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Transitional endoplasmic reticulum ATPase (TER ATPase) (EC 3.6.4.6) (15S Mg(2 )-ATPase p97 subunit) (Valosin-containing protein) (VCP)

 TERA_PIG                Reviewed;         806 AA.
P03974;
23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 5.
10-OCT-2018, entry version 162.
RecName: Full=Transitional endoplasmic reticulum ATPase;
Short=TER ATPase;
EC=3.6.4.6 {ECO:0000250|UniProtKB:P55072};
AltName: Full=15S Mg(2+)-ATPase p97 subunit;
AltName: Full=Valosin-containing protein;
Short=VCP;
Name=VCP;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3468358; DOI=10.1038/325542a0;
Koller K.J., Brownstein M.J.;
"Use of a cDNA clone to identify a supposed precursor protein
containing valosin.";
Nature 325:542-545(1987).
[2]
PROTEIN SEQUENCE OF 493-517.
PubMed=4054310; DOI=10.1016/0014-5793(85)80021-1;
Schmidt W.E., Mutt V., Carlquist M., Kratzin H., Conlon J.M.,
Creutzfeldt W.;
"Valosin: isolation and characterization of a novel peptide from
porcine intestine.";
FEBS Lett. 191:264-268(1985).
[3]
SHOWS THAT VALOSIN IS A PURIFICATION ARTIFACT.
PubMed=2927256; DOI=10.1016/0024-3205(89)90464-5;
Gill J.S., Ghatei M.A., Domin J., Bloom S.R.;
"The generation of valosin-like peptides from a precursor protein in
vitro as an extraction artifact.";
Life Sci. 44:483-491(1989).
-!- FUNCTION: Necessary for the fragmentation of Golgi stacks during
mitosis and for their reassembly after mitosis. Involved in the
formation of the transitional endoplasmic reticulum (tER). The
transfer of membranes from the endoplasmic reticulum to the Golgi
apparatus occurs via 50-70 nm transition vesicles which derive
from part-rough, part-smooth transitional elements of the
endoplasmic reticulum (tER). Vesicle budding from the tER is an
ATP-dependent process. The ternary complex containing UFD1, VCP
and NPLOC4 binds ubiquitinated proteins and is necessary for the
export of misfolded proteins from the ER to the cytoplasm, where
they are degraded by the proteasome. The NPLOC4-UFD1-VCP complex
regulates spindle disassembly at the end of mitosis and is
necessary for the formation of a closed nuclear envelope.
Regulates E3 ubiquitin-protein ligase activity of RNF19A.
Component of the VCP/p97-AMFR/gp78 complex that participates in
the final step of the sterol-mediated ubiquitination and
endoplasmic reticulum-associated degradation (ERAD) of HMGCR.
Involved in endoplasmic reticulum stress-induced pre-emptive
quality control, a mechanism that selectively attenuates the
translocation of newly synthesized proteins into the endoplasmic
reticulum and reroutes them to the cytosol for proteasomal
degradation. Plays a role in the regulation of stress granules
(SGs) clearance process upon arsenite-induced response (By
similarity). Also involved in DNA damage response: recruited to
double-strand breaks (DSBs) sites in a RNF8- and RNF168-dependent
manner and promotes the recruitment of TP53BP1 at DNA damage
sites. Recruited to stalled replication forks by SPRTN: may act by
mediating extraction of DNA polymerase eta (POLH) to prevent
excessive translesion DNA synthesis and limit the incidence of
mutations induced by DNA damage. Required for cytoplasmic
retrotranslocation of stressed/damaged mitochondrial outer-
membrane proteins and their subsequent proteasomal degradation.
Essential for the maturation of ubiquitin-containing
autophagosomes and the clearance of ubiquitinated protein by
autophagy. Acts as a negative regulator of type I interferon
production by interacting with DDX58/RIG-I: interaction takes
place when DDX58/RIG-I is ubiquitinated via 'Lys-63'-linked
ubiquitin on its CARD domains, leading to recruit RNF125 and
promote ubiquitination and degradation of DDX58/RIG-I. May play a
role in the ubiquitin-dependent sorting of membrane proteins to
lysosomes where they undergo degradation. May more particularly
play a role in caveolins sorting in cells. By controlling the
steady-state expression of the IGF1R receptor, indirectly
regulates the insulin-like growth factor receptor signaling
pathway (By similarity). {ECO:0000250|UniProtKB:P46462,
ECO:0000250|UniProtKB:P55072}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000250|UniProtKB:P55072}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- SUBUNIT: Homohexamer. Forms a ring-shaped particle of 12.5 nm
diameter, that displays 6-fold radial symmetry. Part of a ternary
complex containing STX5A, NSFL1C and VCP. NSFL1C forms a
homotrimer that binds to one end of a VCP homohexamer. The complex
binds to membranes enriched in phosphatidylethanolamine-containing
lipids and promotes Golgi membrane fusion. Binds to a heterodimer
of NPLOC4 and UFD1, binding to this heterodimer inhibits Golgi-
membrane fusion. Interaction with VCIP135 leads to dissociation of
the complex via ATP hydrolysis by VCP. Part of a ternary complex
containing NPLOC4, UFD1 and VCP. Interacts with NSFL1C-like
protein p37; the complex has membrane fusion activity and is
required for Golgi and endoplasmic reticulum biogenesis. Interacts
with SELENOS and SYVN1, as well as with DERL1, DERL2 and DERL3;
which probably transfer misfolded proteins from the ER to VCP.
Interacts with SVIP. Component of a complex required to couple
retrotranslocation, ubiquitination and deglycosylation composed of
NGLY1, SAKS1, AMFR, VCP and RAD23B. Directly interacts with UBXN4
and RNF19A. Interacts with CASR. Interacts with UBE4B and YOD1.
Interacts with clathrin. Interacts with RNF103. Interacts with
TRIM13 and TRIM21. Component of a VCP/p97-AMFR/gp78 complex that
participates in the final step of the endoplasmic reticulum-
associated degradation (ERAD) of HMGCR. Interacts directly with
AMFR/gp78 (via its VIM). Interacts with RHBDD1 (via C-terminal
domain). Interacts with SPRTN; leading to recruitment to stalled
replication forks. Interacts with WASHC5. Interacts with UBOX5.
Interacts (via N-terminus) with UBXN7, UBXN8, and probably several
other UBX domain-containing proteins (via UBX domains); the
interactions are mutually exclusive with VIM-dependent
interactions such as those with AMFR and SELENOS. Forms a complex
with UBQLN1 and UBXN4. Interacts (via the PIM motif) with RNF31
(via the PUB domain). Interacts with DDX58/RIG-I and RNF125;
interaction takes place when DDX58/RIG-I is ubiquitinated via
'Lys-63'-linked ubiquitin on its CARD domains, leading to recruit
RNF125 and promote ubiquitination and degradation of DDX58/RIG-I.
Interacts with BAG6. Interacts with UBXN10. Interacts with UBXN6;
the interaction with UBXN6 is direct and competitive with UFD1.
Forms a ternary complex with CAV1 and UBXN6. Interacts with PLAA,
UBXN6 and YOD1; may form a complex involved in macroautophagy.
Interacts with ANKZF1. Interacts with ubiquitin-binding protein
FAF1. Interacts with ZFAND2B (via VIM motif); the interaction is
direct. Interacts with ZFAND1 (via its ubiquitin-like region);
this interaction occurs in an arsenite-dependent manner (By
similarity). {ECO:0000250|UniProtKB:P46462,
ECO:0000250|UniProtKB:P55072, ECO:0000250|UniProtKB:Q01853}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:P55072}. Endoplasmic reticulum
{ECO:0000250|UniProtKB:P55072}. Nucleus
{ECO:0000250|UniProtKB:P55072}. Cytoplasm, Stress granule
{ECO:0000250|UniProtKB:P55072}. Note=Recruited to the cytoplasmic
surface of the endoplasmic reticulum via interaction with
AMFR/gp78. Following DNA double-strand breaks, recruited to the
sites of damage. Recruited to stalled replication forks via
interaction with SPRTN. Recruited to damaged lysosomes decorated
with K48-linked ubiquitin chains. Colocalizes with TIA1, ZFAND1
and G3BP1 in cytoplasmic stress granules (SGs) in response to
arsenite-induced stress treatment (By similarity).
{ECO:0000250|UniProtKB:P55072}.
-!- PTM: ISGylated. {ECO:0000250|UniProtKB:P55072}.
-!- PTM: Methylation at Lys-315 catalyzed by VCPKMT is increased in
the presence of ASPSCR1. Lys-315 methylation may decrease ATPase
activity. {ECO:0000250|UniProtKB:P55072}.
-!- PTM: Phosphorylated by tyrosine kinases in response to T-cell
antigen receptor activation. Phosphorylated in mitotic cells.
{ECO:0000250|UniProtKB:P46462}.
-!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
-!- CAUTION: Valosin is an artifact of purification procedure,
generated in vitro by cleavage of the whole protein upon acid
extraction of tissues. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M30143; AAA31142.1; -; mRNA.
PIR; A26360; VPPG.
RefSeq; NP_999445.1; NM_214280.1.
UniGene; Ssc.856; -.
ProteinModelPortal; P03974; -.
SMR; P03974; -.
BioGrid; 1149651; 1.
STRING; 9823.ENSSSCP00000005692; -.
PaxDb; P03974; -.
PeptideAtlas; P03974; -.
PRIDE; P03974; -.
GeneID; 397524; -.
KEGG; ssc:397524; -.
CTD; 7415; -.
eggNOG; KOG0730; Eukaryota.
eggNOG; COG0464; LUCA.
HOGENOM; HOG000223224; -.
HOVERGEN; HBG001226; -.
InParanoid; P03974; -.
KO; K13525; -.
Proteomes; UP000008227; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; ISS:UniProtKB.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0097352; P:autophagosome maturation; ISS:UniProtKB.
GO; GO:0006914; P:autophagy; ISS:UniProtKB.
GO; GO:1903843; P:cellular response to arsenite ion; ISS:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
GO; GO:0061857; P:endoplasmic reticulum stress-induced pre-emptive quality control; ISS:UniProtKB.
GO; GO:0032510; P:endosome to lysosome transport via multivesicular body sorting pathway; ISS:UniProtKB.
GO; GO:0036503; P:ERAD pathway; ISS:UniProtKB.
GO; GO:0016236; P:macroautophagy; ISS:UniProtKB.
GO; GO:0010498; P:proteasomal protein catabolic process; ISS:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0018279; P:protein N-linked glycosylation via asparagine; ISS:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
GO; GO:0035617; P:stress granule disassembly; ISS:UniProtKB.
GO; GO:0019985; P:translesion synthesis; ISS:UniProtKB.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR005938; AAA_ATPase_CDC48.
InterPro; IPR009010; Asp_de-COase-like_dom_sf.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR003960; ATPase_AAA_CS.
InterPro; IPR004201; Cdc48_dom2.
InterPro; IPR029067; CDC48_domain_2-like_sf.
InterPro; IPR003338; CDC4_N-term_subdom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR015415; Vps4_C.
Pfam; PF00004; AAA; 2.
Pfam; PF02933; CDC48_2; 1.
Pfam; PF02359; CDC48_N; 1.
Pfam; PF09336; Vps4_C; 1.
SMART; SM00382; AAA; 2.
SMART; SM01072; CDC48_2; 1.
SMART; SM01073; CDC48_N; 1.
SUPFAM; SSF50692; SSF50692; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF54585; SSF54585; 1.
TIGRFAMs; TIGR01243; CDC48; 1.
PROSITE; PS00674; AAA; 2.
1: Evidence at protein level;
Acetylation; ATP-binding; Autophagy; Complete proteome; Cytoplasm;
Direct protein sequencing; DNA damage; DNA repair;
Endoplasmic reticulum; Hydrolase; Isopeptide bond; Lipid-binding;
Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Transport; Ubl conjugation;
Ubl conjugation pathway.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P55072}.
CHAIN 2 806 Transitional endoplasmic reticulum
ATPase.
/FTId=PRO_0000084574.
NP_BIND 247 253 ATP 1. {ECO:0000250|UniProtKB:P55072}.
NP_BIND 521 526 ATP 2. {ECO:0000250|UniProtKB:Q01853}.
REGION 797 806 Interaction with UBXN6. {ECO:0000250}.
BINDING 348 348 ATP 1. {ECO:0000250|UniProtKB:P55072}.
BINDING 384 384 ATP 1. {ECO:0000250|UniProtKB:P55072}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P55072}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000250|UniProtKB:P55072}.
MOD_RES 7 7 Phosphoserine.
{ECO:0000250|UniProtKB:P55072}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000250|UniProtKB:P55072}.
MOD_RES 37 37 Phosphoserine.
{ECO:0000250|UniProtKB:P55072}.
MOD_RES 315 315 N6,N6,N6-trimethyllysine; by VCPKMT.
{ECO:0000250|UniProtKB:P55072}.
MOD_RES 436 436 Phosphothreonine.
{ECO:0000250|UniProtKB:P55072}.
MOD_RES 462 462 Phosphoserine.
{ECO:0000250|UniProtKB:P55072}.
MOD_RES 502 502 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q01853}.
MOD_RES 505 505 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q01853}.
MOD_RES 668 668 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q01853}.
MOD_RES 668 668 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q01853}.
MOD_RES 702 702 Phosphoserine.
{ECO:0000250|UniProtKB:P55072}.
MOD_RES 754 754 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q01853}.
MOD_RES 770 770 Phosphoserine.
{ECO:0000250|UniProtKB:P55072}.
MOD_RES 775 775 Phosphoserine.
{ECO:0000250|UniProtKB:P55072}.
MOD_RES 787 787 Phosphoserine.
{ECO:0000250|UniProtKB:P55072}.
MOD_RES 805 805 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q01853}.
CROSSLNK 8 8 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P55072}.
CROSSLNK 18 18 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P55072}.
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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