TERA_XENLA
ID TERA_XENLA Reviewed; 805 AA.
AC P23787; Q7ZWL8;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 3.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Transitional endoplasmic reticulum ATPase;
DE Short=TER ATPase;
DE EC=3.6.4.6 {ECO:0000269|PubMed:2140770};
DE AltName: Full=15S Mg(2+)-ATPase p97 subunit;
DE Short=p97;
DE AltName: Full=Valosin-containing protein;
DE Short=VCP;
GN Name=vcp;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RA Peters J.-M.;
RL Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 443-805, PARTIAL PROTEIN SEQUENCE, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, HOMOHEXAMERIZATION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND PHOSPHORYLATION.
RC TISSUE=Embryo, and Oocyte;
RX PubMed=2140770; DOI=10.1002/j.1460-2075.1990.tb08300.x;
RA Peters J.-M., Walsh M.J., Franke W.W.;
RT "An abundant and ubiquitous homo-oligomeric ring-shaped ATPase particle
RT related to the putative vesicle fusion proteins Sec18p and NSF.";
RL EMBO J. 9:1757-1767(1990).
RN [4]
RP PROTEIN SEQUENCE OF 45-77 AND 389-405, INTERACTION WITH FACT COMPLEX, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10682845; DOI=10.1016/s0014-5793(99)01673-7;
RA Yamada T., Okuhara K., Iwamatsu A., Seo H., Ohta K., Shibata T.,
RA Murofushi H.;
RT "p97 ATPase, an ATPase involved in membrane fusion, interacts with DNA
RT unwinding factor (DUF) that functions in DNA replication.";
RL FEBS Lett. 466:287-291(2000).
RN [5]
RP FUNCTION.
RX PubMed=30979826; DOI=10.26508/lsa.201900390;
RA Priego Moreno S., Jones R.M., Poovathumkadavil D., Scaramuzza S.,
RA Gambus A.;
RT "Mitotic replisome disassembly depends on TRAIP ubiquitin ligase
RT activity.";
RL Life. Sci Alliance 2:0-0(2019).
RN [6]
RP FUNCTION.
RX PubMed=30849395; DOI=10.1016/j.molcel.2018.12.021;
RA Deng L., Wu R.A., Sonneville R., Kochenova O.V., Labib K., Pellman D.,
RA Walter J.C.;
RT "Mitotic CDK Promotes replisome disassembly, fork breakage, and complex DNA
RT rearrangements.";
RL Mol. Cell 73:915-929(2019).
RN [7]
RP FUNCTION.
RX PubMed=30842657; DOI=10.1038/s41586-019-1002-0;
RA Wu R.A., Semlow D.R., Kamimae-Lanning A.N., Kochenova O.V., Chistol G.,
RA Hodskinson M.R., Amunugama R., Sparks J.L., Wang M., Deng L., Mimoso C.A.,
RA Low E., Patel K.J., Walter J.C.;
RT "TRAIP is a master regulator of DNA interstrand crosslink repair.";
RL Nature 567:267-272(2019).
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 (PubMed:30979826,
CC PubMed:30849395, PubMed:30842657). 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 ddx58/rig-i (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:P46462, ECO:0000250|UniProtKB:P55072,
CC ECO:0000250|UniProtKB:Q7ZU99, ECO:0000269|PubMed:30842657,
CC ECO:0000269|PubMed:30849395, ECO:0000269|PubMed:30979826}.
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:0000269|PubMed:2140770};
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). {ECO:0000269|PubMed:2140770}.
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 contains subunits ssrp1/duf87 and supt16h/duf140.
CC {ECO:0000269|PubMed:10682845}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:2140770}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:P55072}. Nucleus
CC {ECO:0000269|PubMed:2140770}. Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:P55072}.
CC -!- TISSUE SPECIFICITY: Expressed in at least oocytes, liver and kidney (at
CC protein level). {ECO:0000269|PubMed:2140770}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:2140770}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X54240; CAA38146.1; -; mRNA.
DR EMBL; BC046949; AAH46949.1; -; mRNA.
DR PIR; S19738; S19738.
DR RefSeq; NP_001095217.1; NM_001101747.1.
DR AlphaFoldDB; P23787; -.
DR SMR; P23787; -.
DR BioGRID; 98733; 1.
DR DIP; DIP-60369N; -.
DR IntAct; P23787; 1.
DR GeneID; 380491; -.
DR KEGG; xla:380491; -.
DR CTD; 380491; -.
DR Xenbase; XB-GENE-969578; vcp.S.
DR OrthoDB; 194195at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 380491; Expressed in intestine and 19 other tissues.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA: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; IDA: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; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; IPI: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:0006281; P:DNA repair; IDA: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:0036297; P:interstrand cross-link repair; IDA:UniProtKB.
DR GO; GO:0016236; P:macroautophagy; ISS:UniProtKB.
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:1905634; P:regulation of protein localization to chromatin; IDA: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 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 ATP-binding; Autophagy; Cytoplasm; Direct protein sequencing; DNA damage;
KW DNA repair; Endoplasmic reticulum; Hydrolase; Lipid-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..805
FT /note="Transitional endoplasmic reticulum ATPase"
FT /id="PRO_0000084576"
FT REGION 708..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
FT CONFLICT 38
FT /note="M -> V (in Ref. 1; CAA38146)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="K -> E (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="A -> G (in Ref. 1; CAA38146)"
FT /evidence="ECO:0000305"
FT CONFLICT 742
FT /note="F -> L (in Ref. 1; CAA38146)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 805 AA; 89212 MW; 157D03B5BDB0F464 CRC64;
MASGSDTKSD DLSTAILKQK SRPNRLIVDE SINEDNSMVS LSQAKMDELQ LFRGDTVLLK
GKKRREAVCI VLSDDTCSDE KIRMNRVVRN NLRVRLGDVI SIQPCPDVKY GKRVHVLPID
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 MSIKKNVFII GATNRPDIID PAILRPGRLD QLIYIPLPDE KSRMAILKAN
LRKSPVAKDV DVDFLAKMTN GFSGADLTEI CQRACKLAIR ESIENEIRRE RDRQTNPSAM
EVEEDDPVPE IRRDHFEEAM RFARRSVSDN DIRKYEMFAQ TLQQSRGFGS FRFPAGGQSG
AGPSPGAGGG SGGGHFTEED DDLYG
