NSF_DICDI
ID NSF_DICDI Reviewed; 738 AA.
AC Q75JI3; O15646; Q552E0;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Vesicle-fusing ATPase;
DE EC=3.6.4.6;
DE AltName: Full=N-ethylmaleimide-sensitive factor A;
DE AltName: Full=NEM-sensitive fusion protein A;
DE AltName: Full=Vesicular-fusion protein nfsA;
GN Name=nsfA; ORFNames=DDB_G0276153;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=AX2;
RX PubMed=9511743; DOI=10.1016/s0378-1119(97)00604-5;
RA Weidenhaupt M., Bruckert F., Satre M.;
RT "Identification of the Dictyostelium discoideum homolog of the N-
RT ethylmaleimide-sensitive fusion protein.";
RL Gene 207:53-60(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [4]
RP FUNCTION.
RX PubMed=1730725; DOI=10.1016/s0021-9258(18)46031-0;
RA Lenhard J.M., Mayorga L., Stahl P.D.;
RT "Characterization of endosome-endosome fusion in a cell-free system using
RT Dictyostelium discoideum.";
RL J. Biol. Chem. 267:1896-1903(1992).
RN [5]
RP FUNCTION.
RX PubMed=9422733; DOI=10.1074/jbc.273.2.793;
RA Laurent O., Bruckert F., Adessi C., Satre M.;
RT "In vitro reconstituted Dictyostelium discoideum early endosome fusion is
RT regulated by Rab7 but proceeds in the absence of ATP-Mg2+ from the bulk
RT solution.";
RL J. Biol. Chem. 273:793-799(1998).
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SNPA AND SNPC.
RX PubMed=10727946; DOI=10.1046/j.1432-1327.2000.01212.x;
RA Weidenhaupt M., Bruckert F., Louwagie M., Garin J., Satre M.;
RT "Functional and molecular identification of novel members of the ubiquitous
RT membrane fusion proteins alpha- and gamma-SNAP (soluble N-ethylmaleimide-
RT sensitive factor-attachment proteins) families in Dictyostelium
RT discoideum.";
RL Eur. J. Biochem. 267:2062-2070(2000).
RN [7]
RP FUNCTION, AND INTERACTION WITH SYN7A.
RX PubMed=10978342; DOI=10.1074/jbc.m006710200;
RA Bogdanovic A., Bruckert F., Morio T., Satre M.;
RT "A syntaxin 7 homologue is present in Dictyostelium discoideum endosomes
RT and controls their homotypic fusion.";
RL J. Biol. Chem. 275:36691-36697(2000).
RN [8]
RP FUNCTION, INTERACTION WITH SYN7A, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12175335; DOI=10.1042/bj20020845;
RA Bogdanovic A., Bennett N., Kieffer S., Louwagie M., Morio T., Garin J.,
RA Satre M., Bruckert F.;
RT "Syntaxin 7, syntaxin 8, Vti1 and VAMP7 (vesicle-associated membrane
RT protein 7) form an active SNARE complex for early macropinocytic
RT compartment fusion in Dictyostelium discoideum.";
RL Biochem. J. 368:29-39(2002).
RN [9]
RP FUNCTION.
RX PubMed=12183371; DOI=10.1242/dev.129.18.4185;
RA Thompson C.R.L., Bretscher M.S.;
RT "Cell polarity and locomotion, as well as endocytosis, depend on NSF.";
RL Development 129:4185-4192(2002).
RN [10]
RP FUNCTION.
RX PubMed=17606987; DOI=10.1242/jcs.007732;
RA Traynor D., Kay R.R.;
RT "Possible roles of the endocytic cycle in cell motility.";
RL J. Cell Sci. 120:2318-2327(2007).
CC -!- FUNCTION: Required for vesicle-mediated transport. Involved in
CC endocytosis and endosome-endosome fusion. May be required for transport
CC from the endoplasmic reticulum to the Golgi stack, and for the fusion
CC of transport vesicles within the Golgi cisternae. Required for cell
CC polarity, locomotion and chemotaxis. {ECO:0000269|PubMed:10978342,
CC ECO:0000269|PubMed:12175335, ECO:0000269|PubMed:12183371,
CC ECO:0000269|PubMed:1730725, ECO:0000269|PubMed:17606987,
CC ECO:0000269|PubMed:9422733, ECO:0000269|PubMed:9511743}.
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; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Interacts with syn7A, snpA and snpC.
CC {ECO:0000269|PubMed:10727946, ECO:0000269|PubMed:10978342,
CC ECO:0000269|PubMed:12175335}.
CC -!- INTERACTION:
CC Q75JI3; Q54NP6: snpA; NbExp=2; IntAct=EBI-1810142, EBI-1810173;
CC Q75JI3; Q9U9R7: snpC; NbExp=2; IntAct=EBI-1810142, EBI-1810184;
CC Q75JI3; Q54JY7: syn7A; NbExp=2; IntAct=EBI-1810142, EBI-1810238;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:10727946}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10727946}; Cytoplasmic side
CC {ECO:0000269|PubMed:10727946}. Endosome membrane
CC {ECO:0000269|PubMed:10727946}; Peripheral membrane protein
CC {ECO:0000269|PubMed:10727946}; Cytoplasmic side
CC {ECO:0000269|PubMed:10727946}.
CC -!- DEVELOPMENTAL STAGE: Expressed in relatively constant amounts
CC throughout the entire differentiation cycle.
CC {ECO:0000269|PubMed:9511743}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; AF006826; AAC48226.1; -; mRNA.
DR EMBL; AAFI02000014; EAL69376.1; -; Genomic_DNA.
DR RefSeq; XP_643273.1; XM_638181.1.
DR AlphaFoldDB; Q75JI3; -.
DR SMR; Q75JI3; -.
DR IntAct; Q75JI3; 3.
DR STRING; 44689.DDB0185052; -.
DR PaxDb; Q75JI3; -.
DR EnsemblProtists; EAL69376; EAL69376; DDB_G0276153.
DR GeneID; 8620316; -.
DR KEGG; ddi:DDB_G0276153; -.
DR dictyBase; DDB_G0276153; nsfA.
DR eggNOG; KOG0741; Eukaryota.
DR HOGENOM; CLU_008037_2_0_1; -.
DR InParanoid; Q75JI3; -.
DR OMA; IQHVKGM; -.
DR PhylomeDB; Q75JI3; -.
DR BRENDA; 3.6.4.6; 1939.
DR Reactome; R-DDI-204005; COPII-mediated vesicle transport.
DR Reactome; R-DDI-6807878; COPI-mediated anterograde transport.
DR Reactome; R-DDI-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-DDI-6811438; Intra-Golgi traffic.
DR Reactome; R-DDI-6811440; Retrograde transport at the Trans-Golgi-Network.
DR PRO; PR:Q75JI3; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048870; P:cell motility; IMP:dictyBase.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IMP:dictyBase.
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:0006909; P:phagocytosis; IMP:dictyBase.
DR GO; GO:0009306; P:protein secretion; IMP:dictyBase.
DR GO; GO:0035494; P:SNARE complex disassembly; IEA:InterPro.
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; 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 SMART; SM00382; AAA; 2.
DR SUPFAM; SSF50692; SSF50692; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54585; SSF54585; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chemotaxis; Cytoplasmic vesicle; Endosome; ER-Golgi transport;
KW Hydrolase; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..738
FT /note="Vesicle-fusing ATPase"
FT /id="PRO_0000327890"
FT BINDING 507..512
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 547..554
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 501
FT /note="F -> L (in Ref. 1; AAC48226)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="E -> D (in Ref. 1; AAC48226)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 738 AA; 82233 MW; CD1AF65CF49BDB64 CRC64;
MSYPPPVGDS IKLKVQASND PEEAFTNRAY LPISSFSFLF PNVQSNLYTT NTNYIKIRVG
ANEYILSASP NKNMKPDSIA LSKALRGWMY VSNNEEVYVE FYDPNPNICG SMKVSIDYLT
KGKQGPKQDS QEIIGKIIDN FNSQYFTFGQ LFYIKNSNST FELRVEAVET NEVPTKDKGW
AIISPATKII LQKMPGSLID IETNGPLVVN QIFTSDWDFE NMGIGGLDAE FRDIFRRAFS
SRIFPPAIVK KLGVNHVKGM LLYGPPGTGK TLIARQIGKM LNGREPKVVS GPSILNKYVG
QSEENIRMLF RDAEIEQKAK GDDSGLHIII FDELDAICKS RGSRQGDSGV GDSVVNQLLA
MIDGVESLNN ILVIGMTNRK DMIDEALLRP GRLEVHVEIS LPDEHGREQI FKIHTAKMRD
QNALDKDVNL ANYAHTTRNY SGAEIEGVVK SAASYAFSRQ VDTKNIKNVE IKPEDIKVCD
QDFKRAITEV TPSFGSTDNQ FESYAENGII NYGPVFDKLL QSGNAFVEQV KKSNRTPMMS
VLLSGRPGCG KSSLAATLAK SSEFPFTRII SPNDLLGYNE SAKASKITKV FEDSYKSPMS
CVVVDEIERL IEYVPIGPRF SNLILQTLAV LFKRTPPKGR KLLVIATTSN PDILKDMDIM
DCFATVLSVP SISTAKEFQT VCFELGFTQK EASEAASFFT SPITIKQIIM IVEMARQEEG
NFIDNFKMCL EDFNIRNF
