; RHOF GTPase cycle.
DR   BioGRID-ORCS; 3355084; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; Snap25; fly.
DR   GenomeRNAi; 3355084; -.
DR   PRO; PR:P36975; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0011288; Expressed in brain and 20 other tissues.
DR   Genevisible; P36975; DM.
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:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0031201; C:SNARE complex; IDA:FlyBase.
DR   GO; GO:0043195; C:terminal bouton; IDA:FlyBase.
DR   GO; GO:0005484; F:SNAP receptor activity; IDA:FlyBase.
DR   GO; GO:0000149; F:SNARE binding; IPI:FlyBase.
DR   GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR   GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR   GO; GO:0007274; P:neuromuscular synaptic transmission; IEP:FlyBase.
DR   GO; GO:0007269; P:neurotransmitter secretion; NAS:FlyBase.
DR   GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IDA:FlyBase.
DR   GO; GO:0016081; P:synaptic vesicle docking; NAS:FlyBase.
DR   GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IDA:FlyBase.
DR   GO; GO:0016082; P:synaptic vesicle priming; IDA:FlyBase.
DR   GO; GO:0048489; P:synaptic vesicle transport; IDA:FlyBase.
DR   GO; GO:0006906; P:vesicle fusion; IDA:FlyBase.
DR   GO; GO:0016192; P:vesicle-mediated transport; NAS:FlyBase.
DR   InterPro; IPR000928; SNAP-25_dom.
DR   InterPro; IPR000727; T_SNARE_dom.
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; Coiled coil; Reference proteome; Repeat; Synapse;
KW   Synaptosome.
FT   CHAIN           1..212
FT                   /note="Synaptosomal-associated protein 25"
FT                   /id="PRO_0000213594"
FT   DOMAIN          26..88
FT                   /note="t-SNARE coiled-coil homology 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   DOMAIN          148..210
FT                   /note="t-SNARE coiled-coil homology 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   VAR_SEQ         47..59
FT                   /note="KEAGIRTLVALDD -> AEVGMRSIVMLDE (in isoform C)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_054454"
SQ   SEQUENCE   212 AA;  23685 MW;  BDC90649A1AF3AC8 CRC64;
     MPADPSEEVA PQVPKTELEE LQINAQGVAD ESLESTRRML ALCEESKEAG IRTLVALDDQ
     GEQLDRIEEG MDQINADMRE AEKNLSGMEK CCGICVLPCN KSQSFKEDDG TWKGNDDGKV
     VNNQPQRVMD DRNGMMAQAG YIGRITNDAR EDEMEENMGQ VNTMIGNLRN MALDMGSELE
     NQNRQIDRIN RKGESNEARI AVANQRAHQL LK
 
 
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