ID A0A3Q1BEF7_AMPOC Unreviewed; 750 AA.
AC A0A3Q1BEF7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, 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};
OS Amphiprion ocellaris (Clown anemonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000012697.1, ECO:0000313|Proteomes:UP000257160};
RN [1] {ECO:0000313|Ensembl:ENSAOCP00000012697.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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 + 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 Evidence={ECO:0000256|ARBA:ARBA00000161,
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 -!- 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; A0A3Q1BEF7; -.
DR STRING; 80972.ENSAOCP00000012697; -.
DR Ensembl; ENSAOCT00000020501.1; ENSAOCP00000012697.1; ENSAOCG00000017242.1.
DR GeneTree; ENSGT00530000064085; -.
DR Proteomes; UP000257160; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0048933; P:afferent axon development in posterior lateral line nerve; IEA:Ensembl.
DR GO; GO:0045162; P:clustering of voltage-gated sodium channels; IEA:Ensembl.
DR GO; GO:0048929; P:efferent axon development in posterior lateral line nerve; IEA:Ensembl.
DR GO; GO:0048592; P:eye morphogenesis; IEA:Ensembl.
DR GO; GO:0021854; P:hypothalamus development; IEA:Ensembl.
DR GO; GO:0048914; P:myelination of anterior lateral line nerve axons; IEA:Ensembl.
DR GO; GO:0048932; P:myelination of posterior lateral line nerve axons; IEA:Ensembl.
DR GO; GO:0051875; P:pigment granule localization; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0014044; P:Schwann cell development; IEA:Ensembl.
DR GO; GO:0035494; P:SNARE complex disassembly; IEA:InterPro.
DR GO; GO:0048794; P:swim bladder development; IEA:Ensembl.
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 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 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|RuleBase:RU367045};
KW Magnesium {ECO:0000256|RuleBase:RU367045};
KW Metal-binding {ECO:0000256|RuleBase:RU367045};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU367045};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU367045};
KW Reference proteome {ECO:0000313|Proteomes:UP000257160};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367045}.
FT DOMAIN 11..91
FT /note="CDC48 N-terminal subdomain"
FT /evidence="ECO:0000259|SMART:SM01073"
FT DOMAIN 117..189
FT /note="CDC48"
FT /evidence="ECO:0000259|SMART:SM01072"
FT DOMAIN 258..405
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 541..677
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 750 AA; 83038 MW; 6396AE50308BFD9F CRC64;
MAARVVIFFK TMQAARCPTD ELSLTNCAVV SEKDLQSGQH VTVKTTPNHK FAFTVKTHHT
VAPGTIAFSL PQRKWAGLSI GQEVEVANYN FDKSKQCIGA MTIEIDFLQK KSTDSSPYDS
DKMAAEFIQQ FNNQAFSVTQ QLVFSFCDKL FGLVVKDIEA MDASILKGEP ASGKKQKIDV
GLMVGNSQVI FEKAENSSLT LVGKAKTKEA RQTIINPDWN FEKMGIGGLD KEFSDIFRRA
FASRVFPPDI VEQMGCKHVK GILLFGPPGC GKTLMARQIG KMLNAREPKI VNGPEILNKY
VGESEANIRK LFAEAEEEQK RLGANSGLHI IIFDELDAIC KQRGTGASST GVHDTVVNQL
LSKIDGVEQL NNILVIGMTN RPDLIDDALM RPGRFEVKME IGLPDEKGRV QILTIHTNKM
RGFNLLAVDV DIKELASETK NYSGAELEGL VRAAQSTAMN RHIKATSTVE VDMEKAEKLQ
VTRADFMGSL NNDIKPAFGT NQEDYSSYIM NGIIKWGDPV THVLDDGELL VQQTKNSDRT
PLVAVLLEGP PHSGKTALAA KIAEDSQFPF IKICSPDKMI GHSEISKCQA IKKVFDDAYK
SQLSCVVVDD IERLLDYVPI GPRFSNLVLQ ALLVLLKKAP PKGRKLLIIG TTSRKDVLQE
MEMLDAFSTT IHIPNISTGE QLVDALELLG SFTDKERASI AQQLKGKRVW IGIKKLLVLI
EMSLQMDQDY RVTKFLSLLR DEGADRSFYE
//
