Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P18708

- NSF_CRIGR

UniProt

P18708 - NSF_CRIGR

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Vesicle-fusing ATPase

Gene

NSF

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Status
Reviewed - Annotation score: 4 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

Binds 1 magnesium ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi550 – 5501Magnesium

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi505 – 5106ATP
Nucleotide bindingi545 – 5528ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. hydrolase activity Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. protein transport Source: UniProtKB-KW
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

  1. cytoplasm Source: UniProtKB-KW
  2. midbody Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 744744Vesicle-fusing ATPasePRO_0000084562Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei105 – 1051N6-acetyllysineBy similarity
Modified residuei259 – 2591PhosphotyrosineBy similarity
Modified residuei569 – 5691Phosphoserine; by CDK16By similarity

Post-translational modificationi

Phosphorylation at Ser-569 interferes with homohexamerization.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP18708.

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 interactions.

Structurei

Secondary structure

1
744
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107
Helixi14 – 185
Beta strandi22 – 243
Turni26 – 283
Beta strandi34 – 407
Beta strandi43 – 519
Beta strandi59 – 624
Helixi64 – 707
Beta strandi77 – 837
Helixi87 – 904
Beta strandi91 – 10212
Helixi104 – 1063
Beta strandi111 – 1133
Helixi114 – 12512
Beta strandi129 – 1313
Beta strandi135 – 1406
Beta strandi143 – 15412
Beta strandi173 – 1764
Beta strandi182 – 1876
Beta strandi194 – 2007
Turni500 – 5023
Helixi512 – 53019
Beta strandi535 – 5428
Helixi549 – 56012
Beta strandi563 – 5686
Helixi570 – 5723
Helixi578 – 59316
Beta strandi595 – 6028
Helixi605 – 6084
Turni613 – 6164
Helixi620 – 62910
Beta strandi639 – 6479
Helixi649 – 6546
Turni658 – 6603
Beta strandi661 – 6666
Beta strandi670 – 6723
Helixi673 – 68311
Helixi688 – 69811
Beta strandi701 – 7055
Helixi707 – 71711
Helixi722 – 7243
Helixi725 – 73511

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D2NX-ray1.75A487-740[»]
1NSFX-ray1.90A478-744[»]
1QCSX-ray1.90A1-205[»]
1QDNX-ray2.30A/B/C1-203[»]
ProteinModelPortaliP18708.
SMRiP18708. Positions 1-201, 489-735.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18708.

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

HOVERGENiHBG000324.

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X15652 mRNA. Translation: CAA33678.1. Different initiation.
PIRiS04235.
RefSeqiXP_007606206.1. XM_007608016.1.

Genome annotation databases

GeneIDi100770898.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X15652 mRNA. Translation: CAA33678.1 . Different initiation.
PIRi S04235.
RefSeqi XP_007606206.1. XM_007608016.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1D2N X-ray 1.75 A 487-740 [» ]
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 [» ]
ProteinModelPortali P18708.
SMRi P18708. Positions 1-201, 489-735.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-35598N.
IntActi P18708. 3 interactions.

Proteomic databases

PRIDEi P18708.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100770898.

Organism-specific databases

CTDi 4905.

Phylogenomic databases

HOVERGENi HBG000324.

Miscellaneous databases

EvolutionaryTracei P18708.

Family and domain databases

Gene3Di 3.10.330.10. 1 hit.
3.40.50.300. 2 hits.
InterProi IPR003593. 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 ]
Pfami PF00004. AAA. 2 hits.
PF02933. CDC48_2. 1 hit.
PF02359. CDC48_N. 1 hit.
[Graphical view ]
SMARTi SM00382. AAA. 2 hits.
SM01072. CDC48_2. 1 hit.
SM01073. CDC48_N. 1 hit.
[Graphical view ]
SUPFAMi SSF50692. SSF50692. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF54585. SSF54585. 1 hit.
PROSITEi PS00674. AAA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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 ATP ANALOG.
  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.

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: October 29, 2014
This is version 118 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

External Data

Dasty 3