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Protein

Vesicle-fusing ATPase

Gene

NSF

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Involved in vesicle-mediated transport. The ATPase activity of NSF serves to disassemble the SNARE complex, freeing the components for subsequent pairing and fusion events.

Catalytic activityi

ATP + H2O = ADP + phosphate.

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi544 – 5441Magnesium

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi539 – 5468ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT4G04910-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Vesicle-fusing ATPase (EC:3.6.4.6)
Alternative name(s):
N-ethylmaleimide-sensitive fusion protein
Vesicular-fusion protein NSF
Gene namesi
Name:NSF
Ordered Locus Names:At4g04910
ORF Names:T1J1.4
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G04910.

Subcellular locationi

GO - Cellular componenti

  • Golgi apparatus Source: TAIR
  • Golgi stack Source: GO_Central
  • plasma membrane Source: TAIR
  • plasmodesma Source: TAIR
  • vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 742742Vesicle-fusing ATPasePRO_0000084568Add
BLAST

Proteomic databases

PaxDbiQ9M0Y8.
PRIDEiQ9M0Y8.

Interactioni

Subunit structurei

Hexamer. Binds to SNARE-SNAP complexes to form 20S particles (By similarity).By similarity

Protein-protein interaction databases

BioGridi11141. 6 interactions.
IntActiQ9M0Y8. 4 interactions.
MINTiMINT-8061068.
STRINGi3702.AT4G04910.1.

Structurei

3D structure databases

ProteinModelPortaliQ9M0Y8.
SMRiQ9M0Y8. Positions 1-708.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0464.
HOGENOMiHOG000198544.
InParanoidiQ9M0Y8.
KOiK06027.
OMAiKAHRHLY.
PhylomeDBiQ9M0Y8.

Family and domain databases

Gene3Di3.10.330.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR009010. Asp_de-COase-like_dom.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR004201. Cdc48_dom2.
IPR029067. CDC48_domain_2-like.
IPR003338. CDC4_N-term_subdom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 2 hits.
PF02933. CDC48_2. 1 hit.
PF02359. CDC48_N. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 2 hits.
SM01073. CDC48_N. 1 hit.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF54585. SSF54585. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9M0Y8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGRYGSQVM TMTVTNTPSA DLAFTNLAYC SSSDLRQFSV PGSDLFLANV
60 70 80 90 100
ADSFILSLCG HGSIRDGNIA LNAIQRRHAR VSTGDMVSVS RFVPPENFDL
110 120 130 140 150
AMLTLELEFV KKGTKSEQVD AALLSTQLKR KYTNQVLTVG QKATFEYHGT
160 170 180 190 200
NYILTVNRAD VEGQDHTNGI ERGLLSKDTY IVFEASNASG IKIVNQREAA
210 220 230 240 250
SSNIFKHKEF NLESLGIGGL GAEFADIFRR AFASRVFPPH VTSRLGIKHV
260 270 280 290 300
KGMLLFGPPG TGKTLMARQI GKMLNGKDPK IVNGPEVLSK FVGETEKNVR
310 320 330 340 350
DLFADAEQDQ RTLGDASELH VIIFDEIDAI CKSRGSTRDG TGVHDSIVNQ
360 370 380 390 400
LLTKIDGVEA LNNVLLIGMT NRKDLLDEAL LRPGRLEVQV EISLPDEAGR
410 420 430 440 450
LQILQIHTNK MKENSFLGTD INLQELAART KNYSGAELEG VVKSATSYAL
460 470 480 490 500
NRQLSMDDLT KPVEEENIKI TMEDFLHAIY EVQPAFGAST DDLERCRLNG
510 520 530 540 550
MVDCGHRHNH IYKRAMLLVE QVKVSTRSPL VTCLLEGPSG SGKTALAATI
560 570 580 590 600
GIDSDFPYVK IVSAETMIGL SESTKCAHIV KVFEDAYKSP MSIIILDDIE
610 620 630 640 650
RLLEFIAIGP RFSNIISQTL MVLLKRLPPK GKKLLVFGTT SEVTFLESVG
660 670 680 690 700
ISDCFSVTHS VPTLQKEDAK KVLNQLNLFS EDDVDSAAEA LNDMPIKKIY
710 720 730 740
MLIEMAAQGE NGGSAEAIYA GREKININHF YDCLGDFIRF TG
Length:742
Mass (Da):81,487
Last modified:February 1, 2003 - v2
Checksum:i39611058DEAC4A32
GO

Sequence cautioni

The sequence AAD17345.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAB81033.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF128393 Genomic DNA. Translation: AAD17345.1. Sequence problems.
AL161502 Genomic DNA. Translation: CAB81033.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE82440.1.
AY102111 mRNA. Translation: AAM26681.1.
PIRiG85061.
RefSeqiNP_192400.2. NM_116729.3.
UniGeneiAt.33942.
At.67369.

Genome annotation databases

EnsemblPlantsiAT4G04910.1; AT4G04910.1; AT4G04910.
GeneIDi825830.
KEGGiath:AT4G04910.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF128393 Genomic DNA. Translation: AAD17345.1. Sequence problems.
AL161502 Genomic DNA. Translation: CAB81033.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE82440.1.
AY102111 mRNA. Translation: AAM26681.1.
PIRiG85061.
RefSeqiNP_192400.2. NM_116729.3.
UniGeneiAt.33942.
At.67369.

3D structure databases

ProteinModelPortaliQ9M0Y8.
SMRiQ9M0Y8. Positions 1-708.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi11141. 6 interactions.
IntActiQ9M0Y8. 4 interactions.
MINTiMINT-8061068.
STRINGi3702.AT4G04910.1.

Proteomic databases

PaxDbiQ9M0Y8.
PRIDEiQ9M0Y8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G04910.1; AT4G04910.1; AT4G04910.
GeneIDi825830.
KEGGiath:AT4G04910.

Organism-specific databases

GeneFarmi2444. 154.
TAIRiAT4G04910.

Phylogenomic databases

eggNOGiCOG0464.
HOGENOMiHOG000198544.
InParanoidiQ9M0Y8.
KOiK06027.
OMAiKAHRHLY.
PhylomeDBiQ9M0Y8.

Enzyme and pathway databases

BioCyciARA:AT4G04910-MONOMER.

Miscellaneous databases

PROiQ9M0Y8.

Family and domain databases

Gene3Di3.10.330.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR009010. Asp_de-COase-like_dom.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR004201. Cdc48_dom2.
IPR029067. CDC48_domain_2-like.
IPR003338. CDC4_N-term_subdom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 2 hits.
PF02933. CDC48_2. 1 hit.
PF02359. CDC48_N. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 2 hits.
SM01073. CDC48_N. 1 hit.
[Graphical view]
SUPFAMiSSF50692. SSF50692. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF54585. SSF54585. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.

Entry informationi

Entry nameiNSF_ARATH
AccessioniPrimary (citable) accession number: Q9M0Y8
Secondary accession number(s): Q9ZPH6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2003
Last sequence update: February 1, 2003
Last modified: July 22, 2015
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.