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   27-MAR-2024, entry version 167.
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).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH RBD2.
RX   PubMed=27655872; DOI=10.15252/embj.201693923;
RA   Hwang J., Ribbens D., Raychaudhuri S., Cairns L., Gu H., Frost A.,
RA   Urban S., Espenshade P.J.;
RT   "A Golgi rhomboid protease Rbd2 recruits Cdc48 to cleave yeast SREBP.";
RL   EMBO J. 35:2332-2349(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. 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. Has a role in
CC       substrate recognition mediating rbd2-dependent cleavage of sterol
CC       regulatory element-binding protein sre1 and sre2 (PubMed:27655872).
CC       {ECO:0000250|UniProtKB:P25694, ECO:0000269|PubMed:27655872}.
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       Interacts with rbd2 (via C-terminal SHP box); the interaction is
CC       required for rbd2-mediated cleavage of sre1 and sre2 (PubMed:27655872).
CC       {ECO:0000250|UniProtKB:P25694, ECO:0000269|PubMed:14993272,
CC       ECO:0000269|PubMed:15120077, ECO:0000269|PubMed:27655872}.
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; 77.
DR   IntAct; Q9P3A7; 3.
DR   STRING; 284812.Q9P3A7; -.
DR   iPTMnet; Q9P3A7; -.
DR   MaxQB; Q9P3A7; -.
DR   PaxDb; 4896-SPAC1565-08-1; -.
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-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:0032473; C:cytoplasmic side of mitochondrial outer membrane; IC: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; IBA:GO_Central.
DR   GO; GO:0140545; F:ATP-dependent protein disaggregase activity; TAS: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:0071712; P:ER-associated misfolded protein catabolic process; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IGI:PomBase.
DR   CDD; cd19519; RecA-like_CDC48_r1-like; 1.
DR   CDD; cd19528; RecA-like_CDC48_r2-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.10.330.10; -; 1.
DR   Gene3D; 6.10.20.150; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR01243; CDC48; 1.
DR   PANTHER; PTHR23077; AAA-FAMILY ATPASE; 1.
DR   PANTHER; PTHR23077:SF171; ATPASE FAMILY PROTEIN 2 HOMOLOG; 1.
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; ADC-like; 1.
DR   SUPFAM; SSF54585; Cdc48 domain 2-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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
//