ID NSF_PONAB Reviewed; 744 AA. AC Q5R410; DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot. DT 21-DEC-2004, sequence version 1. DT 24-JAN-2024, entry version 99. 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; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pongo. OX NCBI_TaxID=9601; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain cortex; RG The German cDNA consortium; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. 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 (By similarity). {ECO:0000250}. 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. Interacts CC with GRIA2. Interacts with PLK2, leading to disrupt the interaction CC with GRIA2. Interacts with MUSK; may regulate MUSK endocytosis and CC activity (By similarity). Interacts with CDK16 (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- PTM: Phosphorylation at Ser-569 interferes with homohexamerization. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CR861450; CAH93506.1; -; mRNA. DR RefSeq; NP_001127050.1; NM_001133578.1. DR AlphaFoldDB; Q5R410; -. DR SMR; Q5R410; -. DR STRING; 9601.ENSPPYP00000009318; -. DR Ensembl; ENSPPYT00000009694.3; ENSPPYP00000009318.3; ENSPPYG00000008293.3. DR GeneID; 100174078; -. DR KEGG; pon:100174078; -. DR CTD; 4905; -. DR eggNOG; KOG0741; Eukaryota. DR GeneTree; ENSGT00530000064085; -. DR InParanoid; Q5R410; -. DR OrthoDB; 553800at2759; -. DR Proteomes; UP000001595; Chromosome 17. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0035494; P:SNARE complex disassembly; IEA:InterPro. DR CDD; cd19504; RecA-like_NSF-SEC18_r1-like; 1. DR Gene3D; 1.10.8.60; -; 2. DR Gene3D; 2.40.40.20; -; 1. DR Gene3D; 3.10.330.10; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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:SF3; VESICLE-FUSING ATPASE; 1. DR PANTHER; PTHR23078; VESICULAR-FUSION PROTEIN NSF; 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 PRINTS; PR00830; ENDOLAPTASE. DR SMART; SM00382; AAA; 2. DR SMART; SM01072; CDC48_2; 1. DR SMART; SM01073; CDC48_N; 1. DR SUPFAM; SSF50692; ADC-like; 1. DR SUPFAM; SSF54585; Cdc48 domain 2-like; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS00674; AAA; 1. PE 2: Evidence at transcript level; KW Acetylation; ATP-binding; Cytoplasm; Hydrolase; Magnesium; Metal-binding; KW Nucleotide-binding; Phosphoprotein; Protein transport; Reference proteome; KW Repeat; Transport. FT CHAIN 1..744 FT /note="Vesicle-fusing ATPase" FT /id="PRO_0000263086" 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; 82626 MW; B6BC0C9D0AC02AA7 CRC64; MAGRSMQAAR CPTDELSLTN CAVVNEKDFQ SGQHVIVRTS PNHRYTFTLK THPSVVPGSI AFSLPQRKWA GLSIGQEIEV SLYTFDKAKQ CIGTMTIEID FLQKKSIDSN PYDTDKMAAE FIQQFNNQAF SVGQQLVFSF NEKLFGLLVK DIEAMDPSIL KGEPATGKRQ 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 METKNFSGAE 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 //