NSF_ARATH
ID NSF_ARATH Reviewed; 742 AA.
AC Q9M0Y8; Q9ZPH6;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 161.
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:29398689};
DE AltName: Full=Vesicular-fusion protein NSF;
GN Name=NSF {ECO:0000303|PubMed:29398689};
GN OrderedLocusNames=At4g04910 {ECO:0000312|Araport:AT4G04910};
GN ORFNames=T1J1.4 {ECO:0000312|EMBL:AAD17345.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF ASP-374.
RX PubMed=29398689; DOI=10.1247/csf.17026;
RA Tanabashi S., Shoda K., Saito C., Sakamoto T., Kurata T., Uemura T.,
RA Nakano A.;
RT "A missense mutation in the NSF gene causes abnormal Golgi morphology in
RT Arabidopsis thaliana.";
RL Cell Struct. Funct. 43:41-51(2018).
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). Required for maintaining the normal morphology
CC of the Golgi apparatus (PubMed:29398689).
CC {ECO:0000250|UniProtKB:P18708, ECO:0000269|PubMed:29398689}.
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 (By similarity). Binds to SNARE-SNAP complexes to
CC form 20S particles (Probable). {ECO:0000250|UniProtKB:P46460,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P54351}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD17345.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB81033.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF128393; AAD17345.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161502; CAB81033.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82440.1; -; Genomic_DNA.
DR EMBL; AY102111; AAM26681.1; -; mRNA.
DR PIR; G85061; G85061.
DR RefSeq; NP_192400.2; NM_116729.4.
DR AlphaFoldDB; Q9M0Y8; -.
DR SMR; Q9M0Y8; -.
DR BioGRID; 11141; 10.
DR IntAct; Q9M0Y8; 4.
DR STRING; 3702.AT4G04910.1; -.
DR iPTMnet; Q9M0Y8; -.
DR PaxDb; Q9M0Y8; -.
DR PRIDE; Q9M0Y8; -.
DR ProteomicsDB; 249130; -.
DR EnsemblPlants; AT4G04910.1; AT4G04910.1; AT4G04910.
DR GeneID; 825830; -.
DR Gramene; AT4G04910.1; AT4G04910.1; AT4G04910.
DR KEGG; ath:AT4G04910; -.
DR Araport; AT4G04910; -.
DR TAIR; locus:2135378; AT4G04910.
DR eggNOG; KOG0741; Eukaryota.
DR HOGENOM; CLU_008037_2_0_1; -.
DR InParanoid; Q9M0Y8; -.
DR OMA; IQHVKGM; -.
DR OrthoDB; 197562at2759; -.
DR PhylomeDB; Q9M0Y8; -.
DR BioCyc; ARA:AT4G04910-MON; -.
DR PRO; PR:Q9M0Y8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9M0Y8; baseline and differential.
DR Genevisible; Q9M0Y8; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005795; C:Golgi stack; IBA:GO_Central.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IGI:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
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:0035494; P:SNARE complex disassembly; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:TAIR.
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; 2.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF02933; CDC48_2; 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 Repeat; Transport.
FT CHAIN 1..742
FT /note="Vesicle-fusing ATPase"
FT /id="PRO_0000084568"
FT BINDING 499..504
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P18708"
FT BINDING 539..546
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P18708"
FT BINDING 544
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P18708"
FT MUTAGEN 374
FT /note="D->N: Abnormalities in the size and shape of the
FT Golgi apparatus, but normal growth and fertility."
FT /evidence="ECO:0000269|PubMed:29398689"
SQ SEQUENCE 742 AA; 81487 MW; 39611058DEAC4A32 CRC64;
MAGRYGSQVM TMTVTNTPSA DLAFTNLAYC SSSDLRQFSV PGSDLFLANV ADSFILSLCG
HGSIRDGNIA LNAIQRRHAR VSTGDMVSVS RFVPPENFDL AMLTLELEFV KKGTKSEQVD
AALLSTQLKR KYTNQVLTVG QKATFEYHGT NYILTVNRAD VEGQDHTNGI ERGLLSKDTY
IVFEASNASG IKIVNQREAA SSNIFKHKEF NLESLGIGGL GAEFADIFRR AFASRVFPPH
VTSRLGIKHV KGMLLFGPPG TGKTLMARQI GKMLNGKDPK IVNGPEVLSK FVGETEKNVR
DLFADAEQDQ RTLGDASELH VIIFDEIDAI CKSRGSTRDG TGVHDSIVNQ LLTKIDGVEA
LNNVLLIGMT NRKDLLDEAL LRPGRLEVQV EISLPDEAGR LQILQIHTNK MKENSFLGTD
INLQELAART KNYSGAELEG VVKSATSYAL NRQLSMDDLT KPVEEENIKI TMEDFLHAIY
EVQPAFGAST DDLERCRLNG MVDCGHRHNH IYKRAMLLVE QVKVSTRSPL VTCLLEGPSG
SGKTALAATI GIDSDFPYVK IVSAETMIGL SESTKCAHIV KVFEDAYKSP MSIIILDDIE
RLLEFIAIGP RFSNIISQTL MVLLKRLPPK GKKLLVFGTT SEVTFLESVG ISDCFSVTHS
VPTLQKEDAK KVLNQLNLFS EDDVDSAAEA LNDMPIKKIY MLIEMAAQGE NGGSAEAIYA
GREKININHF YDCLGDFIRF TG
