ID   NSF1_DROME              Reviewed;         745 AA.
AC   P46461; Q9VYF4;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   24-JAN-2024, entry version 205.
DE   RecName: Full=Vesicle-fusing ATPase 1;
DE            EC=3.6.4.6;
DE   AltName: Full=N-ethylmaleimide-sensitive fusion protein 1;
DE            Short=NEM-sensitive fusion protein 1;
DE   AltName: Full=Protein comatose;
DE   AltName: Full=Vesicular-fusion protein NSF1;
DE   AltName: Full=dNsf-1;
DE            Short=NSF-1;
GN   Name=comt; Synonyms=Nsf, Nsf1; ORFNames=CG1618;
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 (AUG-2003) to the EMBL/GenBank/DDBJ databases.
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.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; 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.
CC   -!- TISSUE SPECIFICITY: Nervous system.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR   EMBL; U09373; AAA83413.1; -; mRNA.
DR   EMBL; AE014298; AAF48244.2; -; Genomic_DNA.
DR   EMBL; BT010259; AAQ23577.1; -; mRNA.
DR   RefSeq; NP_001259506.1; NM_001272577.2.
DR   RefSeq; NP_524877.1; NM_080138.4.
DR   AlphaFoldDB; P46461; -.
DR   SMR; P46461; -.
DR   BioGRID; 70577; 15.
DR   DIP; DIP-20666N; -.
DR   IntAct; P46461; 9.
DR   STRING; 7227.FBpp0073585; -.
DR   PaxDb; 7227-FBpp0305521; -.
DR   DNASU; 47091; -.
DR   EnsemblMetazoa; FBtr0073754; FBpp0073585; FBgn0000346.
DR   EnsemblMetazoa; FBtr0333329; FBpp0305521; FBgn0000346.
DR   GeneID; 47091; -.
DR   KEGG; dme:Dmel_CG1618; -.
DR   AGR; FB:FBgn0000346; -.
DR   CTD; 1312; -.
DR   FlyBase; FBgn0000346; comt.
DR   VEuPathDB; VectorBase:FBgn0000346; -.
DR   eggNOG; KOG0741; Eukaryota.
DR   GeneTree; ENSGT00530000064085; -.
DR   HOGENOM; CLU_008037_2_0_1; -.
DR   InParanoid; P46461; -.
DR   OMA; GVINWGT; -.
DR   OrthoDB; 553800at2759; -.
DR   PhylomeDB; P46461; -.
DR   BRENDA; 3.6.4.6; 1994.
DR   SignaLink; P46461; -.
DR   BioGRID-ORCS; 47091; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; comt; fly.
DR   GenomeRNAi; 47091; -.
DR   PRO; PR:P46461; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0000346; Expressed in second segment of antenna (Drosophila) and 33 other cell types or tissues.
DR   ExpressionAtlas; P46461; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0005795; C:Golgi stack; IBA:GO_Central.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR   GO; GO:0098527; C:neuromuscular junction of somatic muscle; IDA:FlyBase.
DR   GO; GO:0099523; C:presynaptic cytosol; IDA:SynGO.
DR   GO; GO:0043195; C:terminal bouton; IDA:FlyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISS:FlyBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006914; P:autophagy; IMP:FlyBase.
DR   GO; GO:0007030; P:Golgi organization; IMP:FlyBase.
DR   GO; GO:0090160; P:Golgi to lysosome transport; IMP: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:0007274; P:neuromuscular synaptic transmission; IEP:FlyBase.
DR   GO; GO:0070050; P:neuron cellular homeostasis; IMP:FlyBase.
DR   GO; GO:0007269; P:neurotransmitter secretion; NAS:FlyBase.
DR   GO; GO:1900073; P:regulation of neuromuscular synaptic transmission; IGI:FlyBase.
DR   GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IDA:FlyBase.
DR   GO; GO:0035494; P:SNARE complex disassembly; IDA:FlyBase.
DR   GO; GO:0099504; P:synaptic vesicle cycle; IDA:SynGO.
DR   GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IMP:FlyBase.
DR   GO; GO:0016082; P:synaptic vesicle priming; NAS:FlyBase.
DR   CDD; cd19504; RecA-like_NSF-SEC18_r1-like; 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; 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; PF02359; CDC48_N; 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.
DR   Genevisible; P46461; DM.
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..745
FT                   /note="Vesicle-fusing ATPase 1"
FT                   /id="PRO_0000084566"
FT   BINDING         505..510
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P18708"
FT   BINDING         545..552
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P18708"
FT   BINDING         550
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P18708"
SQ   SEQUENCE   745 AA;  82555 MW;  A34E7B037E91769F CRC64;
     MAYILKATKC PTDELSLTNR AIVNVGDFPE EIKYADISPA PGQHFIFALE KTVEVPSGYV
     GFSLVQRKWA MVSINQELEV RPYRFDASSD VITCVSFETD FLQKKTVSQE PYDSDQMAKE
     FIMQFAGMAL TVGQSLVFNF KDKKLLGLAV KSLEAIDPKS LGEGKDTAMR NVRFGRILGN
     TVVQFEKAEN SSLNLQGKSK GKVVRQSIIN PDWDFGKMGI GGLDKEFNSI FRRAFASRVF
     PPELVEQLGC KHVKGILLYG PPGTGKTLMA RQIGTMLNAR EPKIVNGPQI LDKYVGESEA
     NVRRLFAEAE EEEKRLGPNS GLHIIIFDEI DAICKQRGSV AGNSGVHDTV VNQLLTKIDG
     VDQLNNILVI GMTNRRDMID EALLRPGRLE VQMEISLPNE QGRVQILNIH TKRMREFNKI
     NDDVDNKEIA ALTKNFSGAE LEGLVRAAQS SAMNRLIKAD AKVTVDPEAM EKLKVNRDDF
     LHSLEHDIKP AFGTAQEILD NMLARGVINW GAPVSNLLED GMLYVQQAKA PESSGLVSVL
     VAGAPNSGKT ALAAQLAKMS DFPFVKVCSP EDMVGYTESA KCLHIRKIFD DAYRSMLSCI
     VVDNVERLLD YGSIGPRYSN MTLQALLVLL KKQPPKGRKL LILCTSSRRE VLEEMEMLTA
     FTSVLHVPNL SKPDHVLAVL ENTDIFSKGE IQAIGKKMAG KRVFIGIKKL LGLIDMARQT
     EQSQRAIKFL SKMEEEGGLD MVARQ
//