NSF_RAT
ID NSF_RAT Reviewed; 744 AA.
AC Q9QUL6;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Vesicle-fusing ATPase;
DE EC=3.6.4.6;
DE AltName: Full=N-ethylmaleimide-sensitive fusion protein;
DE Short=NEM-sensitive fusion protein;
DE AltName: Full=Vesicular-fusion protein NSF;
GN Name=Nsf; Synonyms=Erg1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Guan Z., Lu L.R., Zheng Z.C., Liu X.Y.;
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Viswanathan V., Vincent S.R.;
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 11-27; 69-87; 170-187; 218-232; 255-266; 316-335;
RP 338-357; 404-413; 435-446; 534-549; 556-566; 595-631 AND 708-725, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP INTERACTION WITH CDK16, AND TISSUE SPECIFICITY.
RX PubMed=16461345; DOI=10.1074/jbc.m513496200;
RA Liu Y., Cheng K., Gong K., Fu A.K., Ip N.Y.;
RT "Pctaire1 phosphorylates N-ethylmaleimide-sensitive fusion protein:
RT implications in the regulation of its hexamerization and exocytosis.";
RL J. Biol. Chem. 281:9852-9858(2006).
RN [5]
RP INTERACTION WITH GRIA2 AND NSF.
RX PubMed=20802490; DOI=10.1038/nn.2624;
RA Evers D.M., Matta J.A., Hoe H.S., Zarkowsky D., Lee S.H., Isaac J.T.,
RA Pak D.T.;
RT "Plk2 attachment to NSF induces homeostatic removal of GluA2 during chronic
RT overexcitation.";
RL Nat. Neurosci. 13:1199-1207(2010).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Required for vesicle-mediated transport. Catalyzes the fusion
CC of transport vesicles within the Golgi cisternae. Is also required for
CC transport from the endoplasmic reticulum to the Golgi stack. Seems to
CC function as a fusion protein required for the delivery of cargo
CC proteins to all compartments of the Golgi stack independent of vesicle
CC origin. Interaction with AMPAR subunit GRIA2 leads to influence GRIA2
CC membrane cycling.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.6;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P18708};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P18708};
CC -!- SUBUNIT: Homohexamer. Interacts with GABARAP and GABARAPL2 (By
CC similarity). Interacts with GRIA2. Interacts with PLK2, leading to
CC disrupt the interaction with GRIA2. Interacts with MUSK; may regulate
CC MUSK endocytosis and activity (By similarity). Interacts with CDK16.
CC {ECO:0000250, ECO:0000269|PubMed:16461345,
CC ECO:0000269|PubMed:20802490}.
CC -!- INTERACTION:
CC Q9QUL6; P19491: Gria2; NbExp=5; IntAct=EBI-925794, EBI-77718;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in brain (at protein level).
CC {ECO:0000269|PubMed:16461345}.
CC -!- PTM: Phosphorylation at Ser-569 interferes with homohexamerization.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; AF142097; AAD39485.1; -; mRNA.
DR EMBL; AF189019; AAF01051.1; -; mRNA.
DR RefSeq; NP_068516.1; NM_021748.1.
DR AlphaFoldDB; Q9QUL6; -.
DR SMR; Q9QUL6; -.
DR BioGRID; 248797; 5.
DR CORUM; Q9QUL6; -.
DR IntAct; Q9QUL6; 6.
DR MINT; Q9QUL6; -.
DR STRING; 10116.ENSRNOP00000006361; -.
DR iPTMnet; Q9QUL6; -.
DR PhosphoSitePlus; Q9QUL6; -.
DR World-2DPAGE; 0004:Q9QUL6; -.
DR jPOST; Q9QUL6; -.
DR PaxDb; Q9QUL6; -.
DR PRIDE; Q9QUL6; -.
DR GeneID; 60355; -.
DR KEGG; rno:60355; -.
DR UCSC; RGD:621594; rat.
DR CTD; 4905; -.
DR RGD; 621594; Nsf.
DR eggNOG; KOG0741; Eukaryota.
DR InParanoid; Q9QUL6; -.
DR OrthoDB; 197562at2759; -.
DR PhylomeDB; Q9QUL6; -.
DR Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR Reactome; R-RNO-416993; Trafficking of GluR2-containing AMPA receptors.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-6811438; Intra-Golgi traffic.
DR Reactome; R-RNO-6811440; Retrograde transport at the Trans-Golgi-Network.
DR PRO; PR:Q9QUL6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0043198; C:dendritic shaft; IDA:UniProtKB.
DR GO; GO:0005795; C:Golgi stack; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0043008; F:ATP-dependent protein binding; IPI:RGD.
DR GO; GO:0140545; F:ATP-dependent protein disaggregase activity; ISS:ParkinsonsUK-UCL.
DR GO; GO:0031748; F:D1 dopamine receptor binding; IPI:RGD.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030165; F:PDZ domain binding; ISO:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:RGD.
DR GO; GO:0000149; F:SNARE binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0019905; F:syntaxin binding; ISO:RGD.
DR GO; GO:0017075; F:syntaxin-1 binding; ISO:RGD.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IBA:GO_Central.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; ISO:RGD.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:RGD.
DR GO; GO:0001921; P:positive regulation of receptor recycling; ISO:RGD.
DR GO; GO:0006813; P:potassium ion transport; ISO:RGD.
DR GO; GO:0015031; P:protein transport; IMP:RGD.
DR GO; GO:0032984; P:protein-containing complex disassembly; IDA:UniProtKB.
DR GO; GO:0017157; P:regulation of exocytosis; IMP:RGD.
DR GO; GO:0002090; P:regulation of receptor internalization; IDA:UniProtKB.
DR GO; GO:0035494; P:SNARE complex disassembly; ISS:ParkinsonsUK-UCL.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:RGD.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR004201; Cdc48_dom2.
DR InterPro; IPR029067; CDC48_domain_2-like_sf.
DR InterPro; IPR003338; CDC4_N-term_subdom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039812; Vesicle-fus_ATPase.
DR PANTHER; PTHR23078; PTHR23078; 1.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF02933; CDC48_2; 1.
DR Pfam; PF02359; CDC48_N; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01072; CDC48_2; 1.
DR SMART; SM01073; CDC48_N; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54585; SSF54585; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..744
FT /note="Vesicle-fusing ATPase"
FT /id="PRO_0000263087"
FT BINDING 505..510
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P18708"
FT BINDING 545..552
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P18708"
FT BINDING 550
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P18708"
FT MOD_RES 105
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P46460"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P46459"
FT MOD_RES 259
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P46460"
FT MOD_RES 569
FT /note="Phosphoserine; by CDK16"
FT /evidence="ECO:0000250|UniProtKB:P46460"
SQ 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
