TERA_XENTR
ID TERA_XENTR Reviewed; 805 AA.
AC Q6GL04;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Transitional endoplasmic reticulum ATPase {ECO:0000250|UniProtKB:P23787};
DE Short=TER ATPase {ECO:0000250|UniProtKB:P23787};
DE EC=3.6.4.6 {ECO:0000250|UniProtKB:P23787};
DE AltName: Full=15S Mg(2+)-ATPase p97 subunit {ECO:0000250|UniProtKB:P23787};
DE Short=p97 {ECO:0000250|UniProtKB:P23787};
DE AltName: Full=Valosin-containing protein {ECO:0000312|EMBL:AAH74716.1};
DE Short=VCP {ECO:0000250|UniProtKB:P23787};
GN Name=vcp {ECO:0000312|EMBL:AAH74716.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:AAH74716.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tail bud {ECO:0000312|EMBL:AAH74716.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Necessary for the fragmentation of Golgi stacks during
CC mitosis and for their reassembly after mitosis. Involved in the
CC formation of the nuclear envelope, and of the transitional endoplasmic
CC reticulum (tER). The transfer of membranes from the endoplasmic
CC reticulum to the Golgi apparatus occurs via 50-70 nm transition
CC vesicles which derive from part-rough, part-smooth transitional
CC elements of the endoplasmic reticulum (tER). Vesicle budding from the
CC tER is an ATP-dependent process. Involved in endoplasmic reticulum
CC stress-induced pre-emptive quality control, a mechanism that
CC selectively attenuates the translocation of newly synthesized proteins
CC into the endoplasmic reticulum and reroutes them to the cytosol for
CC proteasomal degradation. Plays a role in the regulation of stress
CC granules (SGs) clearance process upon arsenite-induced response (By
CC similarity). Also involved in DNA damage response: recruited to double-
CC strand breaks (DSBs) sites and promotes the recruitment of tp53bp1 at
CC DNA damage sites (By similarity). Together with sprtn metalloprotease,
CC involved in the repair of covalent DNA-protein cross-links (DPCs)
CC during DNA synthesis (By similarity). Involved in interstrand cross-
CC link repair in response to replication stress by mediating unloading of
CC the ubiquitinated CMG helicase complex (By similarity). Enhances cell
CC cycle progression and inhibits apoptosis at low temperatures (By
CC similarity). Essential for the maturation of ubiquitin-containing
CC autophagosomes and the clearance of ubiquitinated protein by autophagy
CC (By similarity). Acts as a negative regulator of type I interferon
CC production by promoting ubiquitination of ddx58/rig-i (By similarity).
CC May play a role in the ubiquitin-dependent sorting of membrane proteins
CC to lysosomes where they undergo degradation (By similarity). May more
CC particularly play a role in caveolins sorting in cells (By similarity).
CC By controlling the steady-state expression of the IGF1R receptor,
CC indirectly regulates the insulin-like growth factor receptor signaling
CC pathway (By similarity). {ECO:0000250|UniProtKB:P23787,
CC ECO:0000250|UniProtKB:P46462, ECO:0000250|UniProtKB:P55072,
CC ECO:0000250|UniProtKB:Q7ZU99}.
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:0000250|UniProtKB:P23787};
CC -!- ACTIVITY REGULATION: ATPase activity is inhibited or reduced by
CC lowering pH from 9.0 to 7.0, and by addition of Ca(2+), EDTA, KNO(3) or
CC by treatment with N-ethylmaleimide (NEM).
CC {ECO:0000250|UniProtKB:P23787}.
CC -!- SUBUNIT: Homohexamer. Forms a ring-shaped particle of 12.5 nm diameter,
CC that displays 6-fold radial symmetry. Interacts with the FACT/DUF
CC complex, which includes subunits ssrp1/duf87 and supt16h/duf140 (By
CC similarity). {ECO:0000250|UniProtKB:P23787}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P23787}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P55072}. Nucleus {ECO:0000250|UniProtKB:P23787}.
CC Cytoplasm, Stress granule {ECO:0000250|UniProtKB:P55072}.
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:P23787,
CC ECO:0000250|UniProtKB:Q7ZU99}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000255}.
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DR EMBL; BC074716; AAH74716.1; -; mRNA.
DR RefSeq; NP_001005677.1; NM_001005677.1.
DR AlphaFoldDB; Q6GL04; -.
DR SMR; Q6GL04; -.
DR STRING; 8364.ENSXETP00000054726; -.
DR PaxDb; Q6GL04; -.
DR Ensembl; ENSXETT00000067185; ENSXETP00000096329; ENSXETG00000025788.
DR GeneID; 448177; -.
DR KEGG; xtr:448177; -.
DR CTD; 7415; -.
DR Xenbase; XB-GENE-969573; vcp.
DR eggNOG; KOG0730; Eukaryota.
DR InParanoid; Q6GL04; -.
DR OrthoDB; 194195at2759; -.
DR Reactome; R-XTR-3371511; HSF1 activation.
DR Reactome; R-XTR-382556; ABC-family proteins mediated transport.
DR Reactome; R-XTR-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-XTR-5689896; Ovarian tumor domain proteases.
DR Reactome; R-XTR-6798695; Neutrophil degranulation.
DR Reactome; R-XTR-8876725; Protein methylation.
DR Reactome; R-XTR-8951664; Neddylation.
DR Reactome; R-XTR-9013407; RHOH GTPase cycle.
DR Reactome; R-XTR-9755511; KEAP1-NFE2L2 pathway.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000025788; Expressed in neurula embryo and 21 other tissues.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; ISS:UniProtKB.
DR GO; GO:0097352; P:autophagosome maturation; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; ISS:UniProtKB.
DR GO; GO:1903843; P:cellular response to arsenite ion; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR GO; GO:0043009; P:chordate embryonic development; IEA:Ensembl.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR GO; GO:0061857; P:endoplasmic reticulum stress-induced pre-emptive quality control; ISS:UniProtKB.
DR GO; GO:0032510; P:endosome to lysosome transport via multivesicular body sorting pathway; ISS:UniProtKB.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IBA:GO_Central.
DR GO; GO:0036503; P:ERAD pathway; ISS:UniProtKB.
DR GO; GO:0036297; P:interstrand cross-link repair; ISS:UniProtKB.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0016236; P:macroautophagy; ISS:UniProtKB.
DR GO; GO:0051228; P:mitotic spindle disassembly; IBA:GO_Central.
DR GO; GO:0010498; P:proteasomal protein catabolic process; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; IEA:Ensembl.
DR GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:1905634; P:regulation of protein localization to chromatin; ISS:UniProtKB.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IBA:GO_Central.
DR GO; GO:0035617; P:stress granule disassembly; ISS:UniProtKB.
DR GO; GO:0019985; P:translesion synthesis; ISS:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005938; AAA_ATPase_CDC48.
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; IPR015415; Vps4_C.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 2.
DR Pfam; PF02933; CDC48_2; 1.
DR Pfam; PF02359; CDC48_N; 1.
DR Pfam; PF09336; Vps4_C; 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 TIGRFAMs; TIGR01243; CDC48; 1.
DR PROSITE; PS00674; AAA; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Autophagy; Cytoplasm; DNA damage; DNA repair;
KW Endoplasmic reticulum; Hydrolase; Lipid-binding; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..805
FT /note="Transitional endoplasmic reticulum ATPase"
FT /id="PRO_0000382234"
FT REGION 768..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 247..253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT BINDING 348
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT BINDING 384
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT BINDING 521..526
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q01853"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7ZU99"
SQ SEQUENCE 805 AA; 89236 MW; 52DF6D8968F977EE CRC64;
MASGSDSKSD DLSTAILKQK SRPNRLIVDE SINEDNSVVS LSQAKMDELQ LFRGDTVLLK
GKKRREAVCI VLSDDTCSDE KIRMNRVVRN NLRVRLGDVI SIQPCPDVKY GKRIHVLPID
DTVEGITGNL FEVYLKPYFL EAYRPIRKGD IFLVRGGMRA VEFKVVETDP SPYCIVAPDT
VIHCEGEPIK REDEEESLNE VGYDDIGGCR KQLAQIKEMV ELPLRHPALF KAIGVKPPRG
ILLYGPPGTG KTLIARAVAN ETGAFFFLIN GPEIMSKLAG ESESNLRKAF EEAEKNAPAI
IFIDELDAIA PKREKTHGEV ERRIVSQLLT LMDGLKQRAH VIVMAATNRP NSIDPALRRF
GRFDREVDIG IPDSTGRLEI LQIHTKNMKL SDDVDLEQVA NETHGHVGAD LAALCSEAAL
QAIRKKMDLI DLEDETIDAE VMNSLAVTMD DFRWALSQSN PSALRETVVE VPQVTWEDIG
GLEDVKRELQ ELVQYPVEHP DKFLKFGMTP SKGVLFYGPP GCGKTLLAKA IANECQANFI
SIKGPELLTM WFGESEANVR EIFDKARQAA PCVLFFDELD SIAKARGGNI GDGGGAADRV
INQILTEMDG MSTKKNVFII GATNRPDIID PAILRPGRLD QLIYIPLPDE KSRIAILKAN
LRKSPVAKDV DLDFLAKMTN GFSGADLTEI CQRACKLAIR ESIENEIRRE RERQTNPSAM
EVEEDDPVPE IRRDHFEEAM RFARRSVSDN DIRKYEMFAQ TLQQSRGFGS FRFPAGGQGG
AGPSQGAGGG SGGSHFNEEE DDLYG
