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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_RAT                 Reviewed;         744 AA.
Q9QUL6;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
22-NOV-2017, entry version 125.
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; Synonyms=Erg1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Brain;
Guan Z., Lu L.R., Zheng Z.C., Liu X.Y.;
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
Viswanathan V., Vincent S.R.;
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF 11-27; 69-87; 170-187; 218-232; 255-266; 316-335;
338-357; 404-413; 435-446; 534-549; 556-566; 595-631 AND 708-725, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
Lubec G., Afjehi-Sadat L., Diao W.;
Submitted (APR-2007) to UniProtKB.
[4]
INTERACTION WITH CDK16, AND TISSUE SPECIFICITY.
PubMed=16461345; DOI=10.1074/jbc.M513496200;
Liu Y., Cheng K., Gong K., Fu A.K., Ip N.Y.;
"Pctaire1 phosphorylates N-ethylmaleimide-sensitive fusion protein:
implications in the regulation of its hexamerization and exocytosis.";
J. Biol. Chem. 281:9852-9858(2006).
[5]
INTERACTION WITH GRIA2 AND NSF.
PubMed=20802490; DOI=10.1038/nn.2624;
Evers D.M., Matta J.A., Hoe H.S., Zarkowsky D., Lee S.H., Isaac J.T.,
Pak D.T.;
"Plk2 attachment to NSF induces homeostatic removal of GluA2 during
chronic overexcitation.";
Nat. Neurosci. 13:1199-1207(2010).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P18708};
Note=Binds 1 Mg(2+) ion per subunit.
{ECO:0000250|UniProtKB:P18708};
-!- SUBUNIT: Homohexamer. Interacts with GABARAP and GABARAPL2 (By
similarity). Interacts with GRIA2. Interacts with PLK2, leading to
disrupt the interaction with GRIA2. Interacts with MUSK; may
regulate MUSK endocytosis and activity (By similarity). Interacts
with CDK16. {ECO:0000250, ECO:0000269|PubMed:16461345,
ECO:0000269|PubMed:20802490}.
-!- INTERACTION:
P19491:Gria2; NbExp=5; IntAct=EBI-925794, EBI-77718;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- TISSUE SPECIFICITY: Detected in brain (at protein level).
{ECO:0000269|PubMed:16461345}.
-!- PTM: Phosphorylation at Ser-569 interferes with
homohexamerization. {ECO:0000250}.
-!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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EMBL; AF142097; AAD39485.1; -; mRNA.
EMBL; AF189019; AAF01051.1; -; mRNA.
RefSeq; NP_068516.1; NM_021748.1.
UniGene; Rn.13345; -.
ProteinModelPortal; Q9QUL6; -.
SMR; Q9QUL6; -.
BioGrid; 248797; 3.
CORUM; Q9QUL6; -.
IntAct; Q9QUL6; 4.
MINT; MINT-4567036; -.
STRING; 10116.ENSRNOP00000006361; -.
iPTMnet; Q9QUL6; -.
PhosphoSitePlus; Q9QUL6; -.
World-2DPAGE; 0004:Q9QUL6; -.
PaxDb; Q9QUL6; -.
PRIDE; Q9QUL6; -.
GeneID; 60355; -.
KEGG; rno:60355; -.
UCSC; RGD:621594; rat.
CTD; 4905; -.
RGD; 621594; Nsf.
eggNOG; KOG0741; Eukaryota.
eggNOG; COG0464; LUCA.
HOGENOM; HOG000198544; -.
HOVERGEN; HBG000324; -.
InParanoid; Q9QUL6; -.
KO; K06027; -.
PhylomeDB; Q9QUL6; -.
PRO; PR:Q9QUL6; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0043198; C:dendritic shaft; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005795; C:Golgi stack; IDA:RGD.
GO; GO:0005765; C:lysosomal membrane; ISO:RGD.
GO; GO:0043209; C:myelin sheath; ISO:RGD.
GO; GO:0005886; C:plasma membrane; ISO:RGD.
GO; GO:0014069; C:postsynaptic density; IDA:RGD.
GO; GO:0098793; C:presynapse; IEA:GOC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0043008; F:ATP-dependent protein binding; IPI:RGD.
GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
GO; GO:0042623; F:ATPase activity, coupled; ISO:RGD.
GO; GO:0031748; F:D1 dopamine receptor binding; IPI:RGD.
GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030165; F:PDZ domain binding; ISO:RGD.
GO; GO:0008022; F:protein C-terminus binding; IDA:UniProtKB.
GO; GO:0032403; F:protein complex binding; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; ISO:RGD.
GO; GO:0017137; F:Rab GTPase binding; IDA:RGD.
GO; GO:0000149; F:SNARE binding; ISS:ParkinsonsUK-UCL.
GO; GO:0019905; F:syntaxin binding; ISO:RGD.
GO; GO:0017075; F:syntaxin-1 binding; ISO:RGD.
GO; GO:0006886; P:intracellular protein transport; ISO:RGD.
GO; GO:0061025; P:membrane fusion; TAS:UniProtKB.
GO; GO:0007269; P:neurotransmitter secretion; TAS:UniProtKB.
GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:RGD.
GO; GO:0001921; P:positive regulation of receptor recycling; ISO:RGD.
GO; GO:0006813; P:potassium ion transport; ISO:RGD.
GO; GO:0043241; P:protein complex disassembly; IDA:UniProtKB.
GO; GO:0015031; P:protein transport; IMP:RGD.
GO; GO:0017157; P:regulation of exocytosis; IMP:RGD.
GO; GO:0002090; P:regulation of receptor internalization; IDA:UniProtKB.
GO; GO:0035494; P:SNARE complex disassembly; ISS:ParkinsonsUK-UCL.
GO; GO:0006906; P:vesicle fusion; TAS:UniProtKB.
GO; GO:0016192; P:vesicle-mediated transport; IMP:RGD.
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;
Acetylation; ATP-binding; Complete proteome; Cytoplasm;
Direct protein sequencing; Hydrolase; Magnesium; Metal-binding;
Nucleotide-binding; Phosphoprotein; Protein transport;
Reference proteome; Repeat; Transport.
CHAIN 1 744 Vesicle-fusing ATPase.
/FTId=PRO_0000263087.
NP_BIND 505 510 ATP. {ECO:0000250|UniProtKB:P18708}.
NP_BIND 545 552 ATP. {ECO:0000250|UniProtKB:P18708}.
METAL 550 550 Magnesium.
{ECO:0000250|UniProtKB:P18708}.
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}.
SEQUENCE 744 AA; 82652 MW; 82978187FC3E0E03 CRC64;
MAGRTMQAAR CPTDELSLSN CAVVNEKDYQ SGQHVMVRTS PNHKYIFTLR THPSVVPGCI
AFSLPQRKWA GLSIGQDIEV ALYSFDKAKQ CIGTMTIEID FLQKKNIDSN PYDTDKMAAE
FIQQFNHQAF 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 ALMREEGASP LDFD


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