Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9QUL6 (NSF_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vesicle-fusing ATPase

EC=3.6.4.6
Alternative name(s):
N-ethylmaleimide-sensitive fusion protein
Short name=NEM-sensitive fusion protein
Vesicular-fusion protein NSF
Gene names
Name:Nsf
Synonyms:Erg1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length744 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin. Interaction with AMPAR subunit GRIA2 leads to influence GRIA2 membrane cycling.

Catalytic activity

ATP + H2O = ADP + phosphate.

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Subunit structure

Homohexamer. Interacts with GABARAP and GABARAPL2 By similarity. Interacts with GRIA2. Interacts with PLK2, leading to disrupt the interaction with GRIA2. Interacts with MUSK; may regulate MUSK endocytosis and activity By similarity. Interacts with CDK16. Ref.4 Ref.5

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Detected in brain (at protein level). Ref.4

Post-translational modification

Phosphorylation at Ser-569 interferes with homohexamerization By similarity.

Sequence similarities

Belongs to the AAA ATPase family.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCytoplasm
   DomainRepeat
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay PubMed 11062069. Source: GOC

membrane fusion

Traceable author statement PubMed 9697854. Source: UniProtKB

neurotransmitter secretion

Traceable author statement PubMed 9697854. Source: UniProtKB

protein transport

Inferred from mutant phenotype PubMed 11245593. Source: RGD

regulation of exocytosis

Inferred from mutant phenotype PubMed 11245593. Source: RGD

vesicle fusion

Traceable author statement PubMed 9697854. Source: UniProtKB

vesicle-mediated transport

Inferred from mutant phenotype PubMed 11245593. Source: RGD

   Cellular_componentGolgi stack

Inferred from direct assay PubMed 11062069. Source: RGD

dendritic shaft

Inferred from direct assay PubMed 1041498. Source: UniProtKB

postsynaptic density

Traceable author statement PubMed 9697854. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent protein binding

Inferred from physical interaction PubMed 11062069. Source: RGD

ATPase activity

Traceable author statement PubMed 9697854. Source: UniProtKB

D1 dopamine receptor binding

Inferred from physical interaction PubMed 20623535. Source: RGD

Rab GTPase binding

Inferred from direct assay PubMed 11062069. Source: RGD

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein C-terminus binding

Inferred from physical interaction PubMed 9697854. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 9697854. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Gria2P194915EBI-925794,EBI-77718

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 744744Vesicle-fusing ATPase
PRO_0000263087

Regions

Nucleotide binding505 – 5106ATP By similarity
Nucleotide binding545 – 5528ATP By similarity

Sites

Metal binding5501Magnesium By similarity

Amino acid modifications

Modified residue1051N6-acetyllysine By similarity
Modified residue2591Phosphotyrosine By similarity
Modified residue5691Phosphoserine; by CDK16 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9QUL6 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 82978187FC3E0E03

FASTA74482,652
        10         20         30         40         50         60 
MAGRTMQAAR CPTDELSLSN CAVVNEKDYQ SGQHVMVRTS PNHKYIFTLR THPSVVPGCI 

        70         80         90        100        110        120 
AFSLPQRKWA GLSIGQDIEV ALYSFDKAKQ CIGTMTIEID FLQKKNIDSN PYDTDKMAAE 

       130        140        150        160        170        180 
FIQQFNHQAF SVGQQLVFSF NDKLFGLLVK DIEAMDPSIL KGEPASGKRQ KIEVGLVVGN 

       190        200        210        220        230        240 
SQVAFEKAEN SSLNLIGKAK TKENRQSIIN PDWNFEKMGI GGLDKEFSDI FRRAFASRVF 

       250        260        270        280        290        300 
PPEIVEQMGC KHVKGILLYG PPGCGKTLLA RQIGKMLNAR EPKVVNGPEI LNKYVGESEA 

       310        320        330        340        350        360 
NIRKLFADAE EEQRRLGANS GLHIIIFDEI DAICKQRGSM AGSTGVHDTV VNQLLSKIDG 

       370        380        390        400        410        420 
VEQLNNILVI GMTNRPDLID EALLRPGRLE VKMEIGLPDE KGRLQILHIH TARMRGHQLL 

       430        440        450        460        470        480 
SADVDIKELA VETKNFSGAE LEGLVRAAQS TAMNRHIKAS TKVEVDMEKA ESLQVTRGDF 

       490        500        510        520        530        540 
LASLENDIKP AFGTNQEDYA SYIMNGIIKW GDPVTRVLDD GELLVQQTKN SDRTPLVSVL 

       550        560        570        580        590        600 
LEGPPHSGKT ALAAKIAEES NFPFIKICSP DKMIGFSETA KCQAMKKIFD DAYKSQLSCV 

       610        620        630        640        650        660 
VVDDIERLLD YVPIGPRFSN LVLQALLVLL KKAPPQGRKL LIIGTTSRKD VLQEMEMLNA 

       670        680        690        700        710        720 
FSTTIHVPNI ATGEQLLEAL ELLGNFKDKE RTTIAQQVKG KKVWIGIKKL LMLIEMSLQM 

       730        740 
DPEYRVRKFL ALMREEGASP LDFD 

« Hide

References

[1]Guan Z., Lu L.R., Zheng Z.C., Liu X.Y.
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Brain.
[2]Viswanathan V., Vincent S.R.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
[3]Lubec G., Afjehi-Sadat L., Diao W.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 11-27; 69-87; 170-187; 218-232; 255-266; 316-335; 338-357; 404-413; 435-446; 534-549; 556-566; 595-631 AND 708-725, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus and Spinal cord.
[4]"Pctaire1 phosphorylates N-ethylmaleimide-sensitive fusion protein: implications in the regulation of its hexamerization and exocytosis."
Liu Y., Cheng K., Gong K., Fu A.K., Ip N.Y.
J. Biol. Chem. 281:9852-9858(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDK16, TISSUE SPECIFICITY.
[5]"Plk2 attachment to NSF induces homeostatic removal of GluA2 during chronic overexcitation."
Evers D.M., Matta J.A., Hoe H.S., Zarkowsky D., Lee S.H., Isaac J.T., Pak D.T.
Nat. Neurosci. 13:1199-1207(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GRIA2 AND NSF.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF142097 mRNA. Translation: AAD39485.1.
AF189019 mRNA. Translation: AAF01051.1.
RefSeqNP_068516.1. NM_021748.1.
UniGeneRn.13345.

3D structure databases

ProteinModelPortalQ9QUL6.
SMRQ9QUL6. Positions 1-201, 489-735.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248797. 1 interaction.
IntActQ9QUL6. 4 interactions.
MINTMINT-4567036.

PTM databases

PhosphoSiteQ9QUL6.

2D gel databases

World-2DPAGE0004:Q9QUL6.

Proteomic databases

PaxDbQ9QUL6.
PRIDEQ9QUL6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID60355.
KEGGrno:60355.
UCSCRGD:621594. rat.

Organism-specific databases

CTD4905.
RGD621594. Nsf.

Phylogenomic databases

eggNOGCOG0464.
HOGENOMHOG000198544.
HOVERGENHBG000324.
InParanoidQ9QUL6.
KOK06027.
PhylomeDBQ9QUL6.

Gene expression databases

GenevestigatorQ9QUL6.

Family and domain databases

Gene3D3.10.330.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR003593. 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]
PfamPF00004. AAA. 2 hits.
PF02933. CDC48_2. 1 hit.
PF02359. CDC48_N. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 2 hits.
SM01072. CDC48_2. 1 hit.
SM01073. CDC48_N. 1 hit.
[Graphical view]
SUPFAMSSF50692. SSF50692. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF54585. SSF54585. 1 hit.
PROSITEPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio612027.
PROQ9QUL6.

Entry information

Entry nameNSF_RAT
AccessionPrimary (citable) accession number: Q9QUL6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families