SNAP_DROME
ID SNAP_DROME Reviewed; 292 AA.
AC Q23983; Q541G5;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Alpha-soluble NSF attachment protein;
DE Short=SNAP-alpha;
DE AltName: Full=N-ethylmaleimide-sensitive factor attachment protein;
GN Name=alphaSnap {ECO:0000312|FlyBase:FBgn0250791}; Synonyms=Snap;
GN ORFNames=CG6625 {ECO:0000312|FlyBase:FBgn0250791};
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].
RC TISSUE=Head;
RX PubMed=8202553; DOI=10.1073/pnas.91.12.5715;
RA Ordway R.W., Pallanck L., Ganetzky B.;
RT "Neurally expressed Drosophila genes encoding homologs of the NSF and SNAP
RT secretory proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:5715-5719(1994).
RN [2]
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 [3]
RP GENOME REANNOTATION.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17151602; DOI=10.1038/nature05380;
RA Stuart L.M., Boulais J., Charriere G.M., Hennessy E.J., Brunet S.,
RA Jutras I., Goyette G., Rondeau C., Letarte S., Huang H., Ye P., Morales F.,
RA Kocks C., Bader J.S., Desjardins M., Ezekowitz R.A.B.;
RT "A systems biology analysis of the Drosophila phagosome.";
RL Nature 445:95-101(2007).
CC -!- FUNCTION: Required for vesicular transport between the endoplasmic
CC reticulum and the Golgi apparatus. Also between the endosome and
CC phagosome. {ECO:0000269|PubMed:17151602}.
CC -!- INTERACTION:
CC Q23983; Q24547: Syx1A; NbExp=4; IntAct=EBI-195132, EBI-135062;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000269|PubMed:17151602}. Membrane {ECO:0000269|PubMed:17151602};
CC Peripheral membrane protein {ECO:0000269|PubMed:17151602}.
CC -!- SIMILARITY: Belongs to the SNAP 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; U09374; AAA83414.1; -; mRNA.
DR EMBL; AE014296; AAF49035.1; -; Genomic_DNA.
DR EMBL; AY069477; AAL39622.1; -; mRNA.
DR RefSeq; NP_524180.1; NM_079456.4.
DR AlphaFoldDB; Q23983; -.
DR SMR; Q23983; -.
DR BioGRID; 65495; 30.
DR DIP; DIP-19393N; -.
DR IntAct; Q23983; 33.
DR STRING; 7227.FBpp0074609; -.
DR PaxDb; Q23983; -.
DR PRIDE; Q23983; -.
DR EnsemblMetazoa; FBtr0074840; FBpp0074609; FBgn0250791.
DR GeneID; 40233; -.
DR KEGG; dme:Dmel_CG6625; -.
DR CTD; 40233; -.
DR FlyBase; FBgn0250791; alphaSnap.
DR VEuPathDB; VectorBase:FBgn0250791; -.
DR eggNOG; KOG1586; Eukaryota.
DR GeneTree; ENSGT00390000005826; -.
DR HOGENOM; CLU_046329_0_2_1; -.
DR InParanoid; Q23983; -.
DR OMA; WSVKEYL; -.
DR OrthoDB; 1191204at2759; -.
DR PhylomeDB; Q23983; -.
DR Reactome; R-DME-204005; COPII-mediated vesicle transport.
DR Reactome; R-DME-6807878; COPI-mediated anterograde transport.
DR Reactome; R-DME-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-DME-6811438; Intra-Golgi traffic.
DR Reactome; R-DME-6811440; Retrograde transport at the Trans-Golgi-Network.
DR SignaLink; Q23983; -.
DR BioGRID-ORCS; 40233; 1 hit in 3 CRISPR screens.
DR ChiTaRS; alphaSnap; fly.
DR GenomeRNAi; 40233; -.
DR PRO; PR:Q23983; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0250791; Expressed in second segment of antenna (Drosophila) and 30 other tissues.
DR Genevisible; Q23983; DM.
DR GO; GO:0043679; C:axon terminus; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; IDA:FlyBase.
DR GO; GO:0001671; F:ATPase activator activity; ISS:FlyBase.
DR GO; GO:0000149; F:SNARE binding; IPI:FlyBase.
DR GO; GO:0005483; F:soluble NSF attachment protein activity; IDA:FlyBase.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0048526; P:imaginal disc-derived wing expansion; IMP:FlyBase.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IMP:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:FlyBase.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IEP:FlyBase.
DR GO; GO:0007269; P:neurotransmitter secretion; NAS:FlyBase.
DR GO; GO:0035494; P:SNARE complex disassembly; IDA:FlyBase.
DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IDA:FlyBase.
DR GO; GO:0016082; P:synaptic vesicle priming; NAS:FlyBase.
DR CDD; cd15832; SNAP; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR000744; NSF_attach.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR13768; PTHR13768; 1.
DR PRINTS; PR00448; NSFATTACHMNT.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; ER-Golgi transport; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..292
FT /note="Alpha-soluble NSF attachment protein"
FT /id="PRO_0000219065"
SQ SEQUENCE 292 AA; 33000 MW; 4EE50F038ACFEC5F CRC64;
MGDNEQKALQ LMAEAEKKLT QQKGFLGSLF GGSNKVEDAI ECYQRAGNMF KMSKNWTKAG
ECFCEAATLH ARAGSRHDAG TCYVDASNCY KKVDVESAVN CLMKSIDIYT DMGRFTMAAK
HHQSIAEMYE SDPNNLAKSI QHYEQAADYF KGEESVSSAN KCMLKVAQYA AQLEDYEKAI
SIYEQVAASS LESSLLKYSA KEYFFRAALC HLSVDLLNAQ HAIEKYAQQY PAFQDSREFK
LIKVLCENLE EQNIEGFTEA VKDYDSISRL DQWYTTILLR IKKAADEDPD LR
