TERA_RAT
ID TERA_RAT Reviewed; 806 AA.
AC P46462;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Transitional endoplasmic reticulum ATPase;
DE Short=TER ATPase;
DE EC=3.6.4.6 {ECO:0000250|UniProtKB:P55072};
DE AltName: Full=15S Mg(2+)-ATPase p97 subunit;
DE AltName: Full=Valosin-containing protein;
DE Short=VCP;
GN Name=Vcp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=7806566; DOI=10.1083/jcb.127.6.1871;
RA Zhang L., Ashendel C.L., Becker G.W., Morre D.J.;
RT "Isolation and characterization of the principal ATPase associated with
RT transitional endoplasmic reticulum of rat liver.";
RL J. Cell Biol. 127:1871-1883(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 46-53; 149-155; 192-210; 218-225; 240-251; 296-312;
RP 366-386; 454-465; 616-638; 669-677 AND 701-709, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP INTERACTION WITH STX5A.
RX PubMed=9506515; DOI=10.1016/s0092-8674(00)81128-9;
RA Rabouille C., Kondo H., Newman R., Hui N., Freemont P., Warren G.;
RT "Syntaxin 5 is a common component of the NSF- and p97-mediated reassembly
RT pathways of Golgi cisternae from mitotic Golgi fragments in vitro.";
RL Cell 92:603-610(1998).
RN [5]
RP INTERACTION WITH NPLOC4; UFD1; NSFL1C AND UBE4B, AND SUBCELLULAR LOCATION.
RX PubMed=10811609; DOI=10.1093/emboj/19.10.2181;
RA Meyer H.H., Shorter J.G., Seemann J., Pappin D., Warren G.;
RT "A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to
RT ubiquitin and nuclear transport pathways.";
RL EMBO J. 19:2181-2192(2000).
RN [6]
RP FUNCTION.
RX PubMed=10930451; DOI=10.1091/mbc.11.8.2529;
RA Roy L., Bergeron J.J.M., Lavoie C., Hendriks R., Gushue J., Fazel A.,
RA Pelletier A., Morre D.J., Subramaniam V.N., Hong W., Paiement J.;
RT "Role of p97 and syntaxin 5 in the assembly of transitional endoplasmic
RT reticulum.";
RL Mol. Biol. Cell 11:2529-2542(2000).
RN [7]
RP INTERACTION WITH MEMBRANES.
RX PubMed=12146947; DOI=10.1021/bi0259195;
RA Pecheur E.-I., Martin I., Maier O., Bakowsky U., Ruysschaert J.-M.,
RA Hoekstra D.;
RT "Phospholipid species act as modulators in p97/p47-mediated fusion of Golgi
RT membranes.";
RL Biochemistry 41:9813-9823(2002).
RN [8]
RP FUNCTION, AND INTERACTION WITH NSFL1C; NAP1L4 AND UFD1.
RX PubMed=12411482; DOI=10.1093/emboj/cdf579;
RA Meyer H.H., Wang Y., Warren G.;
RT "Direct binding of ubiquitin conjugates by the mammalian p97 adaptor
RT complexes, p47 and Ufd1-Npl4.";
RL EMBO J. 21:5645-5652(2002).
RN [9]
RP INTERACTION WITH VCIP135.
RX PubMed=12473691; DOI=10.1083/jcb.200208112;
RA Uchiyama K., Jokitalo E., Kano F., Murata M., Zhang X., Canas B.,
RA Newman R., Rabouille C., Pappin D., Freemont P., Kondo H.;
RT "VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is
RT required for Golgi and ER assembly in vivo.";
RL J. Cell Biol. 159:855-866(2002).
RN [10]
RP PHOSPHORYLATION.
RX PubMed=12810701; DOI=10.1083/jcb.200303048;
RA Uchiyama K., Jokitalo E., Lindman M., Jackman M., Kano F., Murata M.,
RA Zhang X., Kondo H.;
RT "The localization and phosphorylation of p47 are important for Golgi
RT disassembly-assembly during the cell cycle.";
RL J. Cell Biol. 161:1067-1079(2003).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-7, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 transitional endoplasmic reticulum (tER). The transfer
CC of membranes from the endoplasmic reticulum to the Golgi apparatus
CC occurs via 50-70 nm transition vesicles which derive from part-rough,
CC part-smooth transitional elements of the endoplasmic reticulum (tER)
CC (PubMed:10930451, PubMed:12411482). Vesicle budding from the tER is an
CC ATP-dependent process (PubMed:10930451, PubMed:12411482). The ternary
CC complex containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins
CC and is necessary for the export of misfolded proteins from the ER to
CC the cytoplasm, where they are degraded by the proteasome
CC (PubMed:10930451, PubMed:12411482). The NPLOC4-UFD1-VCP complex
CC regulates spindle disassembly at the end of mitosis and is necessary
CC for the formation of a closed nuclear envelope. Regulates E3 ubiquitin-
CC protein ligase activity of RNF19A. Component of the VCP/p97-AMFR/gp78
CC complex that participates in the final step of the sterol-mediated
CC ubiquitination and endoplasmic reticulum-associated degradation (ERAD)
CC of HMGCR. Involved in endoplasmic reticulum stress-induced pre-emptive
CC quality control, a mechanism that selectively attenuates the
CC translocation of newly synthesized proteins into the endoplasmic
CC reticulum and reroutes them to the cytosol for proteasomal degradation.
CC Plays a role in the regulation of stress granules (SGs) clearance
CC process upon arsenite-induced response (By similarity). Also involved
CC in DNA damage response: recruited to double-strand breaks (DSBs) sites
CC in a RNF8- and RNF168-dependent manner and promotes the recruitment of
CC TP53BP1 at DNA damage sites. Recruited to stalled replication forks by
CC SPRTN: may act by mediating extraction of DNA polymerase eta (POLH) to
CC prevent excessive translesion DNA synthesis and limit the incidence of
CC mutations induced by DNA damage. Together with SPRTN metalloprotease,
CC involved in the repair of covalent DNA-protein cross-links (DPCs)
CC during DNA synthesis. Involved in interstrand cross-link repair in
CC response to replication stress by mediating unloading of the
CC ubiquitinated CMG helicase complex. Required for cytoplasmic
CC retrotranslocation of stressed/damaged mitochondrial outer-membrane
CC proteins and their subsequent proteasomal degradation. Essential for
CC the maturation of ubiquitin-containing autophagosomes and the clearance
CC of ubiquitinated protein by autophagy. Acts as a negative regulator of
CC type I interferon production by interacting with DDX58/RIG-I:
CC interaction takes place when DDX58/RIG-I is ubiquitinated via 'Lys-63'-
CC linked ubiquitin on its CARD domains, leading to recruit RNF125 and
CC promote ubiquitination and degradation 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:P55072, ECO:0000269|PubMed:10930451,
CC ECO:0000269|PubMed:12411482}.
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:P55072};
CC -!- SUBUNIT: Homohexamer. Forms a ring-shaped particle of 12.5 nm diameter,
CC that displays 6-fold radial symmetry. Interacts with NSFL1C-like
CC protein p37; the complex has membrane fusion activity and is required
CC for Golgi and endoplasmic reticulum biogenesis. Interacts with RHBDD1
CC (via C-terminal domain). Interacts with SELENOS and SYVN1, as well as
CC with DERL1 (via SHP-box motif), DERL2 and DERL3; which probably
CC transfer misfolded proteins from the ER to VCP. Interacts with SVIP.
CC Component of a complex required to couple retrotranslocation,
CC ubiquitination and deglycosylation composed of NGLY1, SAKS1, AMFR, VCP
CC and RAD23B. Directly interacts with UBXN4 and RNF19A. Interacts with
CC CASR. Interacts with UBE4B and YOD1. Interacts with clathrin. Interacts
CC with RNF103. Interacts with TRIM13 and TRIM21. Component of a VCP/p97-
CC AMFR/gp78 complex that participates in the final step of the
CC endoplasmic reticulum-associated degradation (ERAD) of HMGCR. Interacts
CC directly with AMFR/gp78 (via its VIM). Interacts with SPRTN; leading to
CC recruitment to stalled replication forks. Part of a ternary complex
CC containing STX5A, NSFL1C and VCP. NSFL1C forms a homotrimer that binds
CC to one end of a VCP homohexamer. The complex binds to membranes
CC enriched in phosphatidylethanolamine-containing lipids and promotes
CC Golgi membrane fusion. Binds to a heterodimer of NPLOC4 and UFD1,
CC binding to this heterodimer inhibits Golgi-membrane fusion. Interaction
CC with VCIP135 leads to dissociation of the complex via ATP hydrolysis by
CC VCP. Part of a ternary complex containing NPLOC4, UFD1 and VCP.
CC Interacts with WASHC5. Interacts with UBOX5. Interacts (via N-terminus)
CC with UBXN7, UBXN8, and probably several other UBX domain-containing
CC proteins (via UBX domains); the interactions are mutually exclusive
CC with VIM-dependent interactions such as those with AMFR and SELENOS.
CC Forms a complex with UBQLN1 and UBXN4 (By similarity). Interacts (via
CC the PIM motif) with RNF31 (via the PUB domain) (By similarity).
CC Interacts with DDX58/RIG-I and RNF125; interaction takes place when
CC DDX58/RIG-I is ubiquitinated via 'Lys-63'-linked ubiquitin on its CARD
CC domains, leading to recruit RNF125 and promote ubiquitination and
CC degradation of DDX58/RIG-I (By similarity). Interacts with BAG6 (By
CC similarity). Interacts with UBXN10 (By similarity). Interacts with
CC UBXN6; the interaction with UBXN6 is direct and competitive with UFD1
CC (By similarity). Forms a ternary complex with CAV1 and UBXN6. Interacts
CC with PLAA, UBXN6 and YOD1; may form a complex involved in
CC macroautophagy (By similarity). Interacts with ANKZF1 (By similarity).
CC Interacts with ubiquitin-binding protein FAF1 (By similarity).
CC Interacts with ZFAND2B (via VIM motif); the interaction is direct (By
CC similarity). Interacts with ZFAND1 (via its ubiquitin-like region);
CC this interaction occurs in an arsenite-dependent manner (By
CC similarity). Interacts with CCDC47 (By similarity). Interacts with
CC LMBR1L and UBAC2 (By similarity). Interacts with ATXN3 (By similarity).
CC Interacts with TEX264; bridging VCP to covalent DNA-protein cross-links
CC (DPCs) (By similarity). {ECO:0000250|UniProtKB:P55072,
CC ECO:0000250|UniProtKB:Q01853, ECO:0000269|PubMed:10811609,
CC ECO:0000269|PubMed:12411482, ECO:0000269|PubMed:12473691,
CC ECO:0000269|PubMed:9506515}.
CC -!- INTERACTION:
CC P46462; O35987: Nsfl1c; NbExp=12; IntAct=EBI-399011, EBI-1993760;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10811609}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:P55072}. Nucleus
CC {ECO:0000269|PubMed:10811609}. Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:P55072}. Note=Recruited to the cytoplasmic
CC surface of the endoplasmic reticulum via interaction with AMFR/gp78.
CC Following DNA double-strand breaks, recruited to the sites of damage.
CC Recruited to stalled replication forks via interaction with SPRTN.
CC Recruited to damaged lysosomes decorated with K48-linked ubiquitin
CC chains. Colocalizes with TIA1, ZFAND1 and G3BP1 in cytoplasmic stress
CC granules (SGs) in response to arsenite-induced stress treatment (By
CC similarity). {ECO:0000250|UniProtKB:P55072}.
CC -!- DOMAIN: The PIM (PUB-interaction motif) motif mediates interaction with
CC the PUB domain of RNF31. {ECO:0000250|UniProtKB:P55072}.
CC -!- PTM: Phosphorylated by tyrosine kinases in response to T-cell antigen
CC receptor activation. Phosphorylated in mitotic cells.
CC {ECO:0000269|PubMed:12810701}.
CC -!- PTM: ISGylated. {ECO:0000250|UniProtKB:P55072}.
CC -!- PTM: Methylation at Lys-315 catalyzed by VCPKMT is increased in the
CC presence of ASPSCR1. Lys-315 methylation may decrease ATPase activity.
CC {ECO:0000250|UniProtKB:P55072}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; U11760; AAC52154.1; -; mRNA.
DR EMBL; BC060518; AAH60518.1; -; mRNA.
DR PIR; A55190; A55190.
DR RefSeq; NP_446316.1; NM_053864.2.
DR AlphaFoldDB; P46462; -.
DR SMR; P46462; -.
DR BioGRID; 250528; 28.
DR ComplexPortal; CPX-138; Vcp-Npl4-Ufd1 AAA ATPase complex.
DR ComplexPortal; CPX-263; Nsfl1c-Vcp complex.
DR CORUM; P46462; -.
DR IntAct; P46462; 11.
DR MINT; P46462; -.
DR STRING; 10116.ENSRNOP00000040121; -.
DR iPTMnet; P46462; -.
DR PhosphoSitePlus; P46462; -.
DR SwissPalm; P46462; -.
DR World-2DPAGE; 0004:P46462; -.
DR jPOST; P46462; -.
DR PaxDb; P46462; -.
DR PRIDE; P46462; -.
DR Ensembl; ENSRNOT00000046102; ENSRNOP00000040121; ENSRNOG00000034242.
DR GeneID; 116643; -.
DR KEGG; rno:116643; -.
DR UCSC; RGD:621595; rat.
DR CTD; 7415; -.
DR RGD; 621595; Vcp.
DR eggNOG; KOG0730; Eukaryota.
DR GeneTree; ENSGT00900000141071; -.
DR HOGENOM; CLU_000688_12_3_1; -.
DR InParanoid; P46462; -.
DR OMA; HACHDIK; -.
DR OrthoDB; 194195at2759; -.
DR PhylomeDB; P46462; -.
DR TreeFam; TF300542; -.
DR BRENDA; 3.6.4.6; 5301.
DR Reactome; R-RNO-110320; Translesion Synthesis by POLH.
DR Reactome; R-RNO-3371511; HSF1 activation.
DR Reactome; R-RNO-382556; ABC-family proteins mediated transport.
DR Reactome; R-RNO-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR Reactome; R-RNO-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-RNO-5689877; Josephin domain DUBs.
DR Reactome; R-RNO-5689896; Ovarian tumor domain proteases.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-8951664; Neddylation.
DR Reactome; R-RNO-9013407; RHOH GTPase cycle.
DR Reactome; R-RNO-9755511; KEAP1-NFE2L2 pathway.
DR PRO; PR:P46462; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000034242; Expressed in skeletal muscle tissue and 19 other tissues.
DR Genevisible; P46462; RN.
DR GO; GO:1904949; C:ATPase complex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL.
DR GO; GO:0036513; C:Derlin-1 retrotranslocation complex; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0005811; C:lipid droplet; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0000502; C:proteasome complex; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IDA:ParkinsonsUK-UCL.
DR GO; GO:1990730; C:VCP-NSFL1C complex; IPI:ParkinsonsUK-UCL.
DR GO; GO:0043531; F:ADP binding; IMP:RGD.
DR GO; GO:0005524; F:ATP binding; IDA:BHF-UCL.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:RGD.
DR GO; GO:1904288; F:BAT3 complex binding; ISO:RGD.
DR GO; GO:0035800; F:deubiquitinase activator activity; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; IDA:BHF-UCL.
DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; ISO:RGD.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0042288; F:MHC class I protein binding; ISO:RGD.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; ISO:RGD.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; ISO:RGD.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0070842; P:aggresome assembly; ISO:RGD.
DR GO; GO:0046034; P:ATP metabolic process; ISO:RGD.
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: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:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:RGD.
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; ISO:RGD.
DR GO; GO:0036503; P:ERAD pathway; ISS:UniProtKB.
DR GO; GO:0072389; P:flavin adenine dinucleotide catabolic process; ISO:RGD.
DR GO; GO:0036297; P:interstrand cross-link repair; ISS:UniProtKB.
DR GO; GO:0016236; P:macroautophagy; ISS:UniProtKB.
DR GO; GO:0051228; P:mitotic spindle disassembly; IBA:GO_Central.
DR GO; GO:0006734; P:NADH metabolic process; ISO:RGD.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; ISO:RGD.
DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; ISO:RGD.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:1903007; P:positive regulation of Lys63-specific deubiquitinase activity; ISO:RGD.
DR GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; ISO:RGD.
DR GO; GO:1903862; P:positive regulation of oxidative phosphorylation; ISO:RGD.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:RGD.
DR GO; GO:1903006; P:positive regulation of protein K63-linked deubiquitination; ISO:RGD.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:RGD.
DR GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; IMP:RGD.
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:0106300; P:protein-DNA covalent cross-linking repair; ISS:UniProtKB.
DR GO; GO:1903715; P:regulation of aerobic respiration; ISO:RGD.
DR GO; GO:1905634; P:regulation of protein localization to chromatin; ISS:UniProtKB.
DR GO; GO:0050807; P:regulation of synapse organization; IDA:SynGO.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; ISO:RGD.
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 GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:0019079; P:viral genome replication; ISO:RGD.
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 1: Evidence at protein level;
KW Acetylation; ATP-binding; Autophagy; Cytoplasm; Direct protein sequencing;
KW DNA damage; DNA repair; Endoplasmic reticulum; Hydrolase; Isopeptide bond;
KW Lipid-binding; Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT CHAIN 2..806
FT /note="Transitional endoplasmic reticulum ATPase"
FT /id="PRO_0000084575"
FT REGION 708..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 797..806
FT /note="Interaction with UBXN6"
FT /evidence="ECO:0000250"
FT MOTIF 802..806
FT /note="PIM motif"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT COMPBIAS 768..794
FT /note="Polar residues"
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 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT MOD_RES 315
FT /note="N6,N6,N6-trimethyllysine; by VCPKMT"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT MOD_RES 436
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT MOD_RES 502
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q01853"
FT MOD_RES 505
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q01853"
FT MOD_RES 668
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q01853"
FT MOD_RES 668
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q01853"
FT MOD_RES 702
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT MOD_RES 754
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q01853"
FT MOD_RES 770
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT MOD_RES 775
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT MOD_RES 805
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q01853"
FT CROSSLNK 8
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT CROSSLNK 18
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P55072"
SQ SEQUENCE 806 AA; 89349 MW; 501B721D205EBA8A CRC64;
MASGADSKGD DLSTAILKQK NRPNRLIVDE AINEDNSVVS LSQPKMDELQ 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 IPDATGRLEI LQIHTKNMKL ADDVDLEQVA 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 KSRVAILKAN
LRKSPVAKDV DLEFLAKMTN GFSGADLTEI CQRACKLAIR ESIESEIRRE RERQTNPSAM
EVEEDDPVPE IRRDHFEEAM RFARRSVSDN DIRKYEMFAQ TLQQSRGFGS FRFPSGNQGG
AGPSQGSGGG TGGNVYTEDN DDDLYG
