CDC48_SCHPO
ID CDC48_SCHPO Reviewed; 815 AA.
AC Q9P3A7; O14221;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Cell division cycle protein 48 {ECO:0000250|UniProtKB:P25694};
DE EC=3.6.4.6 {ECO:0000250|UniProtKB:P25694};
DE AltName: Full=Transitional endoplasmic reticulum ATPase homolog {ECO:0000305};
GN Name=cdc48 {ECO:0000250|UniProtKB:P25694};
GN ORFNames=SPAC1565.08 {ECO:0000312|PomBase:SPAC1565.08}, SPAC6F12.01;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP INTERACTION WITH UBX2 AND UBX3.
RX PubMed=15120077; DOI=10.1016/j.cub.2004.04.029;
RA Hartmann-Petersen R., Wallace M., Hofmann K., Koch G., Johnsen A.H.,
RA Hendil K.B., Gordon C.;
RT "The Ubx2 and Ubx3 cofactors direct Cdc48 activity to proteolytic and
RT nonproteolytic ubiquitin-dependent processes.";
RL Curr. Biol. 14:824-828(2004).
RN [3]
RP INTERACTION WITH LUB1.
RX PubMed=14993272; DOI=10.1128/mcb.24.6.2324-2331.2004;
RA Ogiso Y., Sugiura R., Kamo T., Yanagiya S., Lu Y., Okazaki K., Shuntoh H.,
RA Kuno T.;
RT "Lub1 participates in ubiquitin homeostasis and stress response via
RT maintenance of cellular ubiquitin contents in fission yeast.";
RL Mol. Cell. Biol. 24:2324-2331(2004).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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. By recruiting and promoting the degradation of
CC ubiquitinated proteins, plays a role in the ubiquitin fusion
CC degradation (UFD) pathway. Has a role in the endoplasmic reticulum-
CC associated degradation (ERAD) pathway which mediates the cytoplasmic
CC elimination of misfolded proteins exported from the ER. Involved in
CC spindle disassembly. Component of the ribosome quality control complex
CC (RQC), a ribosome-associated complex that mediates ubiquitination and
CC extraction of incompletely synthesized nascent chains for proteasomal
CC degradation. CDC48 may provide the mechanical force that dislodges the
CC polyubiquitinated nascent peptides from the exit channel. Required for
CC ribophagy, a process which relocalizes ribosomal particles into the
CC vacuole for degradation in response to starvation.
CC {ECO:0000250|UniProtKB:P25694}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.6;
CC Evidence={ECO:0000250|UniProtKB:P25694};
CC -!- ACTIVITY REGULATION: The first ATP-binding region has low ATPase
CC activity. The second ATP-binding region is responsible for ATPase
CC activity. ATP binding to the first ATP-binding region induces intrinsic
CC activity of the second ATP-binding region. While ATP binding to the
CC first ATP-binding region appears to prevent ATP hydrolysis by the
CC second ATP-binding region, ADP-binding to first region promotes the
CC coordinate and cooperative ATPase cycle of the second ATP-binding
CC region. 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.
CC {ECO:0000250|UniProtKB:P54811}.
CC -!- SUBUNIT: Component of the ribosome quality control complex (RQC),
CC composed of the E3 ubiquitin ligase rkr1/ltn1, rqc1 and mtr1/rqc2, as
CC well as cdc48 and its ubiquitin-binding cofactors. RQC forms a stable
CC complex with 60S ribosomal subunits (By similarity). Interacts with
CC ubx2 and ubx3 (PubMed:15120077). Interacts with lub1 (PubMed:14993272).
CC {ECO:0000250|UniProtKB:P25694, ECO:0000269|PubMed:14993272,
CC ECO:0000269|PubMed:15120077}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; CU329670; CAB99275.1; -; Genomic_DNA.
DR RefSeq; NP_593287.2; NM_001018717.2.
DR AlphaFoldDB; Q9P3A7; -.
DR SMR; Q9P3A7; -.
DR BioGRID; 279194; 75.
DR IntAct; Q9P3A7; 3.
DR STRING; 4896.SPAC1565.08.1; -.
DR iPTMnet; Q9P3A7; -.
DR MaxQB; Q9P3A7; -.
DR PaxDb; Q9P3A7; -.
DR PRIDE; Q9P3A7; -.
DR EnsemblFungi; SPAC1565.08.1; SPAC1565.08.1:pep; SPAC1565.08.
DR GeneID; 2542744; -.
DR KEGG; spo:SPAC1565.08; -.
DR PomBase; SPAC1565.08; cdc48.
DR VEuPathDB; FungiDB:SPAC1565.08; -.
DR eggNOG; KOG0730; Eukaryota.
DR HOGENOM; CLU_000688_12_2_1; -.
DR InParanoid; Q9P3A7; -.
DR OMA; HACHDIK; -.
DR PhylomeDB; Q9P3A7; -.
DR Reactome; R-SPO-110320; Translesion Synthesis by POLH.
DR Reactome; R-SPO-3371511; HSF1 activation.
DR Reactome; R-SPO-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-SPO-5689896; Ovarian tumor domain proteases.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-8876725; Protein methylation.
DR Reactome; R-SPO-8951664; Neddylation.
DR Reactome; R-SPO-9755511; KEAP1-NFE2L2 pathway.
DR PRO; PR:Q9P3A7; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0036266; C:Cdc48p-Npl4p-Vms1p AAA ATPase complex; ISO:PomBase.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000836; C:Hrd1p ubiquitin ligase complex; ISO:PomBase.
DR GO; GO:1990023; C:mitotic spindle midzone; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:1990112; C:RQC complex; ISO:PomBase.
DR GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISM:PomBase.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; EXP:PomBase.
DR GO; GO:0097352; P:autophagosome maturation; IBA:GO_Central.
DR GO; GO:0061163; P:endoplasmic reticulum polarization; IMP:PomBase.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IBA:GO_Central.
DR GO; GO:0051306; P:mitotic sister chromatid separation; IMP:PomBase.
DR GO; GO:0051228; P:mitotic spindle disassembly; IMP:PomBase.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IBA:GO_Central.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; ISO:PomBase.
DR GO; GO:0032933; P:SREBP signaling pathway; IMP:PomBase.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:PomBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IGI:PomBase.
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 Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 2.
DR Pfam; PF02933; CDC48_2; 1.
DR Pfam; PF02359; CDC48_N; 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; Cell cycle; Chaperone; Cytoplasm; Hydrolase;
KW Nucleotide-binding; Nucleus; Protein transport; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1..815
FT /note="Cell division cycle protein 48"
FT /id="PRO_0000084586"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 267..273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT BINDING 368
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT BINDING 404
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P55072"
FT BINDING 541..546
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q01853"
SQ SEQUENCE 815 AA; 90125 MW; 4F4DB89C81DEE532 CRC64;
MNAPSTMTDK KPEVEHLQGE NPPKDTYSAE DTATAILRKK RKPNSLVVDD ATNDDNSVIT
LSSNTMETLQ LFRGDTVVVK GKRRKDTVLI VLTDEEMEDG VARINRVVRN NLRVRLGDIV
TINPCPDIKY AERISVLPLA DTVEGLTGSL FDVYLKPYFV EAYRPIRKGD LFVVRGSMRQ
VEFKVVDVAP DEFGIVSQDT IIHWEGEPIN REDEESSLAE VGYDDIGGCR RQMAQIRELV
ELPLRHPQLF KSIGIKPPRG ILMYGPPGTG KTLMARAVAN ETGAFFFLIN GPEIMSKMAG
ESESNLRKAF EEAEKNSPAI IFIDEIDSIA PKREKTNGEV ERRVVSQLLT LMDGMKARSN
VVVMAATNRP NSIDPALRRF GRFDREVDVG IPDPTGRLEI LRIHTKNMKL ADDVDLEQIA
AETHGYVGSD LASLCSEAAM QQIREKMDMI DLDEDEIDAE VLDSLGVTMD NFRFALGSSN
PSALRETVVE VPNVRWEDIG GLEEVKRELR ETVQMPVMYA EKFLRFGVTP SKGVLFFGPP
GTGKTLLAKA IANECSANFI SVKGPELLSM WFGESESNVR DIFDKARAAA PCVVFLDELD
SIAKARGASA GDSGGGDRVV NQLLTEMDGV NSKKNVFVIG ATNRPDQIDP ALMRPGRLDQ
LIYVPLPDEE ARFSILQTQL RHTPVAEDVD LRAVAKATHG FSGADLEFVV QRAVKLAIKD
SIEEDIKREN ETGEAPADDV VMDEDASVSQ VQRHHVEEAM KMARRSVSDA EVRRYEAYAH
QLLTSRGLTG FQFDSADSNT NGPSFGNDGA DDLYA
