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   27-MAR-2024, entry version 132.
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. Involved in clearance process by mediating
CC       G3BP1 extraction from stress granules (By similarity). Also involved in
CC       DNA damage response: recruited to double-strand breaks (DSBs) sites and
CC       promotes the recruitment of tp53bp1 at DNA damage sites (By
CC       similarity). Together with sprtn metalloprotease, involved in the
CC       repair of covalent DNA-protein cross-links (DPCs) during DNA synthesis
CC       (By similarity). Involved in interstrand cross-link repair in response
CC       to replication stress by mediating unloading of the ubiquitinated CMG
CC       helicase complex (By similarity). Enhances cell cycle progression and
CC       inhibits apoptosis at low temperatures (By similarity). Essential for
CC       the maturation of ubiquitin-containing autophagosomes and the clearance
CC       of ubiquitinated protein by autophagy (By similarity). Acts as a
CC       negative regulator of type I interferon production by promoting
CC       ubiquitination of rigi (By similarity). May play a role in the
CC       ubiquitin-dependent sorting of membrane proteins to lysosomes where
CC       they undergo degradation (By similarity). May more particularly play a
CC       role in caveolins sorting in cells (By similarity). By controlling the
CC       steady-state expression of the IGF1R receptor, indirectly regulates the
CC       insulin-like growth factor receptor signaling pathway (By similarity).
CC       {ECO:0000250|UniProtKB:P23787, ECO:0000250|UniProtKB:P46462,
CC       ECO:0000250|UniProtKB:P55072, 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.ENSXETP00000015296; -.
DR   PaxDb; 8364-ENSXETP00000054726; -.
DR   Ensembl; ENSXETT00000067185; ENSXETP00000096329; ENSXETG00000025788.
DR   GeneID; 448177; -.
DR   KEGG; xtr:448177; -.
DR   AGR; Xenbase:XB-GENE-969573; -.
DR   CTD; 7415; -.
DR   Xenbase; XB-GENE-969573; vcp.
DR   eggNOG; KOG0730; Eukaryota.
DR   InParanoid; Q6GL04; -.
DR   OMA; HACHDIK; -.
DR   OrthoDB; 168438at2759; -.
DR   Reactome; R-XTR-110320; Translesion Synthesis by POLH.
DR   Reactome; R-XTR-382556; ABC-family proteins mediated transport.
DR   Reactome; R-XTR-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR   Reactome; R-XTR-5358346; Hedgehog ligand biogenesis.
DR   Reactome; R-XTR-5689877; Josephin domain DUBs.
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   Bgee; ENSXETG00000025788; Expressed in neurula embryo and 21 other cell types or 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; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
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: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:0055013; P:cardiac muscle cell development; IEA:Ensembl.
DR   GO; GO:1903843; P:cellular response to arsenite ion; 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:0006974; P:DNA damage response; ISS:UniProtKB.
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:0036503; P:ERAD pathway; ISS:UniProtKB.
DR   GO; GO:0060047; P:heart contraction; IEA:Ensembl.
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:0030239; P:myofibril assembly; IEA:Ensembl.
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: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   CDD; cd19519; RecA-like_CDC48_r1-like; 1.
DR   CDD; cd19528; RecA-like_CDC48_r2-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.10.330.10; -; 1.
DR   Gene3D; 6.10.20.150; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR01243; CDC48; 1.
DR   PANTHER; PTHR23077; AAA-FAMILY ATPASE; 1.
DR   PANTHER; PTHR23077:SF69; TRANSITIONAL ENDOPLASMIC RETICULUM ATPASE; 1.
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   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; 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
//