TERA2_CAEEL
ID TERA2_CAEEL Reviewed; 810 AA.
AC P54812; Q18560;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Transitional endoplasmic reticulum ATPase homolog 2;
DE EC=3.6.4.6 {ECO:0000269|PubMed:18782221};
DE AltName: Full=Cell division cycle-related protein 48.2;
DE AltName: Full=p97/CDC48 homolog 2;
GN Name=cdc-48.2; ORFNames=C41C4.8;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP DISRUPTION PHENOTYPE.
RX PubMed=15716356; DOI=10.1091/mbc.e04-08-0726;
RA Poteryaev D., Squirrell J.M., Campbell J.M., White J.G., Spang A.;
RT "Involvement of the actin cytoskeleton and homotypic membrane fusion in ER
RT dynamics in Caenorhabditis elegans.";
RL Mol. Biol. Cell 16:2139-2153(2005).
RN [3]
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=16701565; DOI=10.1016/j.bbrc.2006.04.160;
RA Yamauchi S., Yamanaka K., Ogura T.;
RT "Comparative analysis of expression of two p97 homologues in Caenorhabditis
RT elegans.";
RL Biochem. Biophys. Res. Commun. 345:746-753(2006).
RN [4]
RP FUNCTION, INTERACTION WITH CDC-48.1; UFD-1 AND UBXN-1, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16647269; DOI=10.1016/j.jsb.2006.02.015;
RA Mouysset J., Kaehler C., Hoppe T.;
RT "A conserved role of Caenorhabditis elegans CDC-48 in ER-associated protein
RT degradation.";
RL J. Struct. Biol. 156:41-49(2006).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17512499; DOI=10.1016/j.bbrc.2007.05.022;
RA Sasagawa Y., Yamanaka K., Nishikori S., Ogura T.;
RT "Caenorhabditis elegans p97/CDC-48 is crucial for progression of meiosis
RT I.";
RL Biochem. Biophys. Res. Commun. 358:920-924(2007).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17825049; DOI=10.1111/j.1365-2443.2007.01108.x;
RA Sasagawa Y., Yamanaka K., Ogura T.;
RT "ER E3 ubiquitin ligase HRD-1 and its specific partner chaperone BiP play
RT important roles in ERAD and developmental growth in Caenorhabditis
RT elegans.";
RL Genes Cells 12:1063-1073(2007).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18097415; DOI=10.1038/nature06388;
RA Ramadan K., Bruderer R., Spiga F.M., Popp O., Baur T., Gotta M.,
RA Meyer H.H.;
RT "Cdc48/p97 promotes reformation of the nucleus by extracting the kinase
RT Aurora B from chromatin.";
RL Nature 450:1258-1262(2007).
RN [8]
RP FUNCTION, INTERACTION WITH CDC-48.1 AND UFD-2, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 805-ASP--ASN-810.
RX PubMed=17369820; DOI=10.1038/ncb1554;
RA Janiesch P.C., Kim J., Mouysset J., Barikbin R., Lochmueller H.,
RA Cassata G., Krause S., Hoppe T.;
RT "The ubiquitin-selective chaperone CDC-48/p97 links myosin assembly to
RT human myopathy.";
RL Nat. Cell Biol. 9:379-390(2007).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND MUTAGENESIS
RP OF LYS-256 AND LYS-529.
RX PubMed=18782221; DOI=10.1111/j.1365-2443.2008.01214.x;
RA Nishikori S., Yamanaka K., Sakurai T., Esaki M., Ogura T.;
RT "p97 Homologs from Caenorhabditis elegans, CDC-48.1 and CDC-48.2, suppress
RT the aggregate formation of huntingtin exon1 containing expanded polyQ
RT repeat.";
RL Genes Cells 13:827-838(2008).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18728180; DOI=10.1073/pnas.0805944105;
RA Mouysset J., Deichsel A., Moser S., Hoege C., Hyman A.A., Gartner A.,
RA Hoppe T.;
RT "Cell cycle progression requires the CDC-48UFD-1/NPL-4 complex for
RT efficient DNA replication.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:12879-12884(2008).
RN [11]
RP INTERACTION WITH ATX-3 AND UBXN-5.
RX PubMed=19545544; DOI=10.1016/j.bbrc.2009.06.092;
RA Rodrigues A.J., Neves-Carvalho A., Ferro A., Rokka A., Corthals G.,
RA Logarinho E., Maciel P.;
RT "ATX-3, CDC-48 and UBXN-5: a new trimolecular complex in Caenorhabditis
RT elegans.";
RL Biochem. Biophys. Res. Commun. 386:575-581(2009).
RN [12]
RP INTERACTION WITH UBXN-1; UBXN-2; UBXN-3; UBXN-4; UBXN-6 AND UFD-1, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=20977550; DOI=10.1111/j.1365-2443.2010.01454.x;
RA Sasagawa Y., Yamanaka K., Saito-Sasagawa Y., Ogura T.;
RT "Caenorhabditis elegans UBX cofactors for CDC-48/p97 control
RT spermatogenesis.";
RL Genes Cells 15:1201-1215(2010).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21981920; DOI=10.1016/j.molcel.2011.08.028;
RA Franz A., Orth M., Pirson P.A., Sonneville R., Blow J.J., Gartner A.,
RA Stemmann O., Hoppe T.;
RT "CDC-48/p97 coordinates CDT-1 degradation with GINS chromatin dissociation
RT to ensure faithful DNA replication.";
RL Mol. Cell 44:85-96(2011).
RN [14]
RP FUNCTION, INTERACTION WITH ATX-3 AND UFD-2, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF 805-ASP--ASN-810.
RX PubMed=21317884; DOI=10.1038/ncb2200;
RA Kuhlbrodt K., Janiesch P.C., Kevei E., Segref A., Barikbin R., Hoppe T.;
RT "The Machado-Joseph disease deubiquitylase ATX-3 couples longevity and
RT proteostasis.";
RL Nat. Cell Biol. 13:273-281(2011).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22768338; DOI=10.1371/journal.pone.0040145;
RA Miedel M.T., Graf N.J., Stephen K.E., Long O.S., Pak S.C., Perlmutter D.H.,
RA Silverman G.A., Luke C.J.;
RT "A pro-cathepsin L mutant is a luminal substrate for endoplasmic-reticulum-
RT associated degradation in C. elegans.";
RL PLoS ONE 7:E40145-E40145(2012).
RN [16]
RP FUNCTION, INTERACTION WITH UBXN-2, AND DISRUPTION PHENOTYPE.
RX PubMed=23649807; DOI=10.1083/jcb.201209107;
RA Kress E., Schwager F., Holtackers R., Seiler J., Prodon F., Zanin E.,
RA Eiteneuer A., Toya M., Sugimoto A., Meyer H., Meraldi P., Gotta M.;
RT "The UBXN-2/p37/p47 adaptors of CDC-48/p97 regulate mitosis by limiting the
RT centrosomal recruitment of Aurora A.";
RL J. Cell Biol. 201:559-575(2013).
RN [17]
RP FUNCTION.
RX PubMed=25652260; DOI=10.15252/embr.201439123;
RA Marza E., Taouji S., Barroso K., Raymond A.A., Guignard L., Bonneu M.,
RA Pallares-Lupon N., Dupuy J.W., Fernandez-Zapico M.E., Rosenbaum J.,
RA Palladino F., Dupuy D., Chevet E.;
RT "Genome-wide screen identifies a novel p97/CDC-48-dependent pathway
RT regulating ER-stress-induced gene transcription.";
RL EMBO Rep. 16:332-340(2015).
RN [18]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH UBXN-3 AND CDT-1, INTERACTION
RP WITH UBXN-3 AND CDT-1, AND DISRUPTION PHENOTYPE.
RX PubMed=26842564; DOI=10.1038/ncomms10612;
RA Franz A., Pirson P.A., Pilger D., Halder S., Achuthankutty D., Kashkar H.,
RA Ramadan K., Hoppe T.;
RT "Chromatin-associated degradation is defined by UBXN-3/FAF1 to safeguard
RT DNA replication fork progression.";
RL Nat. Commun. 7:10612-10612(2016).
CC -!- FUNCTION: ATP-dependent chaperone which probably uses the energy
CC provided by ATP hydrolysis to generate mechanical force to unfold
CC substrate proteins, disassemble protein complexes, and disaggregate
CC protein aggregates (PubMed:18782221, PubMed:22768338). However, able to
CC prevent aggregation of unfolded proteins also in an ATP-independent
CC manner (PubMed:18782221). Targets polyubiquitinated proteins for
CC proteasomal degradation by binding to 'Lys-48'-linked polyubiquitin
CC chains (PubMed:19545544). Involved in the cytoplasmic elimination of
CC misfolded proteins exported from the ER (PubMed:16647269,
CC PubMed:17825049, PubMed:21317884, PubMed:22768338, PubMed:25652260).
CC This pathway, known as ERAD, prevents the activation of the unfolded
CC protein response (UPR) caused by the accumulation of misfolded proteins
CC in the ER (PubMed:16647269, PubMed:17825049, PubMed:21317884,
CC PubMed:22768338, PubMed:25652260). Together with udf-2 and chn-1,
CC regulates myosin assembly in body wall muscles by targeting myosin
CC chaperone unc-45 for proteasomal degradation (PubMed:17369820). During
CC oocyte meiosis and together with cdc-48.1, required for chromosome
CC condensation at the diakinesis phase in prophase I and for progression
CC of metaphase I (PubMed:17512499). During the first embryonic cell
CC division, regulates DNA replication and thus chromosome segregation and
CC decondensation, and nuclear envelope re-assembly (PubMed:18097415,
CC PubMed:18728180, PubMed:21981920, PubMed:26842564). In S phase and in
CC association with ufd-1, npl-4.1 and/or npl-4.2 and ubxn-3, ensures the
CC degradation of DNA licensing factor cdt-1 after the initiation of DNA
CC replication and thus the disassembly of the DNA replication CMG
CC helicase complex by promoting the dissociation from chromatin of
CC several of its components including cdc-45 and sld-5 (PubMed:21981920,
CC PubMed:26842564). Regulates ubxn-3 nuclear localization during S phase
CC (PubMed:26842564). During the first embryonic cell divisions and
CC together with cdc-48.1, regulates the re-assembly of the nuclear
CC envelope after mitosis possibly by inactivating kinase air-2, a
CC component of the chromosomal passenger complex (CPC) (PubMed:18097415).
CC {ECO:0000269|PubMed:16647269, ECO:0000269|PubMed:17369820,
CC ECO:0000269|PubMed:17512499, ECO:0000269|PubMed:17825049,
CC ECO:0000269|PubMed:18097415, ECO:0000269|PubMed:18728180,
CC ECO:0000269|PubMed:18782221, ECO:0000269|PubMed:21317884,
CC ECO:0000269|PubMed:21981920, ECO:0000269|PubMed:22768338,
CC ECO:0000269|PubMed:23649807, ECO:0000269|PubMed:25652260,
CC ECO:0000269|PubMed:26842564}.
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:18782221};
CC -!- ACTIVITY REGULATION: The first ATP-binding region has low ATPase
CC activity (By similarity). The second ATP-binding region is responsible
CC for ATPase activity (By similarity). ATP binding to the first ATP-
CC binding region induces intrinsic activity of the second ATP-binding
CC region (By similarity). While ATP binding to the first ATP-binding
CC region appears to prevent ATP hydrolysis by the second ATP-binding
CC region, ADP-binding to first region promotes the coordinate and
CC cooperative ATPase cycle of the second ATP-binding region (By
CC similarity). ATP binding to the first ATP-binding region induces a
CC conformational change, promoting the rotation of the first ATP-binding
CC region relative to the second ATP-binding region in the hexamer (By
CC similarity). Inhibited by N-ethylmaleimide (NEM) (PubMed:18782221).
CC {ECO:0000250|UniProtKB:P54811, ECO:0000269|PubMed:18782221}.
CC -!- SUBUNIT: Homohexamer; oligomerization is ATP-independent
CC (PubMed:18782221). Forms a ring-shaped particle of 18.3 nm diameter,
CC that displays 6-fold radial symmetry (By similarity). Interacts with
CC cdc-48.1 and thus may form heterohexamers (PubMed:16647269,
CC PubMed:17369820). Forms a complex composed of ubxn-3, cdc-48.1 and/or
CC cdc-48.2 and substrate cdt-1 (PubMed:26842564). Interacts (via N-
CC terminus) with ubxn-3 (PubMed:20977550). Interacts (via N-terminus)
CC with atx-3 (via RRDR motif) (PubMed:19545544, PubMed:21317884).
CC Interacts (via N-terminus) with ubxn-5 (PubMed:19545544). Interacts
CC with ufd-1 (PubMed:16647269). Interacts (via DDDLYN motif) with ufd-2
CC (PubMed:21317884, PubMed:17369820). Interacts (via N-terminus) with
CC ubxn-1 (PubMed:16647269, PubMed:20977550). Interacts (via N-terminus)
CC with ubxn-2 (PubMed:23649807, PubMed:20977550). Interacts (via N-
CC terminus) with ubxn-4 (PubMed:20977550). Interacts with ubxn-6
CC (PubMed:20977550). {ECO:0000250|UniProtKB:P54811,
CC ECO:0000269|PubMed:16647269, ECO:0000269|PubMed:17369820,
CC ECO:0000269|PubMed:18782221, ECO:0000269|PubMed:19545544,
CC ECO:0000269|PubMed:20977550, ECO:0000269|PubMed:21317884,
CC ECO:0000269|PubMed:23649807, ECO:0000269|PubMed:26842564}.
CC -!- INTERACTION:
CC P54812; O17850: atx-3; NbExp=3; IntAct=EBI-320265, EBI-320650;
CC P54812; P54811: cdc-48.1; NbExp=6; IntAct=EBI-320265, EBI-320245;
CC P54812; P54812: cdc-48.2; NbExp=3; IntAct=EBI-320265, EBI-320265;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17369820}.
CC -!- TISSUE SPECIFICITY: Expressed in body wall muscles.
CC {ECO:0000269|PubMed:17369820}.
CC -!- DEVELOPMENTAL STAGE: Predominantly expressed in embryos (at protein
CC level) (PubMed:16701565). Expression transiently increases at the L2
CC larval stage (PubMed:17369820). {ECO:0000269|PubMed:16701565,
CC ECO:0000269|PubMed:17369820}.
CC -!- INDUCTION: Induced upon ER stress. Repressed by starvation and
CC oxidative stress. {ECO:0000269|PubMed:16701565}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes embryonic
CC lethality in 30-50 percent of embryos (PubMed:15716356). RNAi-mediated
CC knockdown prevents ubxn-2 nuclear localization in the 2-cell embryo
CC (PubMed:23649807). RNAi-mediated knockdown in an unc-45 (m94) mutant
CC background, does not restore motility (PubMed:17369820). Simultaneous
CC RNAi-mediated knockdown of cdc-48.1 causes embryonic lethality
CC (PubMed:15716356, PubMed:16647269, PubMed:18097415, PubMed:18728180,
CC PubMed:26842564). Defects in oocyte meiosis I progression
CC (PubMed:17512499). Defects in embryo S phase DNA replication causing
CC delays in cell cycle progression (PubMed:17512499, PubMed:18097415,
CC PubMed:18728180, PubMed:21981920). At the end of mitosis, impairs
CC chromatin decondensation and nuclear envelope re-assembly
CC (PubMed:18728180, PubMed:18097415). In addition, abnormal accumulation
CC of air-2 on mitotic chromatin and impaired air-2 activation
CC (PubMed:18097415). Does not affect ER transition into sheet-like
CC structures at the onset of embryonic mitosis (PubMed:15716356).
CC Simultaneous RNAi-mediated knockdown of cdc-48.2 in young adults
CC decreases lifespan, induces the unfolded protein response, increases
CC overall levels of polyubiquitinated proteins, and impairs the
CC degradation of misfolded ER proteins (PubMed:16647269, PubMed:17825049,
CC PubMed:17369820, PubMed:21317884, PubMed:22768338). Causes defects in
CC germline development (PubMed:20977550). {ECO:0000269|PubMed:15716356,
CC ECO:0000269|PubMed:16647269, ECO:0000269|PubMed:17369820,
CC ECO:0000269|PubMed:17512499, ECO:0000269|PubMed:17825049,
CC ECO:0000269|PubMed:18097415, ECO:0000269|PubMed:18728180,
CC ECO:0000269|PubMed:20977550, ECO:0000269|PubMed:21317884,
CC ECO:0000269|PubMed:21981920, ECO:0000269|PubMed:22768338,
CC ECO:0000269|PubMed:23649807, ECO:0000269|PubMed:26842564}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. CDC48 subfamily.
CC {ECO:0000305}.
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DR EMBL; Z48045; CAA88105.1; -; Genomic_DNA.
DR EMBL; Z48334; CAA88105.1; JOINED; Genomic_DNA.
DR PIR; T19879; T19879.
DR RefSeq; NP_495705.1; NM_063304.5.
DR AlphaFoldDB; P54812; -.
DR SMR; P54812; -.
DR BioGRID; 39638; 53.
DR DIP; DIP-26566N; -.
DR IntAct; P54812; 6.
DR STRING; 6239.C41C4.8.2; -.
DR iPTMnet; P54812; -.
DR EPD; P54812; -.
DR PaxDb; P54812; -.
DR PeptideAtlas; P54812; -.
DR PRIDE; P54812; -.
DR EnsemblMetazoa; C41C4.8.1; C41C4.8.1; WBGene00008053.
DR GeneID; 174309; -.
DR KEGG; cel:CELE_C41C4.8; -.
DR UCSC; C41C4.8.1; c. elegans.
DR CTD; 174309; -.
DR WormBase; C41C4.8; CE05402; WBGene00008053; cdc-48.2.
DR eggNOG; KOG0730; Eukaryota.
DR GeneTree; ENSGT00970000196377; -.
DR HOGENOM; CLU_000688_12_0_1; -.
DR InParanoid; P54812; -.
DR OMA; HACHDIK; -.
DR OrthoDB; 194195at2759; -.
DR PhylomeDB; P54812; -.
DR Reactome; R-CEL-110320; Translesion Synthesis by POLH.
DR Reactome; R-CEL-3371511; HSF1 activation.
DR Reactome; R-CEL-382556; ABC-family proteins mediated transport.
DR Reactome; R-CEL-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR Reactome; R-CEL-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-CEL-5689877; Josephin domain DUBs.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-8876725; Protein methylation.
DR Reactome; R-CEL-8951664; Neddylation.
DR Reactome; R-CEL-9013407; RHOH GTPase cycle.
DR Reactome; R-CEL-9755511; KEAP1-NFE2L2 pathway.
DR PRO; PR:P54812; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00008053; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IPI:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:WormBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR GO; GO:0097352; P:autophagosome maturation; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:WormBase.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IGI:WormBase.
DR GO; GO:0051228; P:mitotic spindle disassembly; IBA:GO_Central.
DR GO; GO:1904780; P:negative regulation of protein localization to centrosome; IMP:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; IDA:UniProtKB.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
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; Chaperone; Cytoplasm; Hydrolase; Nucleotide-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..810
FT /note="Transitional endoplasmic reticulum ATPase homolog 2"
FT /id="PRO_0000084578"
FT REGION 713..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..810
FT /note="Interaction with ufd-2"
FT /evidence="ECO:0000269|PubMed:17369820,
FT ECO:0000269|PubMed:21317884"
FT BINDING 252..258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT BINDING 353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT BINDING 389
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT BINDING 526..531
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q01853"
FT MUTAGEN 256
FT /note="K->A: Loss of catalytic activity without affecting
FT oligomerization; when associated with A-529."
FT /evidence="ECO:0000269|PubMed:18782221"
FT MUTAGEN 529
FT /note="K->A: Loss of catalytic activity without affecting
FT oligomerization; when associated with A-256."
FT /evidence="ECO:0000269|PubMed:18782221"
FT MUTAGEN 805..810
FT /note="Missing: Loss of interaction with ufd-2 but not with
FT atx-3."
FT /evidence="ECO:0000269|PubMed:17369820,
FT ECO:0000269|PubMed:21317884"
SQ SEQUENCE 810 AA; 89640 MW; 904DA78FA1B007AE CRC64;
MASVPTQRDE KEKKNDELAT AILKDKKRPN RLIIDQSDND DNSMVMLSQA KMDELGLFRG
DSVILKGKKR RETVSIVLNA DNCPNDKIKM NKVVRNNLRS RLGDVVSISS AQLEYGKRVH
VLPIDDTIEG LTGNLFDVFL RPYFTDAYRP VHKGDIFTVQ AAMRTVEFKV VETDPAPACI
VAPDTVIHYE GDPIKREEEE EALNEVGYDD LGGVRKQLAQ IKEMVELPLR HPQLFKAIGV
KPPRGILLFG PPGTGKTLIA RAVANETGAF FFLINGPEIM SKMSGESESN LRKAFAECEK
NSPAILFIDE IDAIAPKREK AHGEVEKRIV SQLLTLMDGL KTRAHVVVIA ATNRPNSIDG
ALRRFGRFDR EIDIGIPDAV GRLEILRIHT KNMKLGEDVD LEQVANECHG FVGADLASLC
SEAAIQQIRE KMELIDLEDD TIDAEVLNSL AVTMENFRFA MGKSSPSALR EAVVETPNTT
WSDIGGLQNV KRELQELVQY PVEHPEKYLK FGMQPSRGVL FYGPPGCGKT LLAKAIANEC
QANFISIKGP ELLTMWFGES EANVRDVFDK ARAAAPCVLF FDELDSIAKA RGGSVGDAGG
AADRVINQVL TEMDGMNAKK NVFIIGATNR PDIIDPAVLR PGRLDQLIYI PLPDEASRLQ
IFKASLRKTP LSADLDLNFL AKNTVGFSGA DLTEICQRAC KLAIRESIER EIRQEKERQD
RSARGEELME DELADPVPEI TRAHFEEAMK FARRSVTDND IRKYEMFAQT LQQSRGFGNN
FKFPGEAPSA GQPVGGNGGS GGNDDDDLYN
