Skip Header

 
Contribute Send feedback
Read comments (1) or add your own

Reviewed, UniProtKB/Swiss-Prot P18708 (NSF_CRIGR)

Last modified June 16, 2009. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Protein attributes

Sequence length744 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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. Seem to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin. Ref.2

Catalytic activity

ATP + H2O = ADP + phosphate.

Cofactor

Binds 1 magnesium ion per subunit.

Subunit structure

Interacts with GABARAP and GABARAPL2 By similarity. Homohexamer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the AAA ATPase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GABARAPL1Q9H0R81EBI-925742,EBI-746969From a different organism.
Gria2P194911EBI-925742,EBI-77718From a different organism.
Gria3P194921EBI-925742,EBI-77764From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 744744Vesicle-fusing ATPase
PRO_0000084562

Regions

Nucleotide binding260 – 2678ATP Potential
Nucleotide binding543 – 5508ATP Potential

Sites

Metal binding5501Magnesium

Amino acid modifications

Modified residue2591Phosphotyrosine By similarity

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P18708-1 [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: 2657434] [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: 2542798] [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: 9727495] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 497-742.
[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: 9731775] [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: 10445031] [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: 10559905] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-203.

Cross-references

Sequence databases

X15652 mRNA. Translation: CAA33678.1. Different initiation.
PIRS04235.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1D2NX-ray1.75A487-743[»]
1NSFX-ray1.90A478-744[»]
1QCSX-ray1.90A1-205[»]
1QDNX-ray2.30A/B/C1-203[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP18708. 3 interactions.

Phylogenomic databases

HOVERGENP18708.

Enzyme and pathway databases

BRENDA3.6.4.6. 18.

Family and domain databases

InterProIPR003593. ATPase_AAA+_core.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR003338. ATPase_AAA_VAT_N.
IPR004201. Cell_division_protein_CDC48_2.
IPR001984. Peptidase_S16_C.
[Graphical view]
PfamPF00004. AAA. 2 hits.
PF02933. CDC48_2. 1 hit.
PF02359. CDC48_N. 1 hit.
[Graphical view]
PRINTSPR00830. ENDOLAPTASE.
SMARTSM00382. AAA. 2 hits.
[Graphical view]
PROSITEPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetSearch...

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: June 16, 2009
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents