NSF_ORYSJ
ID NSF_ORYSJ Reviewed; 743 AA.
AC Q0DGP6; Q65X08;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2020, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Vesicle-fusing ATPase {ECO:0000305};
DE EC=3.6.4.6 {ECO:0000305};
DE AltName: Full=N-ethylmaleimide-sensitive fusion protein {ECO:0000303|PubMed:32471860};
DE AltName: Full=Vesicular-fusion protein Sec18 {ECO:0000303|PubMed:25848690};
DE Short=OsSec18 {ECO:0000303|PubMed:25848690};
GN Name=NSF {ECO:0000303|PubMed:32471860};
GN Synonyms=SEC18 {ECO:0000303|PubMed:25848690};
GN OrderedLocusNames=Os05g0519400 {ECO:0000312|EMBL:BAF17977.1},
GN LOC_Os05g44310 {ECO:0000305};
GN ORFNames=OsJ_19229 {ECO:0000312|EMBL:EEE64387.1},
GN P0599F04.10 {ECO:0000312|EMBL:AAU44261.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP FUNCTION, INTERACTION WITH 60SP0, AND TISSUE SPECIFICITY.
RX PubMed=25848690; DOI=10.1186/s12870-014-0324-1;
RA Sun Y., Ning T., Liu Z., Pang J., Jiang D., Guo Z., Song G., Yang D.;
RT "The OsSec18 complex interacts with P0(P1-P2)2 to regulate vacuolar
RT morphology in rice endosperm cell.";
RL BMC Plant Biol. 15:55-55(2015).
RN [8]
RP FUNCTION, AND INTERACTION WITH RBP-P AND RAB5A.
RX PubMed=32471860; DOI=10.1105/tpc.20.00111;
RA Tian L., Doroshenk K.A., Zhang L., Fukuda M., Washida H., Kumamaru T.,
RA Okita T.;
RT "Zipcode RNA-binding proteins and membrane trafficking proteins cooperate
RT to transport glutelin mRNAs in rice endosperm.";
RL Plant Cell 32:2566-2581(2020).
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). Involved in spikelet development
CC (PubMed:25848690). Regulates protein storage vacuole (PSV) morphology
CC in endosperm cells (PubMed:25848690). Forms a quaternary complex with
CC the two glutelin zipcode RNA-binding proteins RBP-L and RBP-P, and the
CC membrane trafficking factor RAB5A (PubMed:32471860). This quaternay
CC complex carries glutelin mRNAs for active transport on endosomes to the
CC cortical endoplasmic reticulum membrane, and enables endosome-mediated
CC glutelin mRNA transport in endosperm cells (PubMed:32471860).
CC {ECO:0000250|UniProtKB:P18708, ECO:0000269|PubMed:25848690,
CC ECO:0000269|PubMed:32471860}.
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 Evidence={ECO:0000305};
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 (By similarity). Binds to SNARE-SNAP complexes to
CC form 20S particles (Probable). Interacts with the 60S acidic ribosomal
CC protein P0 (60SP0) (PubMed:25848690). Forms a complex with the
CC heterologous pentameric complex formed by P0 and dimers of P1 and P2
CC (PubMed:25848690). Interacts with RBP-P and RAB5A (PubMed:32471860).
CC {ECO:0000250|UniProtKB:P46460, ECO:0000269|PubMed:25848690,
CC ECO:0000269|PubMed:32471860, ECO:0000305|PubMed:32471860}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P54351}.
CC -!- TISSUE SPECIFICITY: Highly expressed in stems, inflorescences and
CC immature seeds (at protein level) (PubMed:25848690). Expressed in
CC leaves and mature seeds (at protein level) (PubMed:25848690).
CC {ECO:0000269|PubMed:25848690}.
CC -!- MISCELLANEOUS: Overexpression of NSF decreases plant height and grain
CC weight, and alters the morphology of protein bodies.
CC {ECO:0000269|PubMed:25848690}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; AC132491; AAU44261.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF17977.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS94917.1; -; Genomic_DNA.
DR EMBL; CM000142; EEE64387.1; -; Genomic_DNA.
DR EMBL; AK072976; BAG93228.1; -; mRNA.
DR RefSeq; XP_015640101.1; XM_015784615.1.
DR AlphaFoldDB; Q0DGP6; -.
DR SMR; Q0DGP6; -.
DR STRING; 4530.OS05T0519400-01; -.
DR EnsemblPlants; Os05t0519400-01; Os05t0519400-01; Os05g0519400.
DR GeneID; 4339340; -.
DR Gramene; Os05t0519400-01; Os05t0519400-01; Os05g0519400.
DR KEGG; osa:4339340; -.
DR eggNOG; KOG0741; Eukaryota.
DR HOGENOM; CLU_008037_2_0_1; -.
DR OMA; IQHVKGM; -.
DR OrthoDB; 197562at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000007752; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IDA:UniProtKB.
DR GO; GO:1990019; P:protein storage vacuole organization; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; 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; PF02359; CDC48_N; 1.
DR SMART; SM00382; AAA; 2.
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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; ER-Golgi transport; Hydrolase; Magnesium;
KW Metal-binding; Nucleotide-binding; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..743
FT /note="Vesicle-fusing ATPase"
FT /id="PRO_0000451593"
FT BINDING 502..507
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P18708"
FT BINDING 542..549
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P18708"
FT BINDING 547
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P18708"
SQ SEQUENCE 743 AA; 81129 MW; 82F0ECAEE3B4D6B1 CRC64;
MAGRNYHGYG GGGGGGMSMV VASTPGQELA LTNCAYVSSA DIRRFPNALA LVGDAFVFTL
RAHDAVSAGS IALNAIQRRQ TKVSAGDSIT VSSFAPPDDF KLALLTLELE YTKARTNRNE
ELDAVVLAQQ LRRRFLDQVM TSGQRVPFEF CGTNYIFTVN QALLDGQENS TPLDRGFLSS
DTYIIFEAAP NSGIKVVNQK EAASSKLFKH KEFNLEKLGI GGLSAEFTDI FRRAFASRVF
PPHVVNKLGI KHVKGILLYG PPGTGKTLMA RQIGKLLNGN EPKIVNGPEV LSKFVGETEK
NVRDLFADAE NDQKTRGDQS DLHVIIFDEI DAICKSRGST RDGTGVHDSI VNQLLTKIDG
VEALNNVLLI GMTNRKDLLD EALLRPGRLE VHIEINLPDE NGRLQILQIH TNKMKESSFL
SPNVNLQELA ARTKNYSGAE LEGVVKSAVS YALNRQISMD DLTKPLDEES IKVTMDDFVN
ALHEITPAFG ASTDDLERCR LRGMVDCGKA HRHLYERGML LVEQVKVSKG SPLVTCLLEG
PAGSGKSALA ATVGIDSDFA YVKIISAETM IGFSESSKCA QICKVFEDAY KSQFGIIILD
DIERLLEYVA IGPRFSNIIS QTLLVLLKRV PPKGKNLLVI GTTSEVGFLE SIGMCDVFSV
TYHVPKLKKE DATKVLRHLN VFDEADIDAA AEALDDMPIK KLYTLVEMAA QGPSGGSAEA
VYGGEEKIDI NHFFSILSDI IRY
