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P18708 (NSF_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
OrganismCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

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. Ref.2

Catalytic activity

ATP + H2O = ADP + phosphate.

Cofactor

Binds 1 magnesium ion per subunit.

Subunit structure

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

Subcellular location

Cytoplasm.

Post-translational modification

Phosphorylation at Ser-569 interferes with homohexamerization By similarity.

Sequence similarities

Belongs to the AAA ATPase family.

Sequence caution

The sequence CAA33678.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCytoplasm
   DomainRepeat
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processprotein transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

midbody

Inferred from direct assay PubMed 15166316. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleoside-triphosphatase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 744744Vesicle-fusing ATPase
PRO_0000084562

Regions

Nucleotide binding505 – 5106ATP
Nucleotide binding545 – 5528ATP

Sites

Metal binding5501Magnesium

Amino acid modifications

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

Secondary structure

................................................................................ 744
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P18708 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: F3E0CEB2CF1BD582

FASTA74482,536
        10         20         30         40         50         60 
MAGRSMQAAR CPTDELSLSN CAVVSEKDYQ SGQHVIVRTS PNHKYIFTLR THPSVVPGSV 

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

       130        140        150        160        170        180 
FIQQFNNQAF 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 ALLREEGASP LDFD 

« Hide

References

[1]"A fusion protein required for vesicle-mediated transport in both mammalian cells and yeast."
Wilson D.W., Wilcox C.A., Flynn G.C., Chen E., Kuang W.-J., Henzel W.J., Block M.R., Ullrich A., Rothman J.E.
Nature 339:355-359(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Ovary.
[2]"Vesicular transport between the endoplasmic reticulum and the Golgi stack requires the NEM-sensitive fusion protein."
Beckers C.J.M., Block M.R., Glick B.S., Rothman J.E., Balch W.E.
Nature 339:397-398(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[3]"Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein."
Lenzen C.U., Steinmann D., Whiteheart S.W., Weis W.I.
Cell 94:525-536(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 497-742 IN COMPLEX WITH ANP.
[4]Erratum
Lenzen C.U., Steinmann D., Whiteheart S.W., Weis W.I.
Cell 95:289-289(1998)
[5]"Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP."
Yu R.C., Hanson P.I., Jahn R., Bruenger A.T.
Nat. Struct. Biol. 5:803-811(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 489-735.
[6]"NSF N-terminal domain crystal structure: models of NSF function."
Yu R.C., Jahn R., Brunger A.T.
Mol. Cell 4:97-107(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-205.
[7]"Crystal structure of the amino-terminal domain of N-ethylmaleimide-sensitive fusion protein."
May A.P., Misura K.M., Whiteheart S.W., Weis W.I.
Nat. Cell Biol. 1:175-182(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-203.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X15652 mRNA. Translation: CAA33678.1. Different initiation.
PIRS04235.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D2NX-ray1.75A487-743[»]
1NSFX-ray1.90A478-744[»]
1QCSX-ray1.90A1-205[»]
1QDNX-ray2.30A/B/C1-203[»]
ProteinModelPortalP18708.
SMRP18708. Positions 1-201, 489-735.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35598N.
IntActP18708. 3 interactions.

Proteomic databases

PRIDEP18708.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG000324.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR003593. AAA+_ATPase.
IPR009010. Asp_de-COase-like_dom.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR004201. Cdc48_dom2.
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.
PROSITEPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP18708.

Entry information

Entry nameNSF_CRIGR
AccessionPrimary (citable) accession number: P18708
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: April 16, 2014
This is version 113 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references