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Protein

Vesicle-fusing ATPase

Gene

NSF

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg2+ ion per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi550Magnesium1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi505 – 510ATP1 Publication1 Publication6
Nucleotide bindingi545 – 552ATP1 Publication1 Publication8

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
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 namesi
Name:NSF
OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifieri10029 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • midbody Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000845621 – 744Vesicle-fusing ATPaseAdd BLAST744

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei105N6-acetyllysineBy similarity1
Modified residuei207PhosphoserineBy similarity1
Modified residuei259PhosphotyrosineBy similarity1
Modified residuei569Phosphoserine; by CDK16By similarity1

Post-translational modificationi

Phosphorylation at Ser-569 interferes with homohexamerization.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP18708.

PTM databases

iPTMnetiP18708.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

DIPiDIP-35598N.
IntActiP18708. 3 interactors.

Structurei

Secondary structure

1744
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 10Combined sources7
Helixi14 – 18Combined sources5
Beta strandi22 – 24Combined sources3
Turni26 – 28Combined sources3
Beta strandi34 – 40Combined sources7
Beta strandi43 – 51Combined sources9
Beta strandi59 – 62Combined sources4
Helixi64 – 70Combined sources7
Beta strandi77 – 83Combined sources7
Helixi87 – 90Combined sources4
Beta strandi91 – 102Combined sources12
Helixi104 – 106Combined sources3
Beta strandi111 – 113Combined sources3
Helixi114 – 125Combined sources12
Beta strandi129 – 131Combined sources3
Beta strandi135 – 140Combined sources6
Beta strandi143 – 154Combined sources12
Beta strandi173 – 176Combined sources4
Beta strandi182 – 187Combined sources6
Beta strandi194 – 200Combined sources7
Turni500 – 502Combined sources3
Helixi512 – 530Combined sources19
Beta strandi535 – 542Combined sources8
Helixi549 – 560Combined sources12
Beta strandi563 – 568Combined sources6
Helixi570 – 572Combined sources3
Helixi578 – 593Combined sources16
Beta strandi595 – 602Combined sources8
Helixi605 – 608Combined sources4
Turni613 – 616Combined sources4
Helixi620 – 629Combined sources10
Beta strandi639 – 647Combined sources9
Helixi649 – 654Combined sources6
Turni658 – 660Combined sources3
Beta strandi661 – 666Combined sources6
Beta strandi670 – 672Combined sources3
Helixi673 – 683Combined sources11
Helixi688 – 698Combined sources11
Beta strandi701 – 705Combined sources5
Helixi707 – 717Combined sources11
Helixi722 – 724Combined sources3
Helixi725 – 735Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D2NX-ray1.75A487-740[»]
1NSFX-ray1.90A478-744[»]
1QCSX-ray1.90A1-205[»]
1QDNX-ray2.30A/B/C1-203[»]
3J94electron microscopy4.20A/B/C/D/E/F1-744[»]
3J95electron microscopy7.60A/B/C/D/E/F1-744[»]
3J96electron microscopy7.60A/B/C/D/E/F1-744[»]
3J97electron microscopy7.80A/B/C/D/E/F1-744[»]
3J98electron microscopy8.40A/B/C/D/E/F1-744[»]
3J99electron microscopy8.20A/B/C/D/E/F1-744[»]
ProteinModelPortaliP18708.
SMRiP18708.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18708.

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

HOVERGENiHBG000324.
KOiK06027.

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.
SM01072. CDC48_2. 1 hit.
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.

P18708-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGRSMQAAR CPTDELSLSN CAVVSEKDYQ SGQHVIVRTS PNHKYIFTLR
60 70 80 90 100
THPSVVPGSV AFSLPQRKWA GLSIGQEIEV ALYSFDKAKQ CIGTMTIEID
110 120 130 140 150
FLQKKNIDSN PYDTDKMAAE FIQQFNNQAF SVGQQLVFSF NDKLFGLLVK
160 170 180 190 200
DIEAMDPSIL KGEPASGKRQ KIEVGLVVGN SQVAFEKAEN SSLNLIGKAK
210 220 230 240 250
TKENRQSIIN PDWNFEKMGI GGLDKEFSDI FRRAFASRVF PPEIVEQMGC
260 270 280 290 300
KHVKGILLYG PPGCGKTLLA RQIGKMLNAR EPKVVNGPEI LNKYVGESEA
310 320 330 340 350
NIRKLFADAE EEQRRLGANS GLHIIIFDEI DAICKQRGSM AGSTGVHDTV
360 370 380 390 400
VNQLLSKIDG VEQLNNILVI GMTNRPDLID EALLRPGRLE VKMEIGLPDE
410 420 430 440 450
KGRLQILHIH TARMRGHQLL SADVDIKELA VETKNFSGAE LEGLVRAAQS
460 470 480 490 500
TAMNRHIKAS TKVEVDMEKA ESLQVTRGDF LASLENDIKP AFGTNQEDYA
510 520 530 540 550
SYIMNGIIKW GDPVTRVLDD GELLVQQTKN SDRTPLVSVL LEGPPHSGKT
560 570 580 590 600
ALAAKIAEES NFPFIKICSP DKMIGFSETA KCQAMKKIFD DAYKSQLSCV
610 620 630 640 650
VVDDIERLLD YVPIGPRFSN LVLQALLVLL KKAPPQGRKL LIIGTTSRKD
660 670 680 690 700
VLQEMEMLNA FSTTIHVPNI ATGEQLLEAL ELLGNFKDKE RTTIAQQVKG
710 720 730 740
KKVWIGIKKL LMLIEMSLQM DPEYRVRKFL ALLREEGASP LDFD
Length:744
Mass (Da):82,536
Last modified:November 1, 1990 - v1
Checksum:iF3E0CEB2CF1BD582
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15652 mRNA. Translation: CAA33678.1. Different initiation.
PIRiS04235.
RefSeqiXP_007606206.1. XM_007608016.1.

Genome annotation databases

GeneIDi100770898.
KEGGicge:100770898.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15652 mRNA. Translation: CAA33678.1. Different initiation.
PIRiS04235.
RefSeqiXP_007606206.1. XM_007608016.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D2NX-ray1.75A487-740[»]
1NSFX-ray1.90A478-744[»]
1QCSX-ray1.90A1-205[»]
1QDNX-ray2.30A/B/C1-203[»]
3J94electron microscopy4.20A/B/C/D/E/F1-744[»]
3J95electron microscopy7.60A/B/C/D/E/F1-744[»]
3J96electron microscopy7.60A/B/C/D/E/F1-744[»]
3J97electron microscopy7.80A/B/C/D/E/F1-744[»]
3J98electron microscopy8.40A/B/C/D/E/F1-744[»]
3J99electron microscopy8.20A/B/C/D/E/F1-744[»]
ProteinModelPortaliP18708.
SMRiP18708.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35598N.
IntActiP18708. 3 interactors.

PTM databases

iPTMnetiP18708.

Proteomic databases

PRIDEiP18708.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100770898.
KEGGicge:100770898.

Organism-specific databases

CTDi4905.

Phylogenomic databases

HOVERGENiHBG000324.
KOiK06027.

Miscellaneous databases

EvolutionaryTraceiP18708.

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.
SM01072. CDC48_2. 1 hit.
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...

Entry informationi

Entry nameiNSF_CRIGR
AccessioniPrimary (citable) accession number: P18708
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: November 2, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.