NSF2_DROME
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 03-AUG-2022, entry version 178.
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; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; 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 + 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 {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; 93.
DR IntAct; P54351; 4.
DR STRING; 7227.FBpp0082346; -.
DR PaxDb; P54351; -.
DR PRIDE; 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 CTD; 41694; -.
DR FlyBase; FBgn0266464; Nsf2.
DR VEuPathDB; VectorBase:FBgn0266464; -.
DR eggNOG; KOG0741; Eukaryota.
DR GeneTree; ENSGT00530000064085; -.
DR HOGENOM; CLU_008037_2_0_1; -.
DR InParanoid; P54351; -.
DR OMA; IQHVKGM; -.
DR OrthoDB; 197562at2759; -.
DR PhylomeDB; P54351; -.
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; 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 oviduct (Drosophila) and 43 other tissues.
DR ExpressionAtlas; P54351; baseline and differential.
DR Genevisible; P54351; DM.
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: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: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 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..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
