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Transitional endoplasmic reticulum ATPase homolog 1 (EC 3.6.4.6) (Cell division cycle-related protein 48.1) (p97/CDC48 homolog 1)

 TERA1_CAEEL             Reviewed;         809 AA.
P54811;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
02-JUN-2021, entry version 162.
RecName: Full=Transitional endoplasmic reticulum ATPase homolog 1 {ECO:0000305};
EC=3.6.4.6 {ECO:0000269|PubMed:18782221, ECO:0000269|PubMed:18854144, ECO:0000269|PubMed:21454554};
AltName: Full=Cell division cycle-related protein 48.1 {ECO:0000312|WormBase:C06A1.1};
AltName: Full=p97/CDC48 homolog 1 {ECO:0000305};
Name=cdc-48.1 {ECO:0000312|WormBase:C06A1.1};
ORFNames=C06A1.1 {ECO:0000312|WormBase:C06A1.1};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for investigating
biology.";
Science 282:2012-2018(1998).
[2]
DISRUPTION PHENOTYPE.
PubMed=15716356; DOI=10.1091/mbc.e04-08-0726;
Poteryaev D., Squirrell J.M., Campbell J.M., White J.G., Spang A.;
"Involvement of the actin cytoskeleton and homotypic membrane fusion in ER
dynamics in Caenorhabditis elegans.";
Mol. Biol. Cell 16:2139-2153(2005).
[3]
TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
PubMed=16701565; DOI=10.1016/j.bbrc.2006.04.160;
Yamauchi S., Yamanaka K., Ogura T.;
"Comparative analysis of expression of two p97 homologues in Caenorhabditis
elegans.";
Biochem. Biophys. Res. Commun. 345:746-753(2006).
[4]
FUNCTION, INTERACTION WITH CDC-48.2; UFD-1 AND UBXN-1, AND DISRUPTION
PHENOTYPE.
PubMed=16647269; DOI=10.1016/j.jsb.2006.02.015;
Mouysset J., Kaehler C., Hoppe T.;
"A conserved role of Caenorhabditis elegans CDC-48 in ER-associated protein
degradation.";
J. Struct. Biol. 156:41-49(2006).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17512499; DOI=10.1016/j.bbrc.2007.05.022;
Sasagawa Y., Yamanaka K., Nishikori S., Ogura T.;
"Caenorhabditis elegans p97/CDC-48 is crucial for progression of meiosis
I.";
Biochem. Biophys. Res. Commun. 358:920-924(2007).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17825049; DOI=10.1111/j.1365-2443.2007.01108.x;
Sasagawa Y., Yamanaka K., Ogura T.;
"ER E3 ubiquitin ligase HRD-1 and its specific partner chaperone BiP play
important roles in ERAD and developmental growth in Caenorhabditis
elegans.";
Genes Cells 12:1063-1073(2007).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18097415; DOI=10.1038/nature06388;
Ramadan K., Bruderer R., Spiga F.M., Popp O., Baur T., Gotta M.,
Meyer H.H.;
"Cdc48/p97 promotes reformation of the nucleus by extracting the kinase
Aurora B from chromatin.";
Nature 450:1258-1262(2007).
[8]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH UNC-45; UFD-2 AND CHN-1,
INTERACTION WITH CDC-48.2 AND UFD-2, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
804-ASP--ASN-809.
PubMed=17369820; DOI=10.1038/ncb1554;
Janiesch P.C., Kim J., Mouysset J., Barikbin R., Lochmueller H.,
Cassata G., Krause S., Hoppe T.;
"The ubiquitin-selective chaperone CDC-48/p97 links myosin assembly to
human myopathy.";
Nat. Cell Biol. 9:379-390(2007).
[9]
FUNCTION, CATALYTIC ACTIVITY, LACK OF INTERACTION WITH AIR-2, AND
DISRUPTION PHENOTYPE.
PubMed=18854144; DOI=10.1016/j.devcel.2008.08.005;
Heallen T.R., Adams H.P., Furuta T., Verbrugghe K.J., Schumacher J.M.;
"An Afg2/Spaf-related Cdc48-like AAA ATPase regulates the stability and
activity of the C. elegans Aurora B kinase AIR-2.";
Dev. Cell 15:603-616(2008).
[10]
FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND MUTAGENESIS
OF LYS-257 AND LYS-530.
PubMed=18782221; DOI=10.1111/j.1365-2443.2008.01214.x;
Nishikori S., Yamanaka K., Sakurai T., Esaki M., Ogura T.;
"p97 Homologs from Caenorhabditis elegans, CDC-48.1 and CDC-48.2, suppress
the aggregate formation of huntingtin exon1 containing expanded polyQ
repeat.";
Genes Cells 13:827-838(2008).
[11]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH HIM-6 AND CRP-1, INTERACTION
WITH HIM-6 AND CRP-1, AND DISRUPTION PHENOTYPE.
PubMed=18458060; DOI=10.1128/mcb.02252-07;
Caruso M.E., Jenna S., Bouchecareilh M., Baillie D.L., Boismenu D.,
Halawani D., Latterich M., Chevet E.;
"GTPase-mediated regulation of the unfolded protein response in
Caenorhabditis elegans is dependent on the AAA+ ATPase CDC-48.";
Mol. Cell. Biol. 28:4261-4274(2008).
[12]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18728180; DOI=10.1073/pnas.0805944105;
Mouysset J., Deichsel A., Moser S., Hoege C., Hyman A.A., Gartner A.,
Hoppe T.;
"Cell cycle progression requires the CDC-48UFD-1/NPL-4 complex for
efficient DNA replication.";
Proc. Natl. Acad. Sci. U.S.A. 105:12879-12884(2008).
[13]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH ATX-3 AND UBXN-5, AND
INTERACTION WITH ATX-3 AND UBXN-5.
PubMed=19545544; DOI=10.1016/j.bbrc.2009.06.092;
Rodrigues A.J., Neves-Carvalho A., Ferro A., Rokka A., Corthals G.,
Logarinho E., Maciel P.;
"ATX-3, CDC-48 and UBXN-5: a new trimolecular complex in Caenorhabditis
elegans.";
Biochem. Biophys. Res. Commun. 386:575-581(2009).
[14]
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=19773360; DOI=10.1242/jcs.052415;
Sasagawa Y., Otani M., Higashitani N., Higashitani A., Sato K., Ogura T.,
Yamanaka K.;
"Caenorhabditis elegans p97 controls germline-specific sex determination by
controlling the TRA-1 level in a CUL-2-dependent manner.";
J. Cell Sci. 122:3663-3672(2009).
[15]
IDENTIFICATION IN A COMPLEX WITH UBXN-3; UFD-1 AND NPL-4.1, INTERACTION
WITH UBXN-1; UBXN-2; UBXN-3; UBXN-4; UBXN-6 AND UFD-1, SUBCELLULAR
LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=20977550; DOI=10.1111/j.1365-2443.2010.01454.x;
Sasagawa Y., Yamanaka K., Saito-Sasagawa Y., Ogura T.;
"Caenorhabditis elegans UBX cofactors for CDC-48/p97 control
spermatogenesis.";
Genes Cells 15:1201-1215(2010).
[16]
CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
MUTAGENESIS OF LYS-257; GLU-311; ASN-354; ARG-365; PRO-467; ARG-471;
LYS-530; GLU-584; ASN-631 AND ARG-642.
PubMed=21454554; DOI=10.1074/jbc.m110.201400;
Nishikori S., Esaki M., Yamanaka K., Sugimoto S., Ogura T.;
"Positive cooperativity of the p97 AAA ATPase is critical for essential
functions.";
J. Biol. Chem. 286:15815-15820(2011).
[17]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=21981920; DOI=10.1016/j.molcel.2011.08.028;
Franz A., Orth M., Pirson P.A., Sonneville R., Blow J.J., Gartner A.,
Stemmann O., Hoppe T.;
"CDC-48/p97 coordinates CDT-1 degradation with GINS chromatin dissociation
to ensure faithful DNA replication.";
Mol. Cell 44:85-96(2011).
[18]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH ATX-3 AND UFD-2, INTERACTION
WITH ATX-3 AND UFD-2, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
804-ASP--ASN-809.
PubMed=21317884; DOI=10.1038/ncb2200;
Kuhlbrodt K., Janiesch P.C., Kevei E., Segref A., Barikbin R., Hoppe T.;
"The Machado-Joseph disease deubiquitylase ATX-3 couples longevity and
proteostasis.";
Nat. Cell Biol. 13:273-281(2011).
[19]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22768338; DOI=10.1371/journal.pone.0040145;
Miedel M.T., Graf N.J., Stephen K.E., Long O.S., Pak S.C., Perlmutter D.H.,
Silverman G.A., Luke C.J.;
"A pro-cathepsin L mutant is a luminal substrate for endoplasmic-reticulum-
associated degradation in C. elegans.";
PLoS ONE 7:E40145-E40145(2012).
[20]
INTERACTION WITH UBXN-2.
PubMed=23649807; DOI=10.1083/jcb.201209107;
Kress E., Schwager F., Holtackers R., Seiler J., Prodon F., Zanin E.,
Eiteneuer A., Toya M., Sugimoto A., Meyer H., Meraldi P., Gotta M.;
"The UBXN-2/p37/p47 adaptors of CDC-48/p97 regulate mitosis by limiting the
centrosomal recruitment of Aurora A.";
J. Cell Biol. 201:559-575(2013).
[21]
ACTIVITY REGULATION, SUBUNIT, AND MUTAGENESIS OF LYS-530 AND GLU-584.
PubMed=24055316; DOI=10.1016/j.str.2013.08.017;
Noi K., Yamamoto D., Nishikori S., Arita-Morioka K., Kato T., Ando T.,
Ogura T.;
"High-speed atomic force microscopic observation of ATP-dependent rotation
of the AAA+ chaperone p97.";
Structure 21:1992-2002(2013).
[22]
INTERACTION WITH UFD-3 AND CDC-48.2, AND SUBCELLULAR LOCATION.
PubMed=25721663; DOI=10.1016/j.bbrc.2015.02.088;
Murayama Y., Ogura T., Yamanaka K.;
"Characterization of C-terminal adaptors, UFD-2 and UFD-3, of CDC-48 on the
polyglutamine aggregation in C. elegans.";
Biochem. Biophys. Res. Commun. 459:154-160(2015).
[23]
FUNCTION.
PubMed=25652260; DOI=10.15252/embr.201439123;
Marza E., Taouji S., Barroso K., Raymond A.A., Guignard L., Bonneu M.,
Pallares-Lupon N., Dupuy J.W., Fernandez-Zapico M.E., Rosenbaum J.,
Palladino F., Dupuy D., Chevet E.;
"Genome-wide screen identifies a novel p97/CDC-48-dependent pathway
regulating ER-stress-induced gene transcription.";
EMBO Rep. 16:332-340(2015).
[24]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH UBXN-3 AND CDT-1, INTERACTION
WITH UBXN-3 AND CDT-1, AND DISRUPTION PHENOTYPE.
PubMed=26842564; DOI=10.1038/ncomms10612;
Franz A., Pirson P.A., Pilger D., Halder S., Achuthankutty D., Kashkar H.,
Ramadan K., Hoppe T.;
"Chromatin-associated degradation is defined by UBXN-3/FAF1 to safeguard
DNA replication fork progression.";
Nat. Commun. 7:10612-10612(2016).
[25]
INTERACTION WITH UFD-2.
PubMed=27669035; DOI=10.1038/nsmb.3296;
Ackermann L., Schell M., Pokrzywa W., Kevei E., Gartner A., Schumacher B.,
Hoppe T.;
"E4 ligase-specific ubiquitination hubs coordinate DNA double-strand-break
repair and apoptosis.";
Nat. Struct. Mol. Biol. 23:995-1002(2016).
[26]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=28368371; DOI=10.1038/ncb3500;
Sonneville R., Moreno S.P., Knebel A., Johnson C., Hastie C.J., Gartner A.,
Gambus A., Labib K.;
"CUL-2LRR-1 and UBXN-3 drive replisome disassembly during DNA replication
termination and mitosis.";
Nat. Cell Biol. 19:468-479(2017).
-!- FUNCTION: ATP-dependent chaperone which probably uses the energy
provided by ATP hydrolysis to generate mechanical force to unfold
substrate proteins, disassemble protein complexes, and disaggregate
protein aggregates (PubMed:18854144, PubMed:18782221, PubMed:22768338).
Can also prevent aggregation of unfolded proteins also in an ATP-
independent manner (PubMed:18782221). Targets polyubiquitinated
proteins for proteasomal degradation by binding to 'Lys-48'-linked
polyubiquitin chains (PubMed:19545544). Involved in the cytoplasmic
elimination of misfolded proteins exported from the ER
(PubMed:16647269, PubMed:17825049, PubMed:21317884, PubMed:22768338,
PubMed:25652260). This pathway, known as ERAD, prevents the activation
of the unfolded protein response (UPR) caused by the accumulation of
misfolded proteins in the ER (PubMed:16647269, PubMed:17825049,
PubMed:21317884, PubMed:22768338, PubMed:25652260). In association with
helicase him-6 and GTPase crp-1, regulates the unfolded protein
response (UPR) following ER stress, probably independently of the ERAD
pathway (PubMed:18458060). Together with udf-2 and chn-1, regulates
myosin assembly in body wall muscles by targeting myosin chaperone unc-
45 for proteasomal degradation (PubMed:17369820). Together with the
ufd-1-npl-4 complex, controls the switch from spermatogenesis to
oogenesis by regulating E3 ligase cul-2 complex-mediated tra-1
proteasomal degradation (PubMed:19773360). During oocyte meiosis and
together with cdc-48.2, required for chromosome condensation at the
diakinesis phase in prophase I and for progression of metaphase I
(PubMed:17512499). During the first embryonic cell division, regulates
DNA replication and thus chromosome segregation and decondensation, and
nuclear envelope re-assembly (PubMed:18097415, PubMed:18854144,
PubMed:18728180, PubMed:21981920, PubMed:26842564, PubMed:28368371). In
S phase and in association with ufd-1, npl-4.1 and/or npl-4.2 and ubxn-
3, ensures the degradation of DNA licensing factor cdt-1 after the
initiation of DNA replication and thus the disassembly of the DNA
replication CMG helicase complex by promoting the dissociation from
chromatin of several of its components including cdc-45 and sld-5
(PubMed:21981920, PubMed:26842564, PubMed:28368371). Regulates ubxn-3
nuclear localization during S phase (PubMed:26842564). During the first
embryonic cell divisions and together with cdc-48.2, regulates the re-
assembly of the nuclear envelope after mitosis possibly by inactivating
kinase air-2, a component of the chromosomal passenger complex (CPC)
(PubMed:18097415). However, in another study, cdc-48.1 does not appear
to be implicated in the regulation of air-2 (PubMed:18854144).
{ECO:0000269|PubMed:16647269, ECO:0000269|PubMed:17369820,
ECO:0000269|PubMed:17512499, ECO:0000269|PubMed:17825049,
ECO:0000269|PubMed:18097415, ECO:0000269|PubMed:18458060,
ECO:0000269|PubMed:18728180, ECO:0000269|PubMed:18782221,
ECO:0000269|PubMed:18854144, ECO:0000269|PubMed:19545544,
ECO:0000269|PubMed:19773360, ECO:0000269|PubMed:21317884,
ECO:0000269|PubMed:21981920, ECO:0000269|PubMed:22768338,
ECO:0000269|PubMed:25652260, ECO:0000269|PubMed:26842564,
ECO:0000269|PubMed:28368371}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.6;
Evidence={ECO:0000269|PubMed:18782221, ECO:0000269|PubMed:18854144,
ECO:0000269|PubMed:21454554};
-!- ACTIVITY REGULATION: The first ATP-binding region has low ATPase
activity (PubMed:21454554). The second ATP-binding region is
responsible for ATPase activity (PubMed:21454554). ATP binding to the
first ATP-binding region induces intrinsic activity of the second ATP-
binding region (PubMed:21454554). While ATP binding to the first ATP-
binding region appears to prevent ATP hydrolysis by the second ATP-
binding region, ADP-binding to first region promotes the coordinate and
cooperative ATPase cycle of the second ATP-binding region
(PubMed:21454554). ATP binding to the first ATP-binding region induces
a conformational change, promoting the rotation of the first ATP-
binding region relative to the second ATP-binding region in the hexamer
(PubMed:24055316). Inhibited by N-ethylmaleimide (NEM)
(PubMed:18782221). {ECO:0000269|PubMed:18782221,
ECO:0000269|PubMed:21454554, ECO:0000269|PubMed:24055316}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.39 mM for ATP (at 30 degrees Celsius)
{ECO:0000269|PubMed:21454554};
-!- SUBUNIT: Homohexamer; oligomerization is ATP-independent
(PubMed:18782221, PubMed:24055316). Forms a ring-shaped particle of
18.3 nm diameter, that displays 6-fold radial symmetry
(PubMed:24055316). Interacts with cdc-48.2 and thus may form
heterohexamers (PubMed:16647269, PubMed:17369820, PubMed:25721663).
Forms a complex composed of cdc-48.1, him-6 and crp-1; within the
complex, interacts with helicase him-6 and GTPase crp-1
(PubMed:18458060). Forms a complex composed of deubiquitinating enzyme
atx-3, adapter ubxn-5 and cdc-48.1; within the complex, interacts (via
N-terminus) with ubxn-5 and with atx-3 (PubMed:19545544). Forms a
complex composed of deubiquitinating enzyme atx-3, E4 ubiquitin-protein
ligase ufd-2 and cdc-48.1; within the complex, interacts with atx-3 and
(via DDDLYN motif) with ufd-2 (PubMed:21317884, PubMed:27669035).
Interacts (via N-terminus) with atx-3 (via RRDR motif); the interaction
is not required for atx-3 enzymatic activity (PubMed:19545544,
PubMed:21317884). Forms a complex composed of cdc-48.1, myosin
chaperone unc-45, ubiquitin-protein ligases ufd-2 and chn-1; within the
complex, interacts (via DDDLYN motif) with ufd-2 and targets myosin
chaperone unc-45 for proteasomal degradation (PubMed:17369820,
PubMed:27669035). Forms a complex composed of ubxn-3, ufd-1, npl-4.1
and cdc-48.1; within the complex, interacts (via N-terminus) with ubxn-
3 (via FPK motif) and with ufd-1 (PubMed:16647269, PubMed:20977550).
Forms a complex composed of ubxn-3, cdc-48.1 and/or cdc-48.2 and
substrate cdt-1 (PubMed:26842564). Interacts (via N-terminus) with
ubxn-1 (PubMed:16647269, PubMed:20977550). Interacts (via N-terminus)
with ubxn-2 (PubMed:23649807, PubMed:20977550). Interacts (via N-
terminus) with ubxn-4 (PubMed:20977550). Interacts with ubxn-6
(PubMed:20977550). Interacts with ufd-3 (PubMed:25721663). Does not
interact with air-2 (PubMed:18854144). {ECO:0000269|PubMed:16647269,
ECO:0000269|PubMed:17369820, ECO:0000269|PubMed:18458060,
ECO:0000269|PubMed:18782221, ECO:0000269|PubMed:18854144,
ECO:0000269|PubMed:19545544, ECO:0000269|PubMed:20977550,
ECO:0000269|PubMed:21317884, ECO:0000269|PubMed:23649807,
ECO:0000269|PubMed:24055316, ECO:0000269|PubMed:25721663,
ECO:0000269|PubMed:26842564, ECO:0000269|PubMed:27669035}.
-!- INTERACTION:
P54811; P54811: cdc-48.1; NbExp=2; IntAct=EBI-320245, EBI-320245;
P54811; P54812: cdc-48.2; NbExp=6; IntAct=EBI-320245, EBI-320265;
P54811; Q9TXH9: ubxn-1; NbExp=3; IntAct=EBI-320245, EBI-320236;
-!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
{ECO:0000269|PubMed:20977550, ECO:0000269|PubMed:25721663}. Cytoplasm
{ECO:0000269|PubMed:17369820}. Note=Colocalizes with ubxn-1, ubxn-2 and
ubxn-3 to the perinuclear region in spermatocytes (PubMed:20977550).
Localizes to the perinuclear region in intestinal cells
(PubMed:25721663). {ECO:0000269|PubMed:20977550,
ECO:0000269|PubMed:25721663}.
-!- TISSUE SPECIFICITY: Expressed in germ cells and spermatheca
(PubMed:16701565). Expressed in body wall muscles (PubMed:17369820).
{ECO:0000269|PubMed:16701565, ECO:0000269|PubMed:17369820}.
-!- DEVELOPMENTAL STAGE: Expressed highly in embryos (at protein level)
(PubMed:16701565, PubMed:17369820). Expression decreases in larvae and
increases again in adults (at protein level) (PubMed:16701565,
PubMed:17369820). At the L4 larval stage, expressed in the proximal
gonad, predominantly at the pachytene stage and in spermatocytes
(PubMed:19773360). Not expressed in sperm (PubMed:19773360).
{ECO:0000269|PubMed:16701565, ECO:0000269|PubMed:17369820,
ECO:0000269|PubMed:19773360}.
-!- INDUCTION: Induced upon ER stress. Repressed by starvation and
oxidative stress. {ECO:0000269|PubMed:16701565}.
-!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes partial embryonic
lethality (PubMed:15716356, PubMed:18854144). Impairs response to ER
stress (PubMed:18458060). Abnormal accumulation of myosin chaperone
unc-45 in body wall muscles (PubMed:17369820). RNAi-mediated knockdown
in an unc-45 (m94) mutant background, restores motility
(PubMed:17369820). Simultaneous RNAi-mediated knockdown of cdc-48.2 in
embryos causes embryonic lethality (PubMed:15716356, PubMed:16647269,
PubMed:18097415, PubMed:18854144, PubMed:18728180). Defects in oocyte
meiosis I progression (PubMed:17512499). Defects in embryo S phase DNA
replication causing delays in cell cycle progression (PubMed:17512499,
PubMed:18728180, PubMed:21981920, PubMed:26842564, PubMed:28368371). At
the end of mitosis, impairs chromatin decondensation and nuclear
envelope re-assembly (PubMed:18728180, PubMed:18854144,
PubMed:18097415). In addition, abnormal accumulation of air-2 on
mitotic chromatin and impaired air-2 activation (PubMed:18097415). Does
not affect ER transition into sheet-like structures at the onset of
embryonic mitosis (PubMed:15716356). Simultaneous RNAi-mediated
knockdown of cdc-48.2 in young adults decreases lifespan, induces the
unfolded protein response, increases overall levels of
polyubiquitinated proteins, and impairs the degradation of misfolded ER
proteins (PubMed:16647269, PubMed:17825049, PubMed:17369820,
PubMed:21317884, PubMed:22768338). Causes defects in germline
development (PubMed:20977550). In an atx-3 (gk193) mutant background,
causes a 50 percent increase in longevity, a delay in age-related
muscle degeneration and resistance to oxidative and heat stresses
(PubMed:21317884). {ECO:0000269|PubMed:15716356,
ECO:0000269|PubMed:16647269, ECO:0000269|PubMed:17369820,
ECO:0000269|PubMed:17512499, ECO:0000269|PubMed:17825049,
ECO:0000269|PubMed:18097415, ECO:0000269|PubMed:18458060,
ECO:0000269|PubMed:18728180, ECO:0000269|PubMed:18854144,
ECO:0000269|PubMed:20977550, ECO:0000269|PubMed:21317884,
ECO:0000269|PubMed:21981920, ECO:0000269|PubMed:22768338,
ECO:0000269|PubMed:26842564, ECO:0000269|PubMed:28368371}.
-!- SIMILARITY: Belongs to the AAA ATPase family. CDC48 subfamily.
{ECO:0000305}.
-!- CAUTION: The role of cdc-48.1 in the regulation of kinase air-2, a
component of the chromosomal passenger complex (CPC), is controversial.
One study suggests that cdc-48.1 inactivates air-2 at the end of
mitosis whereas a second study shows that cdc-48.1 is not implicated in
the regulation of air-2. {ECO:0000269|PubMed:18097415,
ECO:0000269|PubMed:18854144}.
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EMBL; Z49886; CAA90050.1; -; Genomic_DNA.
PIR; T18970; T18970.
RefSeq; NP_496273.1; NM_063872.4.
SMR; P54811; -.
BioGRID; 39940; 35.
DIP; DIP-26650N; -.
IntAct; P54811; 8.
STRING; 6239.C06A1.1; -.
EPD; P54811; -.
PaxDb; P54811; -.
PeptideAtlas; P54811; -.
EnsemblMetazoa; C06A1.1.1; C06A1.1.1; WBGene00007352.
GeneID; 174624; -.
KEGG; cel:CELE_C06A1.1; -.
UCSC; C06A1.1.1; c. elegans.
CTD; 174624; -.
WormBase; C06A1.1; CE02114; WBGene00007352; cdc-48.1.
eggNOG; KOG0730; Eukaryota.
GeneTree; ENSGT00970000196377; -.
HOGENOM; CLU_000688_12_3_1; -.
InParanoid; P54811; -.
OMA; PIDDTTE; -.
OrthoDB; 194195at2759; -.
PhylomeDB; P54811; -.
PRO; PR:P54811; -.
Proteomes; UP000001940; Chromosome II.
Bgee; WBGene00007352; Expressed in adult organism and 5 other tissues.
GO; GO:0005737; C:cytoplasm; IDA:WormBase.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; IDA:WormBase.
GO; GO:0005634; C:nucleus; IDA:WormBase.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:WormBase.
GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IDA:WormBase.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central.
GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
GO; GO:0097352; P:autophagosome maturation; IBA:GO_Central.
GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:WormBase.
GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IGI:WormBase.
GO; GO:0051228; P:mitotic spindle disassembly; IBA:GO_Central.
GO; GO:0045977; P:positive regulation of mitotic cell cycle, embryonic; IGI:UniProtKB.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:1905634; P:regulation of protein localization to chromatin; IGI:UniProtKB.
GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IBA:GO_Central.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR005938; AAA_ATPase_CDC48.
InterPro; IPR041569; AAA_lid_3.
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; PF17862; AAA_lid_3; 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;
ATP-binding; Chaperone; Cytoplasm; Hydrolase; Nucleotide-binding;
Reference proteome; Repeat.
CHAIN 1..809
/note="Transitional endoplasmic reticulum ATPase homolog 1"
/id="PRO_0000084577"
NP_BIND 253..259
/note="ATP 1"
/evidence="ECO:0000250|UniProtKB:P55072"
NP_BIND 527..532
/note="ATP 2"
/evidence="ECO:0000250|UniProtKB:Q01853"
REGION 1..21
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 779..809
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 803..809
/note="Interaction with ufd-2"
/evidence="ECO:0000269|PubMed:17369820,
ECO:0000269|PubMed:21317884"
COMPBIAS 7..21
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
BINDING 354
/note="ATP 1"
/evidence="ECO:0000250|UniProtKB:P55072"
BINDING 390
/note="ATP 1"
/evidence="ECO:0000250|UniProtKB:P55072"
MUTAGEN 257
/note="K->A: Loss of ATP binding. Complete loss of
catalytic activity. Complete loss of catalytic activity
without affecting oligomerization; when associated with A-
365 and A-530."
/evidence="ECO:0000269|PubMed:18782221,
ECO:0000269|PubMed:21454554"
MUTAGEN 257
/note="K->T: Loss of ATP binding. Complete loss of
catalytic activity."
/evidence="ECO:0000269|PubMed:21454554"
MUTAGEN 311
/note="E->D: Severe loss of ATP hydrolysis without
affecting ATP binding."
/evidence="ECO:0000269|PubMed:21454554"
MUTAGEN 311
/note="E->N,A: Severe loss of ATP hydrolysis without
affecting ATP binding and moderate reduction in
cooperativity between the 2 ATP-binding regions."
/evidence="ECO:0000269|PubMed:21454554"
MUTAGEN 311
/note="E->Q: Severe loss of ATP hydrolysis without
affecting ATP binding and loss of cooperativity between the
2 ATP-binding regions. Slight reduction in catalytic
activity; when associated with A-354, A-365, A-467, S-467
or P-467. Complete loss of catalytic activity; when
associated with Q-584. Restores normal catalytic activity;
when associated with H-471."
/evidence="ECO:0000269|PubMed:21454554"
MUTAGEN 354
/note="N->A: Slight reduction in catalytic activity. Slight
reduction in catalytic activity; when associated with Q-
311. Complete loss of catalytic activity; when associated
with A-631."
/evidence="ECO:0000269|PubMed:21454554"
MUTAGEN 365
/note="R->A: Slight reduction in catalytic activity. Slight
reduction in catalytic activity; when associated with Q-
311. Complete loss of catalytic activity; when associated
with A-257 or A-642. Does not affect oligomerization; when
associated with A-257."
/evidence="ECO:0000269|PubMed:21454554"
MUTAGEN 467
/note="P->A,S: Slight reduction in catalytic activity; when
associated with Q-311."
/evidence="ECO:0000269|PubMed:21454554"
MUTAGEN 471
/note="R->H: Restores normal catalytic activity; when
associated with Q-311."
/evidence="ECO:0000269|PubMed:21454554"
MUTAGEN 530
/note="K->A: Loss of ATP binding and impaired rotation
between the two ATP-binding regions in the hexamer.
Complete loss of catalytic activity. Complete loss of
catalytic activity without affecting oligomerization; when
associated with A-257."
/evidence="ECO:0000269|PubMed:18782221,
ECO:0000269|PubMed:21454554, ECO:0000269|PubMed:24055316"
MUTAGEN 530
/note="K->T: Complete loss of catalytic activity."
/evidence="ECO:0000269|PubMed:21454554"
MUTAGEN 584
/note="E->D: Severe loss of ATP hydrolysis without
affecting ATP binding."
/evidence="ECO:0000269|PubMed:21454554"
MUTAGEN 584
/note="E->Q: Severe loss of ATP hydrolysis without
affecting ATP binding. Does not affect rotation between the
2 ATP-binding regions in the hexamer in presence of ATP or
ADP. Complete loss of catalytic activity; when associated
with Q-311."
/evidence="ECO:0000269|PubMed:21454554,
ECO:0000269|PubMed:24055316"
MUTAGEN 631
/note="N->A: Severe reduction in catalytic activity.
Complete loss of catalytic activity; when associated with
A-354."
/evidence="ECO:0000269|PubMed:21454554"
MUTAGEN 642
/note="R->A: Severe reduction in catalytic activity.
Complete loss of catalytic activity; when associated with
A-365."
/evidence="ECO:0000269|PubMed:21454554"
MUTAGEN 804..809
/note="Missing: Loss of interaction with ufd-2 but not with
atx-3."
/evidence="ECO:0000269|PubMed:17369820,
ECO:0000269|PubMed:21317884"
SEQUENCE 809 AA; 89785 MW; ECF02EF8B939A777 CRC64;
MASVPTHQSE KEKKNDELST AILKDKVKPN RLIVDQSEQD DNSVIAVSQA KMDELGLFRG
DAVILKGKKR KESVAIIVSD ESCPNEKVRM NRVVRNNLRI RLGDVVSITP APNLSYGTRI
HVLPIDDTIE GLTGNLFDVF LKPYFLEAYR PLHKGDIFTV QAAMRTVEFK VVETEPAPAC
IVSPDTMIHY EGDPIKREEE EESMNDIGYD DLGGVRKQLA QIKEMVELPL RHPQLFKAIG
IKPPRGILLF GPPGTGKTLI ARAVANETGS FFFLINGPEV MSKMSGESES NLRKAFEECE
KNQPAILFID EIDAIAPKRE KTNGEVERRI VSQLLTLMDG VKGRSNLVVI AATNRPNSID
GALRRFGRFD REIDIGIPDA VGRLEILRIH TKNMKLADDV DLEQIANECH GFVGADLASL
CSEAALQQIR EKMELIDLED DQIDAEVLNS LAVTMENFRF AQGKSSPSAL REAVVETPNT
TWSDIGGLQN VKRELQELVQ YPVEHPEKYL KFGMQPSRGV LFYGPPGCGK TLLAKAIANE
CQANFISIKG PELLTMWFGE SEANVRDVFD KARAAAPCVL FFDELDSIAK ARGGGAGGDG
GGASDRVINQ VLTEMDGMNA KKNVFIIGAT NRPDIIDPAV LRPGRLDQLI YIPLPDEASR
HQILKASLRK TPLSKDLDLT FLAKNTVGFS GADLTEICQR ACKLAIRESI EKEIRIEKER
QDRQARGEEL MEDDAVDPVP EITRAHFEEA MKFARRSVTD NDIRKYEMFA QTLQQSRGFG
NNFKFPGEQR GSDAPSAPVP AQDDDDLYN


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Related Genes :
[cdc-48.1 C06A1.1] Transitional endoplasmic reticulum ATPase homolog 1 (EC 3.6.4.6) (Cell division cycle-related protein 48.1) (p97/CDC48 homolog 1)
[cdc-48.2 C41C4.8] Transitional endoplasmic reticulum ATPase homolog 2 (EC 3.6.4.6) (Cell division cycle-related protein 48.2) (p97/CDC48 homolog 2)
[CDC48 YDL126C] Cell division control protein 48 (EC 3.6.4.6) (Cell division cycle protein 48) (Transitional endoplasmic reticulum ATPase homolog)
[VCP] Transitional endoplasmic reticulum ATPase (TER ATPase) (EC 3.6.4.6) (15S Mg(2+)-ATPase p97 subunit) (Valosin-containing protein) (VCP)
[vcp] Transitional endoplasmic reticulum ATPase (TER ATPase) (EC 3.6.4.6) (15S Mg(2+)-ATPase p97 subunit) (p97) (Valosin-containing protein) (VCP)
[cdc-48.3 K04G2.3] ATPase family protein 2 homolog (EC 3.6.4.10) (Cell division cycle-related protein 48.3)
[TER94 VCP CG2331] Transitional endoplasmic reticulum ATPase TER94 (EC 3.6.4.6) (Valosin-containing protein homolog)
[vcp] Transitional endoplasmic reticulum ATPase (TER ATPase) (EC 3.6.4.6) (15S Mg(2+)-ATPase p97 subunit) (p97) (Valosin-containing protein) (VCP)
[CDC48A CDC48 At3g09840 F8A24.11] Cell division control protein 48 homolog A (AtCDC48a)
[ORF1ab orf1ab] 2'-O-methyltransferase (EC 2.7.7.48) (EC 3.4.19.12) (EC 3.4.22.69) (EC 3.6.4.12) (EC 3.6.4.13) (3C-like proteinase) (Growth factor-like peptide) (Guanine-N7 methyltransferase) (Helicase) (Host translation inhibitor nsp1) (Leader protein) (NendoU) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (Papain-like proteinase) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (p65 homolog)
[ORF1ab orf1ab] 2'-O-methyltransferase (EC 2.7.7.48) (EC 3.4.19.12) (EC 3.4.22.69) (EC 3.6.4.12) (EC 3.6.4.13) (3C-like proteinase) (Growth factor-like peptide) (Guanine-N7 methyltransferase) (Helicase) (Host translation inhibitor nsp1) (Leader protein) (NendoU) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (Papain-like proteinase) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (p65 homolog)
[Hspa5 Grp78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[Dnajc10 Erdj5 Jpdi] DnaJ homolog subfamily C member 10 (EC 1.8.4.-) (Endoplasmic reticulum DNA J domain-containing protein 5) (ER-resident protein ERdj5) (ERdj5) (Endoplasmic reticulum DnaJ-PDI fusion protein 1) (J domain-containing protein disulfide isomerase-like protein) (J domain-containing PDI-like protein) (JPDI)
[orf1ab ORF1ab] 2'-O-methyltransferase (EC 2.7.7.48) (EC 3.4.19.12) (EC 3.4.22.69) (EC 3.6.4.12) (EC 3.6.4.13) (3C-like proteinase) (Growth factor-like peptide) (Guanine-N7 methyltransferase) (Helicase) (Host translation inhibitor nsp1) (Leader protein) (NendoU) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (Papain-like proteinase) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (p65 homolog)
[Vcpip1 Vcip135] Deubiquitinating protein VCPIP1 (EC 3.4.19.12) (Valosin-containing protein p97/p47 complex-interacting protein 1) (Valosin-containing protein p97/p47 complex-interacting protein p135) (VCP/p47 complex-interacting 135-kDa protein)
[DER1 YBR201W YBR1413] Degradation in the endoplasmic reticulum protein 1
[Vcpip1 Vcip135] Deubiquitinating protein VCPIP1 (EC 3.4.19.12) (Valosin-containing protein p97/p47 complex-interacting protein 1) (Valosin-containing protein p97/p47 complex-interacting protein p135) (VCP/p47 complex-interacting 135-kDa protein)
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Host translation inhibitor nsp1 (Leader protein) (Non-structural protein 1) (nsp1); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.-) (PL2-PRO) (Papain-like protease) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.69) (Main protease) (Mpro) (Non-structural protein 5) (nsp5) (SARS coronavirus main proteinase); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Non-structural protein 12) (nsp12); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Non-structural protein 13) (nsp13); Proofreading exoribonuclease (ExoN) (EC 3.1.13.-) (Guanine-N7 methyltransferase) (Non-structural protein 14) (nsp14); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (Non-structural protein 15) (nsp15); 2'-O-methyltransferase (EC 2.1.1.-) (Non-structural protein 16) (nsp16)]
[yaiE ppnP yaiE_1 yaiE_2 A6581_06820 A6592_08565 A6V01_02400 A8C65_08910 A9819_01890 A9P13_20020 A9R57_08485 A9X72_19070 AC067_13660 AC789_1c03900 ACN002_0406 ACN68_10320 ACN81_25005 ACU57_12035 ACU90_20960 AM270_02350 AM333_11080 AM340_00170 AM375_22275 AM446_21575 AM464_18935 AM465_24670 AMK83_08820 AML35_16935 APT94_15240 APU18_24510 APX88_10995 ARC77_21605 AU473_24575 AUQ13_18550 AUS26_08265 AW059_14025 AWB10_19430 AWE53_023695 AWF06_05110 AWF59_002255 AZZ83_000156 B6V57_02070 B7C53_19905 B9N33_08655 B9T59_05995 BANRA_00817 BANRA_00925 BANRA_02015 BANRA_03594 BB545_15535 BE963_16095 BEN53_04105 BER14_23410 BFD68_18150 BFL24_02350 BHF03_17705 BHS81_02405 BHS87_02130 BIQ87_02175 BIU72_03345 BIZ41_26355 BJJ90_20310 BK248_04610 BK292_14635 BK296_16405 BK373_01320 BK375_26975 BK383_14985 BMA87_04900 BMT91_05310 BN17_01951 BOH76_16090 BON63_11530 BON65_18745 BON66_09075 BON69_11595 BON72_15085 BON75_11450 BON76_23825 BON83_20655 BON86_03800 BON87_15370 BON91_23895 BON92_15465 BON94_14845 BON95_06500 BON96_22295 BON98_18895 BTQ04_02855 BTQ06_17790 BUE81_15520 BvCms12BK_04795 BvCms2454_01767 BvCms28BK_00703 BvCms35BK_00554 BvCmsC61A_02990 BvCmsHHP001_01952 BvCmsHHP019_02594 BvCmsHHP019_02735 BvCmsHHP056_01410 BvCmsKKP036_04281 BvCmsKKP061_04019 BvCmsKSNP073_05624 BvCmsKSNP081_00030 BvCmsKSNP120_04274 BvCmsKSP011_04945 BvCmsKSP024_04930 BvCmsKSP045_04772 BvCmsKSP058_04860 BvCmsKSP067_05191 BvCmsKSP076_04759 BvCmsNSP006_01281 BvCmsNSP007_00849 BvCmsNSP047_03416 BvCmsNSP072_00997 BvCmsOUP014_01108 BvCmsSINP011_02573 BvCmsSINP022_02885 BvCmsSIP019_03625 BvCmsSIP024_01003 BvCmsSIP044_01545 BVL39_00880 BW690_06575 BWI89_12535 BWP17_02145 BXT93_00165 BZL31_10725 BZL69_16805 C2M16_02670 C2U48_08110 C3F40_10585 C4K41_08090 C4M78_16865 C5715_13595 C5F72_20070 C5F73_09375 C5N07_12740 C5P01_16305 C5P44_19530 C6669_02755 C6984_01965 C7235_18880 C7B02_04545 C7B06_13385 C7B07_15195 C7B08_06180 C7B18_00985 C9114_16640 C9160_00550 C9162_12650 C9201_03800 C9306_02820 C9E25_04580 C9E63_22465 C9E67_23765 C9Z03_06575 C9Z23_12315 C9Z28_08265 C9Z37_04640 C9Z68_20485 C9Z70_09610 C9Z78_08360 CA593_01185 CCZ17_04120 CDC27_00860 CDL37_09465 CG692_05055 CI641_017850 CI694_14320 CJU64_02110 CO706_24355 COD30_16055 COD46_04855 CQP61_20925 CR538_19495 CR539_06140 CRD98_01665 CRE06_07890 CRM83_13790 CT144_18010 CT146_15735 CUB99_06570 CV83915_01183 CVH05_20630 CWS33_22875 CY655_02075 D0X26_07420 D1912_23295 D2184_11515 D2185_12065 D2188_07740 D3821_12900 D3822_22465 D3C88_28950 D3O91_15305 D3Y67_14350 D4023_06905 D4M06_05545 D4M76_11590 D4U49_03050 D4V08_07680 D5H35_11765 D6004_10480 D6C57_04065 D6D43_08420 D6T60_09300 D6X76_06760 D7K63_09055 D7K66_05505 D7Y10_05925 D7Z75_05315 D8Y65_05290 D9610_20040 D9C99_17255 D9D20_11505 D9D31_21970 D9D43_14830 D9D94_14580 D9E34_09525 D9E49_06955 D9E73_13115 D9E88_02060 D9F32_03890 D9F87_10325 D9G11_17940 D9G42_13940 D9G48_15840 D9G69_10950 D9G95_10030 D9H53_17415 D9H68_03320 D9H70_06445 D9H94_24405 D9I18_05395 D9I20_07245 D9I87_03310 D9I88_07660 D9I97_02265 D9J03_17400 D9J11_02150 D9J44_05830 D9J52_12125 D9J60_08565 D9J61_02635 D9K02_04260 D9K48_11575 D9K54_20845 D9L89_06360 D9X97_05410 D9Z28_01965 DAH18_14975 DAH23_10455 DAH30_15925 DAH34_21345 DAH37_05240 DD762_07680 DEN86_05080 DEN89_14495 DEO04_04545 DEO20_14385 DIV22_26285 DJ503_01820 DL455_04445 DL473_20145 DL530_07575 DL545_19130 DL637_11475 DL705_16435 DL800_03885 DL979_15710 DLU82_01595 DLX40_16565 DM102_12740 DM129_06110 DM155_09525 DM962_06005 DMZ30_04890 DMZ50_06340 DN627_04525 DN660_05650 DN808_18120 DNC98_06510 DND16_02325 DND79_04070 DNI21_04080 DNQ45_00335 DNR41_17405 DOT59_02705 DOY61_02085 DOY67_05265 DP258_05110 DP277_07535 DQF57_07675 DQO13_05500 DQP61_12090 DRW19_06400 DS143_21555 DS732_06920 DS966_18475 DSZ60_03875 DT034_10500 DTL43_07415 DTL90_10740 DTM10_06080 DTM25_13935 DTM45_10960 DTZ20_03380 DU321_19460 DU333_14985 DW236_15815 DWB25_19225 DXT69_08115 DXT71_02970 DXT73_01860 DXX80_018650 E0I42_07410 E0L04_02150 E0L12_02445 E2115_06350 E2119_01725 E2123_04610 E2127_09375 E2128_04435 E2129_13975 E2134_12225 E2135_01410 E2855_00540 E2863_00426 E4K51_12070 E4K53_09880 E4K55_09545 E4K61_11255 E5P24_15620 E5P28_11315 E5S34_07545 E5S38_06765 E5S43_12135 E5S44_09845 E5S56_05125 E5S58_11035 E5S61_09810 E5S62_19990 E8P32_20890 EA174_09235 EA184_12770 EA191_05310 EA206_10815 EA211_00925 EA213_08335 EA214_19270 EA219_17055 EA225_09190 EA233_12800 EA239_15730 EA250_12110 EA433_19520 EA435_05820 EA834_11650 EAI42_35435 EAI46_25725 EAI46_25840 EAI52_02950 EAM59_14455 EAN77_07940 EAX79_06830 EB510_01625 EB515_09345 EB525_RS00545 EBM08_07705 EBP16_12520 EC1094V2_3464 EC3234A_4c00610 EC382_12595 EC95NR1_04612 ECs0441 ECTO124_03817 ECTO6_03708 ED225_07600 ED600_06320 ED611_06650 ED648_16775 ED903_13725 ED944_09580 EEA45_02855 EEP23_01045 EF082_13590 EF173_10565 EG599_13105 EG808_04255 EGT48_21390 EH412_12630 EHD79_03470 EHH55_15815 EHJ36_08465 EI021_16245 EI032_07550 EI041_08145 EIA21_11810 EIZ93_00830 EJC75_24145 EKI52_09170 EL75_3359 EL79_3454 EL80_3408 ELT17_22260 ELT22_04045 ELT23_00125 ELT31_00280 ELT33_03015 ELT48_00735 ELT49_21480 ELT58_21305 ELU82_03335 ELU85_08960 ELU96_05805 ELV00_13055 ELV08_00785 ELV13_00555 ELV15_22680 ELV22_01630 ELV24_16525 ELV28_08410 ELX56_03900 ELX61_20790 ELX68_02065 ELX69_19550 ELX70_07125 ELX76_05850 ELX79_24270 ELX83_01445 ELX96_14305 ELY05_09885 ELY23_04665 ELY24_07180 ELY32_22740 ELY41_15435 ELY48_07355 ELY50_04295 EO241_13835 EPS70_14865 EPS76_10515 EPS91_09770 EPS94_16700 EPT01_06355 EQ820_00745 EQ823_11615 EQ825_18070 EQ830_03660 EQO00_19840 ERS085362_02676 ERS085366_04179 ERS085379_01215 ERS085386_01096 ERS085404_01742 ERS085406_02227 ERS150873_01858 EST51_18990 ETECE1373_03601 ETECE1441_03612 ETECE1649_03506 ETECE1779_04258 ETECE36_04584 ETECE925_03600 EVY14_00050 EWK56_10245 EXM29_24150 ExPECSC038_04895 ExPECSC065_04439 EXX06_12400 EXX13_09665 EXX23_09965 EXX24_01870 EXX53_07630 EXX55_11875 EXX71_12170 EXX87_11565 EYD11_17450 EYV18_10135 EYX82_01145 EYY27_15550 EYY34_27625 EYY78_10095 F0L67_19465 F1E19_02455 F6T45_22350 F6T51_06360 F6V70_05450 F7F11_06850 F7F23_13355 F7F26_08530 F7F56_11190 F7F79_08660 F7G03_09695 F7G05_12635 F7O57_06490 F9B07_11235 F9X20_010625 F9X20_10705 FAF34_030290 FKC84_04690 FKO60_24460 FNJ67_20330 FNJ69_23475 FORC82_3666 FPI65_02250 FQ021_04720 FQ915_14565 FQU83_20855 FRV13_03860 FTV90_10360 FTV92_11870 FTV93_12360 FV250_14320 FV293_06120 FV295_17245 FV438_20585 FVA71_19985 FWK02_29295 FZC17_02065 FZN26_02330 FZN30_08825 G3565_02860 G4276_18370 G4280_18620 G5606_10990 G5668_11855 G5670_13140 G5680_11755 G5688_07395 G5696_10795 G5697_16390 G5V60_18285 G6Z99_23355 G9448_08700 G9P49_16830 G9P50_16250 GE057_12200 GE087_02515 GE096_15955 GE400_02540 GE558_09695 GFU47_21615 GFY48_03475 GHD50_02110 GIJ01_19765 GIY13_13165 GJ11_02375 GKE29_12130 GKE58_10855 GKE60_09410 GKE79_09230 GKE87_01825 GKF34_16490 GKF52_17565 GKF86_04910 GKF89_04055 GKG12_02940 GNZ02_03615 GNZ05_01665 GP650_16700 GP662_13045 GP666_10645 GP698_13660 GP711_02810 GP720_05730 GP935_14810 GP945_18805 GP946_18990 GP954_12950 GP979_17585 GQE22_09325 GQE33_07115 GQE34_00765 GQE36_18000 GQE42_04900 GQE64_07505 GQE67_02555 GQE87_15550 GQF59_00790 GQM04_16295 GQM06_17115 GQM09_10135 GQM10_05275 GQM13_16755 GQM17_10365 GQM18_17190 GQM28_05335 GQN24_05490 GRC73_12510 GRW02_05020 GRW05_15575 GRW30_07965 GRW57_16360 GRW80_21245 GRW81_04110 GUB08_22335 GUB91_14510 GUB95_14180 GUC01_07480 GUC12_15000 GUC40_07390 GUI16_08025 GUI33_03675 GXC14_20220 H4P50_19265 H4P51_19115 H5C68_16910 H5C80_22515 HAP53_09400 HCR07_11915 HF065_000755 HF523_01165 HF527_18375 HFD31_001236 HFD39_002504 HFD59_003103 HFD69_003066 HFU80_001346 HGR17_22385 HGR87_01460 HGR88_06440 HGS97_11820 HGT58_04135 HH117_07870 HH456_002645 HH707_000108 HH814_000579 HH830_001792 HHA77_001423 HHG54_000763 HHH24_000946 HHH97_002377 HHJ41_01370 HHJ44_22155 HHJ51_05025 HI055_001796 HI083_000480 HIB31_002797 HIF87_003470 HIN76_001080 HIO03_001580 HIO61_000590 HIQ74_001213 HIQ82_002038 HIR91_000876 HIT56_001577 HIZ44_002483 HIZ62_001433 HJ359_001771 HJ411_000554 HJ802_001358 HJI79_003357 HJL93_002730 HJM41_000592 HJM89_001896 HJN45_001169 HJO02_002671 HJO44_000019 HJO53_003212 HJP34_000144 HJQ03_003089 HJR58_002219 HJR60_001095 HJR92_002545 HJS12_001242 HJS53_002270 HJT66_002048 HJT90_002082 HJU54_001570 HJV81_000744 HK427_001468 HKA14_002869 HKA45_002554 HKA57_001676 HKC58_001279 HL152_08835 HL186_02490 HL563_20960 HLI97_000112 HLQ75_07955 HLQ92_12990 HLT96_03035 HLU13_05400 HLU98_04605 HLY53_21035 HLZ85_06695 HmCms169_03669 HmCms184_01874 HmCmsJML074_04353 HmCmsJML079_00649 HmCmsJML146_03132 HmCmsJML204_02343 HMG20_09930 HMG24_12660 HMG27_12270 HMG35_19725 HMP86_22290 HMPREF3040_03387 HMQ05_07470 HMT01_08840 HMT08_08320 HMT08_28135 HMW26_10275 HMW26_27920 HNC38_21355 HNC40_07205 HNC59_10160 HNC73_14325 HNC73_28105 HNC75_03340 HNC80_02630 HNC88_10750 HNC94_01805 HNC99_09055 HND23_10890 HNN86_05540 HNO03_09675 HNO08_21040 HNV44_01815 HNV91_05205 HNX16_02485 HNX34_02410 HNY58_07155 HP431_07725 HPE39_05435 HPE49_20435 HPE52_15660 HPM96_04240 HR075_18950 HS093_08480 HV005_16510 HV021_17015 HV022_17950 HV055_18220 HV065_00215 HV068_18270 HV098_18955 HV108_19500 HV109_18115 HV131_23750 HV149_18435 HV152_17755 HV156_07825 HV159_09785 HV168_09465 HV188_05655 HV226_23340 HV244_16550 HV297_16755 HV303_20415 HV348_18230 HVV37_09655 HVV39_18775 HVV53_22620 HVV73_17755 HVV78_05095 HVV92_19015 HVW09_04615 HVW11_04845 HVW22_00965 HVW33_09625 HVW37_18825 HVW43_10265 HVW44_14930 HVW45_17890 HVW59_08530 HVW60_17400 HVW76_17030 HVW90_08090 HVW93_05045 HVW95_10270 HVW98_04760 HVX00_17970 HVX17_19490 HVX22_17445 HVX24_17055 HVX28_17275 HVX30_05390 HVX33_08680 HVX51_18435 HVX60_09555 HVX73_17865 HVX96_09065 HVY01_17550 HVY77_19945 HVY79_05095 HVY93_17995 HVZ20_05415 HVZ21_18085 HVZ24_17385 HVZ33_18480 HVZ42_18115 HVZ44_17970 HVZ47_04860 HVZ53_18680 HVZ62_09000 HVZ71_18990 HWQ66_23340 HX136_19525 HZT35_11660 IB283_04800 IEM32_07330 IMQ59_17410 JE86ST02C_04160 JE86ST05C_04220 MJ49_04490 MS8345_00396 NCTC10082_01078 NCTC10089_03910 NCTC10418_05682 NCTC10429_03762 NCTC10764_05371 NCTC10767_04209 NCTC10865_04787 NCTC11022_05137 NCTC11126_00022 NCTC11181_01145 NCTC11341_03896 NCTC12950_04180 NCTC13127_05156 NCTC13216_02895 NCTC13846_03688 NCTC7922_06246 NCTC7927_04270 NCTC8009_07014 NCTC8179_01642 NCTC8450_01367 NCTC8500_04283 NCTC8621_03984 NCTC8622_02997 NCTC8959_05017 NCTC8960_01314 NCTC8985_02798 NCTC9001_00537 NCTC9007_00270 NCTC9036_03840 NCTC9044_03501 NCTC9045_04434 NCTC9050_01764 NCTC9055_00703 NCTC9058_03120 NCTC9062_04466 NCTC9075_05103 NCTC9077_04792 NCTC9081_02496 NCTC9111_03977 NCTC9117_04804 NCTC9119_03997 NCTC9434_02812 NCTC9701_04128 NCTC9702_04480 NCTC9703_03222 NCTC9706_01114 NCTC9777_00174 NCTC9969_04032 PGD_02920 PU06_02955 RG28_02910 RG36_04960 RK56_026705 RM34_04980 RX35_02064 SAMEA3472043_02682 SAMEA3472044_00466 SAMEA3472047_02102 SAMEA3472055_02163 SAMEA3472056_03633 SAMEA3472070_02281 SAMEA3472080_01810 SAMEA3472090_01813 SAMEA3472108_01855 SAMEA3472110_00729 SAMEA3472112_02965 SAMEA3472114_01257 SAMEA3472147_04902 SAMEA3484427_03543 SAMEA3484429_01888 SAMEA3484434_01710 SAMEA3485101_03989 SAMEA3751407_02141 SAMEA3752372_02749 SAMEA3752553_00287 SAMEA3752557_00215 SAMEA3752559_02897 SAMEA3752620_00785 SAMEA3753064_01236 SAMEA3753097_00513 SAMEA3753164_00218 SAMEA3753290_01725 SAMEA3753300_00458 SK85_00418 SY51_02060 TUM18780_32860 UC41_24265 UN86_08900 UN91_18725 WP2S18E08_35360 WP4S17E03_35290 WP4S17E08_35200 WP4S18E07_34480 WP4S18E08_34230 WP5S18E09_34520 WP7S17E01_36800 WP7S17E04_33320 WP7S18E09_37190 WQ89_01420 WR15_04360 YDC107_3656] Pyrimidine/purine nucleoside phosphorylase (EC 2.4.2.1) (EC 2.4.2.2) (Adenosine phosphorylase) (Cytidine phosphorylase) (Guanosine phosphorylase) (EC 2.4.2.15) (Inosine phosphorylase) (Thymidine phosphorylase) (EC 2.4.2.4) (Uridine phosphorylase) (EC 2.4.2.3) (Xanthosine phosphorylase)
[Dnajb11] DnaJ homolog subfamily B member 11 (APOBEC1-binding protein 2) (ABBP-2) (ER-associated DNAJ) (ER-associated Hsp40 co-chaperone) (Endoplasmic reticulum DNA J domain-containing protein 3) (ER-resident protein ERdj3) (ERdj3) (ERj3p)
[DNAJB11 EDJ ERJ3 HDJ9 PSEC0121 UNQ537/PRO1080] DnaJ homolog subfamily B member 11 (APOBEC1-binding protein 2) (ABBP-2) (DnaJ protein homolog 9) (ER-associated DNAJ) (ER-associated Hsp40 co-chaperone) (Endoplasmic reticulum DNA J domain-containing protein 3) (ER-resident protein ERdj3) (ERdj3) (ERj3p) (HEDJ) (Human DnaJ protein 9) (hDj-9) (PWP1-interacting protein 4)
[ORF1ab ORF1a orf1ab] 3C-like proteinase (EC 3.4.19.12) (EC 3.4.22.69) (Growth factor-like peptide) (Leader protein) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (Papain-like proteinase) (p65 homolog)
[Nfe2l1 Nrf1] Endoplasmic reticulum membrane sensor NFE2L1 (Locus control region-factor 1) (LCR-F1) (Nuclear factor erythroid 2-related factor 1) (NF-E2-related factor 1) (NFE2-related factor 1) (Nuclear factor, erythroid derived 2, like 1) [Cleaved into: Transcription factor NRF1]
[STH1 NPS1 YIL126W] Nuclear protein STH1/NPS1 (EC 3.6.4.12) (ATP-dependent helicase STH1) (Chromatin structure-remodeling complex protein STH1) (SNF2 homolog)
[Rad9a Rad9] Cell cycle checkpoint control protein RAD9A (mRAD9) (EC 3.1.11.2) (DNA repair exonuclease rad9 homolog A) (Rad9-like protein)
[] Genome polyprotein [Cleaved into: Core protein precursor (Capsid protein C) (p23); Mature core protein (p21); Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); Viroporin p7; Protease NS2 (p23) (EC 3.4.22.-) (Non-structural protein 2) (NS2); Serine protease/helicase NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3 helicase) (NS3 protease) (NS3P) (Viroporin p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56/58); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[Cdk1 Cdc2 Cdc2a Cdkn1] Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase)
[Cdc7 Cdc7l1] Cell division cycle 7-related protein kinase (CDC7-related kinase) (muCdc7) (EC 2.7.11.1)
[ufd-1 F19B6.2] Ubiquitin fusion degradation protein 1 homolog (UB fusion protein 1)
[] Genome polyprotein [Cleaved into: P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); P2; Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); P3; Protein 3AB; Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (EC 3.4.22.28) (Picornain 3C) (P3C); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]

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