NSF1_DROME
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 03-AUG-2022, entry version 199.
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.FBpp0305521; -.
DR PaxDb; P46461; -.
DR PRIDE; P46461; -.
DR DNASU; 47091; -.
DR EnsemblMetazoa; FBtr0073754; FBpp0073585; FBgn0000346.
DR EnsemblMetazoa; FBtr0333329; FBpp0305521; FBgn0000346.
DR GeneID; 47091; -.
DR KEGG; dme:Dmel_CG1618; -.
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; 197562at2759; -.
DR PhylomeDB; P46461; -.
DR BRENDA; 3.6.4.6; 1994.
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; 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 tissues.
DR ExpressionAtlas; P46461; baseline and differential.
DR Genevisible; P46461; DM.
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 Gene3D; 3.40.50.300; -; 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; PTHR23078; 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 SMART; SM00382; AAA; 2.
DR SMART; SM01072; CDC48_2; 1.
DR SMART; SM01073; CDC48_N; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54585; SSF54585; 1.
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..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
