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TERA_PIG
ID   TERA_PIG                Reviewed;         806 AA.
AC   P03974;
DT   23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 5.
DT   03-AUG-2022, entry version 179.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3468358; DOI=10.1038/325542a0;
RA   Koller K.J., Brownstein M.J.;
RT   "Use of a cDNA clone to identify a supposed precursor protein containing
RT   valosin.";
RL   Nature 325:542-545(1987).
RN   [2]
RP   PROTEIN SEQUENCE OF 493-517.
RX   PubMed=4054310; DOI=10.1016/0014-5793(85)80021-1;
RA   Schmidt W.E., Mutt V., Carlquist M., Kratzin H., Conlon J.M.,
RA   Creutzfeldt W.;
RT   "Valosin: isolation and characterization of a novel peptide from porcine
RT   intestine.";
RL   FEBS Lett. 191:264-268(1985).
RN   [3]
RP   SHOWS THAT VALOSIN IS A PURIFICATION ARTIFACT.
RX   PubMed=2927256; DOI=10.1016/0024-3205(89)90464-5;
RA   Gill J.S., Ghatei M.A., Domin J., Bloom S.R.;
RT   "The generation of valosin-like peptides from a precursor protein in vitro
RT   as an extraction artifact.";
RL   Life Sci. 44:483-491(1989).
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       Vesicle budding from the tER is an ATP-dependent process. 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. The NPLOC4-
CC       UFD1-VCP complex regulates spindle disassembly at the end of mitosis
CC       and is necessary for the formation of a closed nuclear envelope.
CC       Regulates E3 ubiquitin-protein ligase activity of RNF19A. Component of
CC       the VCP/p97-AMFR/gp78 complex that participates in the final step of
CC       the sterol-mediated ubiquitination and endoplasmic reticulum-associated
CC       degradation (ERAD) of HMGCR. Involved in endoplasmic reticulum stress-
CC       induced pre-emptive quality control, a mechanism that selectively
CC       attenuates the translocation of newly synthesized proteins into the
CC       endoplasmic reticulum and reroutes them to the cytosol for proteasomal
CC       degradation. Plays a role in the regulation of stress granules (SGs)
CC       clearance process upon arsenite-induced response (By similarity). Also
CC       involved in DNA damage response: recruited to double-strand breaks
CC       (DSBs) sites in a RNF8- and RNF168-dependent manner and promotes the
CC       recruitment of TP53BP1 at DNA damage sites. Recruited to stalled
CC       replication forks by SPRTN: may act by mediating extraction of DNA
CC       polymerase eta (POLH) to prevent excessive translesion DNA synthesis
CC       and limit the incidence of mutations induced by DNA damage. Together
CC       with SPRTN metalloprotease, involved in the repair of covalent DNA-
CC       protein cross-links (DPCs) during DNA synthesis. Involved in
CC       interstrand cross-link repair in response to replication stress by
CC       mediating unloading of the ubiquitinated CMG helicase complex. Required
CC       for cytoplasmic retrotranslocation of stressed/damaged mitochondrial
CC       outer-membrane proteins and their subsequent proteasomal degradation.
CC       Essential for the maturation of ubiquitin-containing autophagosomes and
CC       the clearance of ubiquitinated protein by autophagy. Acts as a negative
CC       regulator of type I interferon production by interacting with
CC       DDX58/RIG-I: interaction takes place when DDX58/RIG-I is ubiquitinated
CC       via 'Lys-63'-linked ubiquitin on its CARD domains, leading to recruit
CC       RNF125 and promote ubiquitination and degradation of DDX58/RIG-I. May
CC       play a role in the ubiquitin-dependent sorting of membrane proteins to
CC       lysosomes where they undergo degradation. May more particularly play a
CC       role in caveolins sorting in cells. By controlling the steady-state
CC       expression of the IGF1R receptor, indirectly regulates the insulin-like
CC       growth factor receptor signaling pathway (By similarity).
CC       {ECO:0000250|UniProtKB:P23787, ECO:0000250|UniProtKB:P46462,
CC       ECO:0000250|UniProtKB:P55072}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homohexamer. Forms a ring-shaped particle of 12.5 nm diameter,
CC       that displays 6-fold radial symmetry. 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 NSFL1C-like protein p37; the complex has membrane fusion
CC       activity and is required for Golgi and endoplasmic reticulum
CC       biogenesis. Interacts with SELENOS and SYVN1, as well as with DERL1
CC       (via SHP-box motif), DERL2 and DERL3; which probably transfer misfolded
CC       proteins from the ER to VCP. Interacts with SVIP. Component of a
CC       complex required to couple retrotranslocation, ubiquitination and
CC       deglycosylation composed of NGLY1, SAKS1, AMFR, VCP and RAD23B.
CC       Directly interacts with UBXN4 and RNF19A. Interacts with CASR.
CC       Interacts with UBE4B and YOD1. Interacts with clathrin. Interacts with
CC       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 RHBDD1 (via C-
CC       terminal domain). Interacts with SPRTN; leading to recruitment to
CC       stalled replication forks. Interacts with WASHC5. Interacts with UBOX5.
CC       Interacts (via N-terminus) with UBXN7, UBXN8, and probably several
CC       other UBX domain-containing proteins (via UBX domains); the
CC       interactions are mutually exclusive with VIM-dependent interactions
CC       such as those with AMFR and SELENOS. Forms a complex with UBQLN1 and
CC       UBXN4. Interacts (via the PIM motif) with RNF31 (via the PUB domain).
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. Interacts with BAG6. Interacts with UBXN10.
CC       Interacts with UBXN6; the interaction with UBXN6 is direct and
CC       competitive with UFD1. Forms a ternary complex with CAV1 and UBXN6.
CC       Interacts with PLAA, UBXN6 and YOD1; may form a complex involved in
CC       macroautophagy. Interacts with ANKZF1. Interacts with ubiquitin-binding
CC       protein FAF1. Interacts with ZFAND2B (via VIM motif); the interaction
CC       is direct. Interacts with ZFAND1 (via its ubiquitin-like region); this
CC       interaction occurs in an arsenite-dependent manner (By similarity).
CC       Interacts with CCDC47 (By similarity). Interacts with LMBR1L and UBAC2
CC       (By similarity). Interacts with ATXN3 (By similarity). Interacts with
CC       TEX264; bridging VCP to covalent DNA-protein cross-links (DPCs) (By
CC       similarity). {ECO:0000250|UniProtKB:P46462,
CC       ECO:0000250|UniProtKB:P55072, ECO:0000250|UniProtKB:Q01853}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P55072}. Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P55072}. Nucleus {ECO:0000250|UniProtKB:P55072}.
CC       Cytoplasm, Stress granule {ECO:0000250|UniProtKB:P55072}.
CC       Note=Recruited to the cytoplasmic surface of the endoplasmic reticulum
CC       via interaction with AMFR/gp78. Following DNA double-strand breaks,
CC       recruited to the sites of damage. Recruited to stalled replication
CC       forks via interaction with SPRTN. Recruited to damaged lysosomes
CC       decorated with K48-linked ubiquitin chains. Colocalizes with TIA1,
CC       ZFAND1 and G3BP1 in cytoplasmic stress granules (SGs) in response to
CC       arsenite-induced stress treatment (By similarity).
CC       {ECO:0000250|UniProtKB:P55072}.
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   -!- PTM: Phosphorylated by tyrosine kinases in response to T-cell antigen
CC       receptor activation. Phosphorylated in mitotic cells.
CC       {ECO:0000250|UniProtKB:P46462}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC   -!- CAUTION: Valosin is an artifact of purification procedure, generated in
CC       vitro by cleavage of the whole protein upon acid extraction of tissues.
CC       {ECO:0000305}.
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DR   EMBL; M30143; AAA31142.1; -; mRNA.
DR   PIR; A26360; VPPG.
DR   RefSeq; NP_999445.1; NM_214280.1.
DR   AlphaFoldDB; P03974; -.
DR   SMR; P03974; -.
DR   BioGRID; 1149651; 1.
DR   STRING; 9823.ENSSSCP00000005692; -.
DR   PaxDb; P03974; -.
DR   PeptideAtlas; P03974; -.
DR   PRIDE; P03974; -.
DR   GeneID; 397524; -.
DR   KEGG; ssc:397524; -.
DR   CTD; 7415; -.
DR   eggNOG; KOG0730; Eukaryota.
DR   InParanoid; P03974; -.
DR   OrthoDB; 194195at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
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; IBA:GO_Central.
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; IBA:GO_Central.
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: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: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: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:0106300; P:protein-DNA covalent cross-linking repair; ISS:UniProtKB.
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   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; Ubl conjugation pathway.
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_0000084574"
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   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:0000250|UniProtKB:P55072"
FT   MOD_RES         7
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P55072"
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;  89289 MW;  83B36B03DB7D9B35 CRC64;
     MASGADSKGD DLSTAILKQK NRPNRLIVDE AINEDNSVVS LSQPKMDELQ LFRGDTVLLK
     GKKRREAVCI VLSDDTCSDE KIRMNRVVRN NLRVHLGDVI 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 DLVQYPVEHP 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 TGGSVYTEDN DDDLYG
 
 
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