Vesicle-fusing ATPase - Cricetulus griseus (Chinese hamster)

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P18708 (NSF_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 108. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)

Taxonomic identifier

10029 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Cricetulus

Protein attributes

Sequence length	744 AA.
Sequence status	Complete.
Protein existence	Evidence 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. 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 process	Protein transport Transport
Cellular component	Cytoplasm
Domain	Repeat
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	protein transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell midbody Inferred from direct assay PubMed 15166316. Source: UniProtKB
Molecular_function	ATP 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 744

744

Vesicle-fusing ATPase

PRO_0000084562

Regions

Nucleotide binding

505 – 510

ATP

Nucleotide binding

545 – 552

ATP

Sites

Metal binding

550

Magnesium

Amino acid modifications

Modified residue

259

Phosphotyrosine By similarity

Modified residue

569

Phosphoserine; by CDK16 By similarity

Secondary structure

744

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P18708 [UniParc].

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

FASTA

744

82,536

        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.

PIR

S04235.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D2N	X-ray	1.75	A	487-743	[»]
1NSF	X-ray	1.90	A	478-744	[»]
1QCS	X-ray	1.90	A	1-205	[»]
1QDN	X-ray	2.30	A/B/C	1-203	[»]

ProteinModelPortal

P18708.

SMR

P18708. Positions 1-201, 489-735.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35598N.

IntAct

P18708. 3 interactions.

Proteomic databases

PRIDE

P18708.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

HOVERGEN

HBG000324.

Family and domain databases

Gene3D

2.40.40.20. 1 hit.

InterPro

IPR003593. AAA+_ATPase.
IPR009010. Asp_de-COase-like_dom.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR004201. Cdc48_dom2.
IPR003338. CDC4_N-term_subdom.
[Graphical view]

Pfam

PF00004. AAA. 2 hits.
PF02933. CDC48_2. 1 hit.
PF02359. CDC48_N. 1 hit.
[Graphical view]

SMART

SM00382. AAA. 2 hits.
SM01072. CDC48_2. 1 hit.
SM01073. CDC48_N. 1 hit.
[Graphical view]

SUPFAM

SSF50692. Asp_decarb_fold. 1 hit.

PROSITE

PS00674. AAA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P18708.

Entry information

Entry name

NSF_CRIGR

Accession

Primary (citable) accession number: P18708

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	May 1, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents