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Vesicle-fusing ATPase (EC 3.6.4.6) (N-ethylmaleimide-sensitive fusion protein) (NEM-sensitive fusion protein) (Vesicular-fusion protein NSF)

 NSF_CRIGR               Reviewed;         744 AA.
P18708;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1990, sequence version 1.
22-NOV-2017, entry version 137.
RecName: Full=Vesicle-fusing ATPase;
EC=3.6.4.6;
AltName: Full=N-ethylmaleimide-sensitive fusion protein;
Short=NEM-sensitive fusion protein;
AltName: Full=Vesicular-fusion protein NSF;
Name=NSF;
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Cricetidae; Cricetinae; Cricetulus.
NCBI_TaxID=10029;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Ovary;
PubMed=2657434; DOI=10.1038/339355a0;
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.;
"A fusion protein required for vesicle-mediated transport in both
mammalian cells and yeast.";
Nature 339:355-359(1989).
[2]
FUNCTION.
PubMed=2542798; DOI=10.1038/339397a0;
Beckers C.J.M., Block M.R., Glick B.S., Rothman J.E., Balch W.E.;
"Vesicular transport between the endoplasmic reticulum and the Golgi
stack requires the NEM-sensitive fusion protein.";
Nature 339:397-398(1989).
[3]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 487-740 IN COMPLEX WITH ATP
ANALOG.
PubMed=9727495; DOI=10.1016/S0092-8674(00)81593-7;
Lenzen C.U., Steinmann D., Whiteheart S.W., Weis W.I.;
"Crystal structure of the hexamerization domain of N-ethylmaleimide-
sensitive fusion protein.";
Cell 94:525-536(1998).
[4]
ERRATUM.
Lenzen C.U., Steinmann D., Whiteheart S.W., Weis W.I.;
Cell 95:289-289(1998).
[5]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 478-744 IN COMPLEX WITH ATP
AND MAGNESIUM.
PubMed=9731775; DOI=10.1038/1843;
Yu R.C., Hanson P.I., Jahn R., Bruenger A.T.;
"Structure of the ATP-dependent oligomerization domain of N-
ethylmaleimide sensitive factor complexed with ATP.";
Nat. Struct. Biol. 5:803-811(1998).
[6]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-205.
PubMed=10445031; DOI=10.1016/S1097-2765(00)80191-4;
Yu R.C., Jahn R., Brunger A.T.;
"NSF N-terminal domain crystal structure: models of NSF function.";
Mol. Cell 4:97-107(1999).
[7]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-203.
PubMed=10559905; DOI=10.1038/11097;
May A.P., Misura K.M., Whiteheart S.W., Weis W.I.;
"Crystal structure of the amino-terminal domain of N-ethylmaleimide-
sensitive fusion protein.";
Nat. Cell Biol. 1:175-182(1999).
-!- 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.
{ECO:0000269|PubMed:2542798}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000305|PubMed:9731775};
Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000305|PubMed:9731775};
-!- SUBUNIT: 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). {ECO:0000250}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-925742, EBI-925742;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- PTM: Phosphorylation at Ser-569 interferes with
homohexamerization. {ECO:0000250}.
-!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA33678.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; X15652; CAA33678.1; ALT_INIT; mRNA.
PIR; S04235; S04235.
RefSeq; XP_007606206.1; XM_007608016.1.
PDB; 1D2N; X-ray; 1.75 A; A=487-740.
PDB; 1NSF; X-ray; 1.90 A; A=478-744.
PDB; 1QCS; X-ray; 1.90 A; A=1-205.
PDB; 1QDN; X-ray; 2.30 A; A/B/C=1-203.
PDB; 3J94; EM; 4.20 A; A/B/C/D/E/F=1-744.
PDB; 3J95; EM; 7.60 A; A/B/C/D/E/F=1-744.
PDB; 3J96; EM; 7.60 A; A/B/C/D/E/F=1-744.
PDB; 3J97; EM; 7.80 A; A/B/C/D/E/F=1-744.
PDB; 3J98; EM; 8.40 A; A/B/C/D/E/F=1-744.
PDB; 3J99; EM; 8.20 A; A/B/C/D/E/F=1-744.
PDBsum; 1D2N; -.
PDBsum; 1NSF; -.
PDBsum; 1QCS; -.
PDBsum; 1QDN; -.
PDBsum; 3J94; -.
PDBsum; 3J95; -.
PDBsum; 3J96; -.
PDBsum; 3J97; -.
PDBsum; 3J98; -.
PDBsum; 3J99; -.
ProteinModelPortal; P18708; -.
SMR; P18708; -.
DIP; DIP-35598N; -.
IntAct; P18708; 9.
iPTMnet; P18708; -.
PRIDE; P18708; -.
Ensembl; ENSCGRT00001028633; ENSCGRP00001024387; ENSCGRG00001022331.
GeneID; 100770898; -.
KEGG; cge:100770898; -.
CTD; 4905; -.
HOVERGEN; HBG000324; -.
KO; K06027; -.
EvolutionaryTrace; P18708; -.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005765; C:lysosomal membrane; IEA:Ensembl.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IDA:ParkinsonsUK-UCL.
GO; GO:0042623; F:ATPase activity, coupled; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0035255; F:ionotropic glutamate receptor binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030165; F:PDZ domain binding; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IDA:ParkinsonsUK-UCL.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0000149; F:SNARE binding; IDA:ParkinsonsUK-UCL.
GO; GO:0017075; F:syntaxin-1 binding; IEA:Ensembl.
GO; GO:0006886; P:intracellular protein transport; IEA:Ensembl.
GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
GO; GO:0001921; P:positive regulation of receptor recycling; IEA:Ensembl.
GO; GO:0006813; P:potassium ion transport; IEA:Ensembl.
GO; GO:0035494; P:SNARE complex disassembly; IDA:ParkinsonsUK-UCL.
Gene3D; 3.10.330.10; -; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR009010; Asp_de-COase-like_dom_sf.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR003960; ATPase_AAA_CS.
InterPro; IPR004201; Cdc48_dom2.
InterPro; IPR029067; CDC48_domain_2-like_sf.
InterPro; IPR003338; CDC4_N-term_subdom.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00004; AAA; 2.
Pfam; PF02933; CDC48_2; 1.
Pfam; PF02359; CDC48_N; 1.
SMART; SM00382; AAA; 2.
SMART; SM01072; CDC48_2; 1.
SMART; SM01073; CDC48_N; 1.
SUPFAM; SSF50692; SSF50692; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF54585; SSF54585; 1.
PROSITE; PS00674; AAA; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Cytoplasm;
Direct protein sequencing; Hydrolase; Magnesium; Metal-binding;
Nucleotide-binding; Phosphoprotein; Protein transport; Repeat;
Transport.
CHAIN 1 744 Vesicle-fusing ATPase.
/FTId=PRO_0000084562.
NP_BIND 505 510 ATP. {ECO:0000269|PubMed:9731775,
ECO:0000305|PubMed:9727495}.
NP_BIND 545 552 ATP. {ECO:0000269|PubMed:9731775,
ECO:0000305|PubMed:9727495}.
METAL 550 550 Magnesium. {ECO:0000269|PubMed:9731775}.
MOD_RES 105 105 N6-acetyllysine.
{ECO:0000250|UniProtKB:P46460}.
MOD_RES 207 207 Phosphoserine.
{ECO:0000250|UniProtKB:P46459}.
MOD_RES 259 259 Phosphotyrosine.
{ECO:0000250|UniProtKB:P46460}.
MOD_RES 569 569 Phosphoserine; by CDK16.
{ECO:0000250|UniProtKB:P46460}.
STRAND 4 10 {ECO:0000244|PDB:1QCS}.
HELIX 14 18 {ECO:0000244|PDB:1QCS}.
STRAND 22 24 {ECO:0000244|PDB:1QCS}.
TURN 26 28 {ECO:0000244|PDB:1QCS}.
STRAND 34 40 {ECO:0000244|PDB:1QCS}.
STRAND 43 51 {ECO:0000244|PDB:1QCS}.
STRAND 59 62 {ECO:0000244|PDB:1QCS}.
HELIX 64 70 {ECO:0000244|PDB:1QCS}.
STRAND 77 83 {ECO:0000244|PDB:1QCS}.
HELIX 87 90 {ECO:0000244|PDB:1QCS}.
STRAND 91 102 {ECO:0000244|PDB:1QCS}.
HELIX 104 106 {ECO:0000244|PDB:1QCS}.
STRAND 111 113 {ECO:0000244|PDB:1QCS}.
HELIX 114 125 {ECO:0000244|PDB:1QCS}.
STRAND 129 131 {ECO:0000244|PDB:1QCS}.
STRAND 135 140 {ECO:0000244|PDB:1QCS}.
STRAND 143 154 {ECO:0000244|PDB:1QCS}.
STRAND 173 176 {ECO:0000244|PDB:1QCS}.
STRAND 182 187 {ECO:0000244|PDB:1QCS}.
STRAND 194 200 {ECO:0000244|PDB:1QCS}.
TURN 500 502 {ECO:0000244|PDB:1D2N}.
HELIX 512 530 {ECO:0000244|PDB:1D2N}.
STRAND 535 542 {ECO:0000244|PDB:1D2N}.
HELIX 549 560 {ECO:0000244|PDB:1D2N}.
STRAND 563 568 {ECO:0000244|PDB:1D2N}.
HELIX 570 572 {ECO:0000244|PDB:1D2N}.
HELIX 578 593 {ECO:0000244|PDB:1D2N}.
STRAND 595 602 {ECO:0000244|PDB:1D2N}.
HELIX 605 608 {ECO:0000244|PDB:1D2N}.
TURN 613 616 {ECO:0000244|PDB:1D2N}.
HELIX 620 629 {ECO:0000244|PDB:1D2N}.
STRAND 639 647 {ECO:0000244|PDB:1D2N}.
HELIX 649 654 {ECO:0000244|PDB:1D2N}.
TURN 658 660 {ECO:0000244|PDB:1D2N}.
STRAND 661 666 {ECO:0000244|PDB:1D2N}.
STRAND 670 672 {ECO:0000244|PDB:1D2N}.
HELIX 673 683 {ECO:0000244|PDB:1D2N}.
HELIX 688 698 {ECO:0000244|PDB:1D2N}.
STRAND 701 705 {ECO:0000244|PDB:1D2N}.
HELIX 707 717 {ECO:0000244|PDB:1D2N}.
HELIX 722 724 {ECO:0000244|PDB:1D2N}.
HELIX 725 735 {ECO:0000244|PDB:1D2N}.
SEQUENCE 744 AA; 82536 MW; F3E0CEB2CF1BD582 CRC64;
MAGRSMQAAR CPTDELSLSN CAVVSEKDYQ SGQHVIVRTS PNHKYIFTLR THPSVVPGSV
AFSLPQRKWA GLSIGQEIEV ALYSFDKAKQ CIGTMTIEID FLQKKNIDSN PYDTDKMAAE
FIQQFNNQAF SVGQQLVFSF NDKLFGLLVK DIEAMDPSIL KGEPASGKRQ KIEVGLVVGN
SQVAFEKAEN SSLNLIGKAK TKENRQSIIN PDWNFEKMGI GGLDKEFSDI FRRAFASRVF
PPEIVEQMGC KHVKGILLYG PPGCGKTLLA RQIGKMLNAR EPKVVNGPEI LNKYVGESEA
NIRKLFADAE EEQRRLGANS GLHIIIFDEI DAICKQRGSM AGSTGVHDTV VNQLLSKIDG
VEQLNNILVI GMTNRPDLID EALLRPGRLE VKMEIGLPDE KGRLQILHIH TARMRGHQLL
SADVDIKELA VETKNFSGAE LEGLVRAAQS TAMNRHIKAS TKVEVDMEKA ESLQVTRGDF
LASLENDIKP AFGTNQEDYA SYIMNGIIKW GDPVTRVLDD GELLVQQTKN SDRTPLVSVL
LEGPPHSGKT ALAAKIAEES NFPFIKICSP DKMIGFSETA KCQAMKKIFD DAYKSQLSCV
VVDDIERLLD YVPIGPRFSN LVLQALLVLL KKAPPQGRKL LIIGTTSRKD VLQEMEMLNA
FSTTIHVPNI ATGEQLLEAL ELLGNFKDKE RTTIAQQVKG KKVWIGIKKL LMLIEMSLQM
DPEYRVRKFL ALLREEGASP LDFD


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