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Protein

Alpha-soluble NSF attachment protein

Gene

alphaSnap

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus. Also between the endosome and phagosome.1 Publication

GO - Molecular functioni

  • ATPase activator activity Source: FlyBase
  • SNARE binding Source: FlyBase
  • soluble NSF attachment protein activity Source: FlyBase
  • syntaxin binding Source: GO_Central

GO - Biological processi

  • compound eye morphogenesis Source: FlyBase
  • ER to Golgi vesicle-mediated transport Source: FlyBase
  • imaginal disc-derived wing expansion Source: FlyBase
  • intracellular protein transport Source: UniProtKB
  • intra-Golgi vesicle-mediated transport Source: UniProtKB
  • mitotic cytokinesis Source: FlyBase
  • neuromuscular synaptic transmission Source: FlyBase
  • neuron projection morphogenesis Source: FlyBase
  • neurotransmitter secretion Source: FlyBase
  • phagocytosis Source: FlyBase
  • protein hexamerization Source: FlyBase
  • protein homooligomerization Source: FlyBase
  • SNARE complex disassembly Source: FlyBase
  • synaptic transmission Source: FlyBase
  • synaptic vesicle fusion to presynaptic active zone membrane Source: FlyBase
  • synaptic vesicle priming Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-DME-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-DME-6807878. COPI-mediated anterograde transport.
R-DME-6811434. COPI-dependent Golgi-to-ER retrograde traffic.
R-DME-6811438. Intra-Golgi traffic.
R-DME-6811440. Retrograde transport at the Trans-Golgi-Network.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-soluble NSF attachment protein
Short name:
SNAP-alpha
Alternative name(s):
N-ethylmaleimide-sensitive factor attachment protein
Gene namesi
Name:alphaSnapImported
Synonyms:Snap
ORF Names:CG6625Imported
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0250791. alphaSnap.

Subcellular locationi

GO - Cellular componenti

  • axon terminus Source: FlyBase
  • cytoplasm Source: FlyBase
  • cytoplasmic, membrane-bounded vesicle Source: UniProtKB-SubCell
  • cytoplasmic vesicle Source: UniProtKB
  • extrinsic component of membrane Source: FlyBase
  • membrane Source: UniProtKB
  • terminal bouton Source: FlyBase
  • vacuolar membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 292292Alpha-soluble NSF attachment proteinPRO_0000219065Add
BLAST

Proteomic databases

PaxDbiQ23983.
PRIDEiQ23983.

Expressioni

Gene expression databases

BgeeiQ23983.
GenevisibleiQ23983. DM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
Syx1AQ245474EBI-195132,EBI-135062

GO - Molecular functioni

  • SNARE binding Source: FlyBase
  • soluble NSF attachment protein activity Source: FlyBase
  • syntaxin binding Source: GO_Central

Protein-protein interaction databases

BioGridi65495. 29 interactions.
DIPiDIP-19393N.
IntActiQ23983. 33 interactions.
MINTiMINT-325149.
STRINGi7227.FBpp0074609.

Structurei

3D structure databases

ProteinModelPortaliQ23983.
SMRiQ23983. Positions 17-290.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SNAP family.Curated

Phylogenomic databases

eggNOGiKOG1586. Eukaryota.
ENOG410XPQ6. LUCA.
GeneTreeiENSGT00390000005826.
InParanoidiQ23983.
KOiK15296.
OMAiQAGSAFC.
OrthoDBiEOG7FNC80.
PhylomeDBiQ23983.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR000744. NSF_attach.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PANTHERiPTHR13768. PTHR13768. 1 hit.
PRINTSiPR00448. NSFATTACHMNT.
SUPFAMiSSF48452. SSF48452. 1 hit.

Sequencei

Sequence statusi: Complete.

Q23983-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGDNEQKALQ LMAEAEKKLT QQKGFLGSLF GGSNKVEDAI ECYQRAGNMF
60 70 80 90 100
KMSKNWTKAG ECFCEAATLH ARAGSRHDAG TCYVDASNCY KKVDVESAVN
110 120 130 140 150
CLMKSIDIYT DMGRFTMAAK HHQSIAEMYE SDPNNLAKSI QHYEQAADYF
160 170 180 190 200
KGEESVSSAN KCMLKVAQYA AQLEDYEKAI SIYEQVAASS LESSLLKYSA
210 220 230 240 250
KEYFFRAALC HLSVDLLNAQ HAIEKYAQQY PAFQDSREFK LIKVLCENLE
260 270 280 290
EQNIEGFTEA VKDYDSISRL DQWYTTILLR IKKAADEDPD LR
Length:292
Mass (Da):33,000
Last modified:November 1, 1996 - v1
Checksum:i4EE50F038ACFEC5F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09374 mRNA. Translation: AAA83414.1.
AE014296 Genomic DNA. Translation: AAF49035.1.
AY069477 mRNA. Translation: AAL39622.1.
RefSeqiNP_524180.1. NM_079456.4.
UniGeneiDm.2107.

Genome annotation databases

EnsemblMetazoaiFBtr0074840; FBpp0074609; FBgn0250791.
GeneIDi40233.
KEGGidme:Dmel_CG6625.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09374 mRNA. Translation: AAA83414.1.
AE014296 Genomic DNA. Translation: AAF49035.1.
AY069477 mRNA. Translation: AAL39622.1.
RefSeqiNP_524180.1. NM_079456.4.
UniGeneiDm.2107.

3D structure databases

ProteinModelPortaliQ23983.
SMRiQ23983. Positions 17-290.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi65495. 29 interactions.
DIPiDIP-19393N.
IntActiQ23983. 33 interactions.
MINTiMINT-325149.
STRINGi7227.FBpp0074609.

Proteomic databases

PaxDbiQ23983.
PRIDEiQ23983.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0074840; FBpp0074609; FBgn0250791.
GeneIDi40233.
KEGGidme:Dmel_CG6625.

Organism-specific databases

CTDi40233.
FlyBaseiFBgn0250791. alphaSnap.

Phylogenomic databases

eggNOGiKOG1586. Eukaryota.
ENOG410XPQ6. LUCA.
GeneTreeiENSGT00390000005826.
InParanoidiQ23983.
KOiK15296.
OMAiQAGSAFC.
OrthoDBiEOG7FNC80.
PhylomeDBiQ23983.

Enzyme and pathway databases

ReactomeiR-DME-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-DME-6807878. COPI-mediated anterograde transport.
R-DME-6811434. COPI-dependent Golgi-to-ER retrograde traffic.
R-DME-6811438. Intra-Golgi traffic.
R-DME-6811440. Retrograde transport at the Trans-Golgi-Network.

Miscellaneous databases

ChiTaRSiSnap25. fly.
GenomeRNAii40233.
PROiQ23983.

Gene expression databases

BgeeiQ23983.
GenevisibleiQ23983. DM.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR000744. NSF_attach.
IPR011990. TPR-like_helical_dom.
[Graphical view]
PANTHERiPTHR13768. PTHR13768. 1 hit.
PRINTSiPR00448. NSFATTACHMNT.
SUPFAMiSSF48452. SSF48452. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Neurally expressed Drosophila genes encoding homologs of the NSF and SNAP secretory proteins."
    Ordway R.W., Pallanck L., Ganetzky B.
    Proc. Natl. Acad. Sci. U.S.A. 91:5715-5719(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Head.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  5. Cited for: FUNCTION, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiSNAP_DROME
AccessioniPrimary (citable) accession number: Q23983
Secondary accession number(s): Q541G5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.