ID   NSF2_DROME              Reviewed;         752 AA.
AC   P54351; Q494J2; Q9VFQ5;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   02-SEP-2026, entry version 193.
DE   RecName: Full=Vesicle-fusing ATPase 2;
DE            EC=3.6.4.6;
DE   AltName: Full=N-ethylmaleimide-sensitive fusion protein 2;
DE            Short=NEM-sensitive fusion protein 2;
DE   AltName: Full=Vesicular-fusion protein NSF2;
DE   AltName: Full=dNsf-2;
DE            Short=NSF-2;
GN   Name=Nsf2; ORFNames=CG33101;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=Canton-S;
RX   PubMed=7642522; DOI=10.1074/jbc.270.32.18742;
RA   Pallanck L., Ordway R.W., Ramaswami M., Chi W.Y., Krishnan K.S.,
RA   Ganetzky B.;
RT   "Distinct roles for N-ethylmaleimide-sensitive fusion protein (NSF)
RT   suggested by the identification of a second Drosophila NSF homolog.";
RL   J. Biol. Chem. 270:18742-18744(1995).
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., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA   Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 8-752.
RC   TISSUE=Head;
RX   PubMed=7624376; DOI=10.1073/pnas.92.15.7095;
RA   Boulianne G.L., Trimble W.S.;
RT   "Identification of a second homolog of N-ethylmaleimide-sensitive fusion
RT   protein that is expressed in the nervous system and secretory tissues of
RT   Drosophila.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:7095-7099(1995).
CC   -!- FUNCTION: Required for vesicle-mediated transport. Catalyzes the fusion
CC       of transport vesicles within the Golgi cisternae. Is also required for
CC       transport from the endoplasmic reticulum to the Golgi stack. Seems to
CC       function as a fusion protein required for the delivery of cargo
CC       proteins to all compartments of the Golgi stack independent of vesicle
CC       origin (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.6;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P18708};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P18708};
CC   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7642522}.
CC   -!- TISSUE SPECIFICITY: Nervous system and secretory tissues.
CC       {ECO:0000269|PubMed:7642522}.
CC   -!- DEVELOPMENTAL STAGE: The highest levels are detected in embryos before
CC       and during cellularization. After onset of gastrulation the highest
CC       levels of expression appear in embryonic regions that give rise to
CC       endodermal and ectodermal tissues including the midgut and hindgut.
CC       {ECO:0000269|PubMed:7642522}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-9 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC46844.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U30502; AAA75044.1; -; mRNA.
DR   EMBL; AE014297; AAF54995.2; -; Genomic_DNA.
DR   EMBL; BT023784; AAZ41793.1; -; mRNA.
DR   EMBL; U28836; AAC46844.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001287318.1; NM_001300389.1.
DR   RefSeq; NP_001287319.1; NM_001300390.1.
DR   RefSeq; NP_788676.1; NM_176499.2.
DR   AlphaFoldDB; P54351; -.
DR   SMR; P54351; -.
DR   BioGRID; 66772; 95.
DR   FunCoup; P54351; 2133.
DR   IntAct; P54351; 21.
DR   STRING; 7227.FBpp0311095; -.
DR   PaxDb; 7227-FBpp0311095; -.
DR   PeptideAtlas; P54351; -.
DR   DNASU; 41694; -.
DR   EnsemblMetazoa; FBtr0082883; FBpp0082346; FBgn0266464.
DR   EnsemblMetazoa; FBtr0344766; FBpp0311094; FBgn0266464.
DR   EnsemblMetazoa; FBtr0344767; FBpp0311095; FBgn0266464.
DR   GeneID; 41694; -.
DR   KEGG; dme:Dmel_CG33101; -.
DR   AGR; FB:FBgn0290174; -.
DR   CTD; 41694; -.
DR   FlyBase; FBgn0290174; Nsf2.
DR   VEuPathDB; VectorBase:FBgn0266464; -.
DR   eggNOG; KOG0741; Eukaryota.
DR   HOGENOM; CLU_008037_2_0_1; -.
DR   InParanoid; P54351; -.
DR   OMA; CFDNEIA; -.
DR   OrthoDB; 9982946at2759; -.
DR   PhylomeDB; P54351; -.
DR   BRENDA; 3.6.4.6; 1994.
DR   Reactome; R-DME-204005; COPII-mediated vesicle transport.
DR   Reactome; R-DME-416993; Trafficking of GluR2-containing AMPA receptors.
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; P54351; -.
DR   BioGRID-ORCS; 41694; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 41694; -.
DR   PRO; PR:P54351; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0266464; Expressed in adult midgut enterocyte in digestive tract and 179 other cell types or tissues.
DR   ExpressionAtlas; P54351; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR   GO; GO:0005795; C:Golgi stack; IBA:GO_Central.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISS:FlyBase.
DR   GO; GO:0043001; P:Golgi to plasma membrane protein transport; IBA:GO_Central.
DR   GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR   GO; GO:0035002; P:liquid clearance, open tracheal system; HMP:FlyBase.
DR   GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:FlyBase.
DR   GO; GO:0007269; P:neurotransmitter secretion; NAS:FlyBase.
DR   GO; GO:0007424; P:open tracheal system development; HMP:FlyBase.
DR   GO; GO:0008582; P:regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR   GO; GO:0035494; P:SNARE complex disassembly; ISS:FlyBase.
DR   GO; GO:0016082; P:synaptic vesicle priming; NAS:FlyBase.
DR   GO; GO:0007430; P:terminal branching, open tracheal system; HMP:FlyBase.
DR   GO; GO:0060439; P:trachea morphogenesis; IMP:FlyBase.
DR   GO; GO:0016192; P:vesicle-mediated transport; ISS:FlyBase.
DR   CDD; cd19504; RecA-like_NSF-SEC18_r1-like; 1.
DR   FunFam; 2.40.40.20:FF:000032; vesicle-fusing ATPase 2; 1.
DR   FunFam; 3.10.330.10:FF:000010; vesicle-fusing ATPase 2; 1.
DR   FunFam; 1.10.8.60:FF:000026; vesicle-fusing ATPase isoform X1; 1.
DR   FunFam; 1.10.8.60:FF:000031; vesicle-fusing ATPase isoform X1; 1.
DR   FunFam; 3.40.50.300:FF:000166; vesicle-fusing ATPase isoform X1; 1.
DR   FunFam; 3.40.50.300:FF:000187; Vesicular-fusion ATPase SEC18; 1.
DR   Gene3D; 1.10.8.60; -; 2.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.10.330.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR004201; Cdc48_dom2.
DR   InterPro; IPR029067; CDC48_domain_2-like_sf.
DR   InterPro; IPR003338; CDC4_N-term_subdom.
DR   InterPro; IPR054419; NSF_ATPase_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039812; Vesicle-fus_ATPase.
DR   PANTHER; PTHR23078:SF3; VESICLE-FUSING ATPASE; 1.
DR   PANTHER; PTHR23078; VESICULAR-FUSION PROTEIN NSF; 1.
DR   Pfam; PF00004; AAA; 2.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF02933; CDC48_2; 1.
DR   Pfam; PF02359; CDC48_N; 1.
DR   Pfam; PF21964; NSF_ATPase_lid; 1.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01072; CDC48_2; 1.
DR   SMART; SM01073; CDC48_N; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF54585; Cdc48 domain 2-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00674; AAA; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; ER-Golgi transport; Hydrolase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Protein transport; Reference proteome;
KW   Repeat; Transport.
FT   CHAIN           1..752
FT                   /note="Vesicle-fusing ATPase 2"
FT                   /id="PRO_0000084567"
FT   BINDING         510..515
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P18708"
FT   BINDING         550..557
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P18708"
FT   CONFLICT        680
FT                   /note="N -> H (in Ref. 1; AAA75044 and 5; AAC46844)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   752 AA;  83434 MW;  0AEF9E88FC3D18AF CRC64;
     MSIEKAHRMR AIKCPTDELS LTNKAIVNVS DFTEEVKYVD ISPGPGLHYI FALEKISGPE
     LPLGHVGFSL VQRKWATLSI NQEIDVRPYR FDASADIITL VSFETDFLQK KTTTQEPYDS
     DEMAKEFLMQ FAGMPLTVGQ TLVFQFKDKK FLGLAVKTLE AVDPRTVGDS LPKTRNVRFG
     RILGNTVVQF EKAENSVLNL QGRSKGKIVR QSIINPDWDF GKMGIGGLDK EFNAIFRRAF
     ASRVFPPELV EQLGIKHVKG ILLYGPPGTG KTLMARQIGT MLNAREPKIV NGPQILDKYV
     GESEANIRRL FAEAEEEEKR LGPNSGLHII IFDEIDAICK ARGSVAGNSG VHDTVVNQLL
     AKIDGVEQLN NILVIGMTNR RDMIDEALLR PGRLEVQMEI SLPNEQGRVQ ILNIHTKRMR
     DFNKIASDVD NNEIAAKTKN FSGAELEGLV RAAQSTAMNR LIKADSKVHV DPEAMEKLRV
     TRADFLHALD NDIKPAFGAA QEMLENLLAR GIINWGPPVT ELLEDGMLSV QQAKATESSG
     LVSVLIEGAP NSGKSALAAN LAQLSDFPFV KVCSPEDMVG FTESAKCLHI RKIFDDAYRS
     TLSCIVVDNV ERLLDYGPIG PRYSNLTLQA LLVLLKKQPP KGRKLLILCT SSRRDVLEEM
     EMLSAFTSVL HVSNLSTPEN VLAVLDDSDL FSPEELQSIA RKMAGKRLCI GIKKLLALID
     MIRQSEPHQR VIKFLSKMEE EGGLEMDRVQ GH
//