ID A0A670IZM9_PODMU Unreviewed; 733 AA.
AC A0A670IZM9;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 28-JAN-2026, entry version 26.
DE RecName: Full=Vesicle-fusing ATPase {ECO:0000256|ARBA:ARBA00019912, ECO:0000256|RuleBase:RU367045};
DE EC=3.6.4.6 {ECO:0000256|ARBA:ARBA00012674, ECO:0000256|RuleBase:RU367045};
GN Name=NSF {ECO:0000313|Ensembl:ENSPMRP00000017276.1};
OS Podarcis muralis (Wall lizard) (Lacerta muralis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Laterata;
OC Lacertibaenia; Lacertidae; Podarcis.
OX NCBI_TaxID=64176 {ECO:0000313|Ensembl:ENSPMRP00000017276.1, ECO:0000313|Proteomes:UP000472272};
RN [1] {ECO:0000313|Ensembl:ENSPMRP00000017276.1, ECO:0000313|Proteomes:UP000472272}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30819892; DOI=10.1073/pnas.1820320116;
RA Andrade P., Pinho C., Perez I de Lanuza G., Afonso S., Brejcha J.,
RA Rubin C.J., Wallerman O., Pereira P., Sabatino S.J., Bellati A.,
RA Pellitteri-Rosa D., Bosakova Z., Bunikis I., Carretero M.A., Feiner N.,
RA Marsik P., Pauperio F., Salvi D., Soler L., While G.M., Uller T., Font E.,
RA Andersson L., Carneiro M.;
RT "Regulatory changes in pterin and carotenoid genes underlie balanced color
RT polymorphisms in the wall lizard.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:5633-5642(2019).
RN [2] {ECO:0000313|Ensembl:ENSPMRP00000017276.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSPMRP00000017276.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
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. {ECO:0000256|RuleBase:RU367045}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + phosphate + H(+); 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 Evidence={ECO:0000256|ARBA:ARBA00048883,
CC ECO:0000256|RuleBase:RU367045};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU367045};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|RuleBase:RU367045};
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. Interacts with CDK16. {ECO:0000256|ARBA:ARBA00046527}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU367045}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU367045}.
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DR AlphaFoldDB; A0A670IZM9; -.
DR Ensembl; ENSPMRT00000018393.1; ENSPMRP00000017276.1; ENSPMRG00000011432.1.
DR GeneTree; ENSGT00530000064085; -.
DR OMA; CFDNEIA; -.
DR Proteomes; UP000472272; Chromosome 13.
DR GO; GO:0005795; C:Golgi stack; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IEA:TreeGrafter.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IEA:TreeGrafter.
DR GO; GO:0035494; P:SNARE complex disassembly; IEA:InterPro.
DR CDD; cd19504; RecA-like_NSF-SEC18_r1-like; 1.
DR FunFam; 1.10.8.60:FF:000026; vesicle-fusing ATPase isoform X1; 1.
DR FunFam; 1.10.8.60:FF:000031; vesicle-fusing ATPase isoform X1; 1.
DR FunFam; 2.40.40.20:FF:000006; vesicle-fusing ATPase isoform X1; 1.
DR FunFam; 3.10.330.10:FF:000003; vesicle-fusing ATPase isoform X1; 1.
DR FunFam; 3.40.50.300:FF:000166; vesicle-fusing ATPase isoform X1; 1.
DR FunFam; 3.40.50.300:FF:000187; Vesicular-fusion ATPase SEC18; 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; IPR054419; NSF_ATPase_lid.
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 Pfam; PF21964; NSF_ATPase_lid; 1.
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 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU367045};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU367045};
KW ER-Golgi transport {ECO:0000256|RuleBase:RU367045};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU367045};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU367045};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367045};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU367045};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU367045};
KW Reference proteome {ECO:0000313|Proteomes:UP000472272};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367045}.
FT DOMAIN 1..80
FT /note="CDC48 N-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01073"
FT DOMAIN 106..178
FT /note="CDC48"
FT /evidence="ECO:0000259|SMART:SM01072"
FT DOMAIN 247..394
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 530..666
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 733 AA; 81443 MW; 2DDDCAD840744FD1 CRC64;
MQAARCPTDE LSLSNCAVVN EKDFQSGLHV VVKTSPNHKY IFTLRTYSSV VPGTIAFSLP
QRKWAGLSIG QDIDVSVYNF DKTKQCVGTM TIEIDFLQKK SVDSNPYDSD KMAAEFIQQF
NNQAFTVGQQ LVFSFNDKLF GLLVKDIEAM DPSILKGEPA TGKKQKIEVG LVVGNSQVAF
EKAESSSLTL IGKSKTRENR QSIINPDWNF EKMGIGGLDK EFSDIFRRAF ASRVFPPEIV
EQMGCKHVKG ILLFGPPGCG KTLMARQIGK MLNAREPKIV NGPEILNKYV GESEANIRKL
FADAEEEQRR LGANSGVHII IFDEIDAICK QRGSMAGSTG VHDTVVNQLL SKIDGVEQLN
NILVIGMTNR PDLIDEALLR PGRLEVKMEI GLPDEKGRMQ ILNIHTSRMR THQLLASDVD
ISELAVETKN FSGAELEGLV RAAQSTAMNR HIKATTKVEV DMEKAECLQV TRVDFLTSLE
NDIKPAFGTN QEDYASYIMN GIMKWGDPVT RVLDDGELLV QQAKNSDRTP LVSVLLEGPP
HSGKTALAAK IAEESNFPFI KICSPDKMIG FSETAKCQAM KKIFDDAYKS QLSCVVVDDI
ERLLDYVPIG PRFSNLVLQA LLVLLKKAPP HGRKLLIIGT TSRKDVLQEM EMLDAFSTTI
HVPNIATGDH LMEALELLGS FKDKERSTIA QNVKGRKVWI GIKKLLMLIE MSMQMDPEYR
VRKFLALLRE EGA
//
