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Database: UniProt
Entry: P25694
LinkDB: P25694
Original site: P25694 
ID   CDC48_YEAST             Reviewed;         835 AA.
AC   P25694; D6VRM4;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 3.
DT   29-SEP-2021, entry version 212.
DE   RecName: Full=Cell division control protein 48 {ECO:0000305|PubMed:6749598};
DE            EC=3.6.4.6 {ECO:0000269|PubMed:21454554};
DE   AltName: Full=Cell division cycle protein 48 {ECO:0000303|PubMed:6749598};
DE   AltName: Full=Transitional endoplasmic reticulum ATPase homolog {ECO:0000305};
GN   Name=CDC48 {ECO:0000303|PubMed:6749598};
GN   OrderedLocusNames=YDL126C {ECO:0000312|SGD:S000002284};
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1860879; DOI=10.1083/jcb.114.3.443;
RA   Froehlich K.-U., Fries H.W., Ruediger M., Erdmann R., Botstein D.,
RA   Mecke D.;
RT   "Yeast cell cycle protein CDC48p shows full-length homology to the
RT   mammalian protein VCP and is a member of a protein family involved in
RT   secretion, peroxisome formation, and gene expression.";
RL   J. Cell Biol. 114:443-453(1991).
RN   [2]
RP   SEQUENCE REVISION.
RA   Froehlich K.-U.;
RL   Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   GENE NAME.
RX   PubMed=6749598;
RA   Moir D., Stewart S.E., Osmond B.C., Botstein D.;
RT   "Cold-sensitive cell-division-cycle mutants of yeast: isolation,
RT   properties, and pseudoreversion studies.";
RL   Genetics 100:547-563(1982).
RN   [6]
RP   FUNCTION, INTERACTION WITH NPL4, AND SUBCELLULAR LOCATION.
RX   PubMed=11733065; DOI=10.1016/s0092-8674(01)00595-5;
RA   Rape M., Hoppe T., Gorr I., Kalocay M., Richly H., Jentsch S.;
RT   "Mobilization of processed, membrane-tethered SPT23 transcription factor by
RT   CDC48(UFD1/NPL4), a ubiquitin-selective chaperone.";
RL   Cell 107:667-677(2001).
RN   [7]
RP   INTERACTION WITH NPL4.
RX   PubMed=11598205; DOI=10.1091/mbc.12.10.3226;
RA   Hitchcock A.L., Krebber H., Frietze S., Lin A., Latterich M., Silver P.A.;
RT   "The conserved npl4 protein complex mediates proteasome-dependent membrane-
RT   bound transcription factor activation.";
RL   Mol. Biol. Cell 12:3226-3241(2001).
RN   [8]
RP   FUNCTION.
RX   PubMed=11813000; DOI=10.1038/ncb746;
RA   Jarosch E., Taxis C., Volkwein C., Bordallo J., Finley D., Wolf D.H.,
RA   Sommer T.;
RT   "Protein dislocation from the ER requires polyubiquitination and the AAA-
RT   ATPase Cdc48.";
RL   Nat. Cell Biol. 4:134-139(2002).
RN   [9]
RP   FUNCTION.
RX   PubMed=11740563; DOI=10.1038/414652a;
RA   Ye Y., Meyer H.H., Rapoport T.A.;
RT   "The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER
RT   into the cytosol.";
RL   Nature 414:652-656(2001).
RN   [10]
RP   FUNCTION.
RX   PubMed=11847109; DOI=10.1093/emboj/21.4.615;
RA   Braun S., Matuschewski K., Rape M., Thoms S., Jentsch S.;
RT   "Role of the ubiquitin-selective CDC48(UFD1/NPL4) chaperone (segregase) in
RT   ERAD of OLE1 and other substrates.";
RL   EMBO J. 21:615-621(2002).
RN   [11]
RP   FUNCTION, AND INTERACTION WITH ASE1 AND CDC5.
RX   PubMed=14636562; DOI=10.1016/s0092-8674(03)00815-8;
RA   Cao K., Nakajima R., Meyer H.H., Zheng Y.;
RT   "The AAA-ATPase Cdc48/p97 regulates spindle disassembly at the end of
RT   mitosis.";
RL   Cell 115:355-367(2003).
RN   [12]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [13]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-594 AND LYS-673, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=SUB592;
RX   PubMed=12872131; DOI=10.1038/nbt849;
RA   Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA   Roelofs J., Finley D., Gygi S.P.;
RT   "A proteomics approach to understanding protein ubiquitination.";
RL   Nat. Biotechnol. 21:921-926(2003).
RN   [14]
RP   INTERACTION WITH UBX PROTEINS.
RX   PubMed=15258615; DOI=10.1038/sj.embor.7400203;
RA   Schuberth C., Richly H., Rumpf S., Buchberger A.;
RT   "Shp1 and Ubx2 are adaptors of Cdc48 involved in ubiquitin-dependent
RT   protein degradation.";
RL   EMBO Rep. 5:818-824(2004).
RN   [15]
RP   IDENTIFICATION IN CDC48-NPL4-UFD1 ATPASE COMPLEX, AND INTERACTION WITH HRD1
RP   COMPLEX.
RX   PubMed=16873066; DOI=10.1016/j.cell.2006.05.043;
RA   Carvalho P., Goder V., Rapoport T.A.;
RT   "Distinct ubiquitin-ligase complexes define convergent pathways for the
RT   degradation of ER proteins.";
RL   Cell 126:361-373(2006).
RN   [16]
RP   IDENTIFICATION IN A COMPLEX WITH NPL4; UFD1; SHP1 AND UFD2, IDENTIFICATION
RP   IN A COMPLEX WITH NPL4; UFD1; SHP1; DOA1 AND OTU1, AND INTERACTION WITH
RP   OTU1; UFD2 AND DOA1.
RX   PubMed=16427015; DOI=10.1016/j.molcel.2005.12.014;
RA   Rumpf S., Jentsch S.;
RT   "Functional division of substrate processing cofactors of the ubiquitin-
RT   selective Cdc48 chaperone.";
RL   Mol. Cell 21:261-269(2006).
RN   [17]
RP   FUNCTION, AND INTERACTION WITH DOA1.
RX   PubMed=16428438; DOI=10.1128/mcb.26.3.822-830.2006;
RA   Mullally J.E., Chernova T., Wilkinson K.D.;
RT   "Doa1 is a Cdc48 adapter that possesses a novel ubiquitin binding domain.";
RL   Mol. Cell. Biol. 26:822-830(2006).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519 AND SER-770, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-770, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472 AND THR-735, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [21]
RP   INTERACTION WITH DOA1.
RX   PubMed=19805280; DOI=10.1073/pnas.0908321106;
RA   Zhao G., Li G., Schindelin H., Lennarz W.J.;
RT   "An Armadillo motif in Ufd3 interacts with Cdc48 and is involved in
RT   ubiquitin homeostasis and protein degradation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:16197-16202(2009).
RN   [22]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519 AND THR-735, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [23]
RP   FUNCTION, IDENTIFICATION IN A COMPLEX WITH UBP3; BRE5 AND DOA1, AND
RP   INTERACTION WITH UBP3 AND DOA1.
RX   PubMed=20508643; DOI=10.1038/embor.2010.74;
RA   Ossareh-Nazari B., Bonizec M., Cohen M., Dokudovskaya S., Delalande F.,
RA   Schaeffer C., Van Dorsselaer A., Dargemont C.;
RT   "Cdc48 and Ufd3, new partners of the ubiquitin protease Ubp3, are required
RT   for ribophagy.";
RL   EMBO Rep. 11:548-554(2010).
RN   [24]
RP   FUNCTION, AND INTERACTION WITH VMS1.
RX   PubMed=21070972; DOI=10.1016/j.molcel.2010.10.021;
RA   Heo J.M., Livnat-Levanon N., Taylor E.B., Jones K.T., Dephoure N., Ring J.,
RA   Xie J., Brodsky J.L., Madeo F., Gygi S.P., Ashrafi K., Glickman M.H.,
RA   Rutter J.;
RT   "A stress-responsive system for mitochondrial protein degradation.";
RL   Mol. Cell 40:465-480(2010).
RN   [25]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH VMS1.
RX   PubMed=21148305; DOI=10.1074/jbc.m110.179259;
RA   Tran J.R., Tomsic L.R., Brodsky J.L.;
RT   "A Cdc48p-associated factor modulates endoplasmic reticulum-associated
RT   degradation, cell stress, and ubiquitinated protein homeostasis.";
RL   J. Biol. Chem. 286:5744-5755(2011).
RN   [26]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-261; GLU-315; ASN-358;
RP   ARG-369; PRO-471; ARG-475; LYS-534; GLU-588 AND ARG-645.
RX   PubMed=21454554; DOI=10.1074/jbc.m110.201400;
RA   Nishikori S., Esaki M., Yamanaka K., Sugimoto S., Ogura T.;
RT   "Positive cooperativity of the p97 AAA ATPase is critical for essential
RT   functions.";
RL   J. Biol. Chem. 286:15815-15820(2011).
RN   [27]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=23178123; DOI=10.1016/j.cell.2012.10.044;
RA   Brandman O., Stewart-Ornstein J., Wong D., Larson A., Williams C.C.,
RA   Li G.W., Zhou S., King D., Shen P.S., Weibezahn J., Dunn J.G., Rouskin S.,
RA   Inada T., Frost A., Weissman J.S.;
RT   "A ribosome-bound quality control complex triggers degradation of nascent
RT   peptides and signals translation stress.";
RL   Cell 151:1042-1054(2012).
RN   [28]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [29]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-305; LYS-322; LYS-346; LYS-522
RP   AND LYS-539, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=22106047; DOI=10.1002/pmic.201100166;
RA   Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT   "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL   Proteomics 12:236-240(2012).
RN   [30]
RP   SUBUNIT.
RX   PubMed=23479637; DOI=10.1073/pnas.1221724110;
RA   Defenouillere Q., Yao Y., Mouaikel J., Namane A., Galopier A., Decourty L.,
RA   Doyen A., Malabat C., Saveanu C., Jacquier A., Fromont-Racine M.;
RT   "Cdc48-associated complex bound to 60S particles is required for the
RT   clearance of aberrant translation products.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:5046-5051(2013).
RN   [31]
RP   FUNCTION.
RX   PubMed=24261871; DOI=10.1111/gtc.12106;
RA   Matsuda R., Ikeuchi K., Nomura S., Inada T.;
RT   "Protein quality control systems associated with no-go and nonstop mRNA
RT   surveillance in yeast.";
RL   Genes Cells 19:1-12(2014).
RN   [32]
RP   FUNCTION, AND INTERACTION WITH DOA1.
RX   PubMed=27044889; DOI=10.1083/jcb.201510098;
RA   Wu X., Li L., Jiang H.;
RT   "Doa1 targets ubiquitinated substrates for mitochondria-associated
RT   degradation.";
RL   J. Cell Biol. 213:49-63(2016).
RN   [33]
RP   FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=29355480; DOI=10.7554/elife.33116;
RA   Yang X., Arines F.M., Zhang W., Li M.;
RT   "Sorting of a multi-subunit ubiquitin ligase complex in the endolysosome
RT   system.";
RL   Elife 7:0-0(2018).
RN   [34]
RP   FUNCTION.
RX   PubMed=31445887; DOI=10.1016/j.molcel.2019.07.006;
RA   Matsumoto S., Nakatsukasa K., Kakuta C., Tamura Y., Esaki M., Endo T.;
RT   "Msp1 clears mistargeted proteins by facilitating their transfer from
RT   mitochondria to the ER.";
RL   Mol. Cell 76:191-205(2019).
RN   [35] {ECO:0007744|PDB:6OA9, ECO:0007744|PDB:6OAA, ECO:0007744|PDB:6OAB}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.70 ANGSTROMS) IN COMPLEX WITH UFD1/NPL4
RP   AND POLYUBIQUITINATED SUBSTRATE, AND FUNCTION.
RX   PubMed=31249135; DOI=10.1126/science.aax1033;
RA   Twomey E.C., Ji Z., Wales T.E., Bodnar N.O., Ficarro S.B., Marto J.A.,
RA   Engen J.R., Rapoport T.A.;
RT   "Substrate processing by the Cdc48 ATPase complex is initiated by ubiquitin
RT   unfolding.";
RL   Science 365:0-0(2019).
RN   [36] {ECO:0007744|PDB:6OMB, ECO:0007744|PDB:6OPC}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.70 ANGSTROMS) IN COMPLEX WITH ADAPTER
RP   SHP1 AND POLYUBIQUITINATED SUBSTRATE, AND FUNCTION.
RX   PubMed=31249134; DOI=10.1126/science.aax0486;
RA   Cooney I., Han H., Stewart M.G., Carson R.H., Hansen D.T., Iwasa J.H.,
RA   Price J.C., Hill C.P., Shen P.S.;
RT   "Structure of the Cdc48 segregase in the act of unfolding an authentic
RT   substrate.";
RL   Science 365:502-505(2019).
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:21454554, PubMed:31445887). By recruiting
CC       and promoting the degradation of ubiquitinated proteins, plays a role
CC       in the ubiquitin fusion degradation (UFD) pathway (PubMed:16428438).
CC       Has a role in the endoplasmic reticulum-associated degradation (ERAD)
CC       pathway which mediates the cytoplasmic elimination of misfolded
CC       proteins exported from the ER (PubMed:11813000, PubMed:11740563,
CC       PubMed:11847109, PubMed:21148305). Required for the proteasome-
CC       dependent processing/activation of MGA2 and SPT23 transcription factors
CC       leading to the subsequent expression of OLE1 (PubMed:11847109,
CC       PubMed:11733065). Has an additional role in the turnover of OLE1 where
CC       it targets ubiquitinated OLE1 and other proteins to the ERAD
CC       (PubMed:11847109). Regulates ubiquitin-mediated mitochondria protein
CC       degradation (PubMed:21070972, PubMed:27044889). Involved in spindle
CC       disassembly probably by promoting the degradation of spindle assembly
CC       factors ASE1 and CDC5 at the end of mitosis (PubMed:14636562).
CC       Component of the ribosome quality control complex (RQC), a ribosome-
CC       associated complex that mediates ubiquitination and extraction of
CC       incompletely synthesized nascent chains for proteasomal degradation
CC       (PubMed:23178123, PubMed:24261871). CDC48 may provide the mechanical
CC       force that dislodges the polyubiquitinated nascent peptides from the
CC       exit channel (PubMed:23178123, PubMed:24261871). Required for
CC       ribophagy, a process which relocalizes ribosomal particles into the
CC       vacuole for degradation in response to starvation (PubMed:20508643).
CC       Component of the DSC E3 ubiquitin ligase complexes that tag proteins
CC       present in Golgi, endosome and vacuole membranes and function in
CC       protein homeostasis under non-stress conditions and support a role in
CC       protein quality control (PubMed:29355480). Substrate initially binds
CC       through the attached polyubiquitin chain to UDF1/NPL4 and then moves
CC       through the pore of the ATPase rings and is thereby unfolded
CC       (PubMed:31249135, PubMed:31249134). Acts on a broad range of even well-
CC       folded proteins via ubiquitin-binding and unfolding to initiate
CC       substrate processing (PubMed:31249135). Involved in degradation of
CC       mislocalized tail-anchored transmembrane proteins extracted from the
CC       mitochondrion outer membrane by MSP1 and ubiquitinated by DOA10
CC       (PubMed:31445887). {ECO:0000269|PubMed:11733065,
CC       ECO:0000269|PubMed:11740563, ECO:0000269|PubMed:11813000,
CC       ECO:0000269|PubMed:11847109, ECO:0000269|PubMed:14636562,
CC       ECO:0000269|PubMed:16428438, ECO:0000269|PubMed:20508643,
CC       ECO:0000269|PubMed:21070972, ECO:0000269|PubMed:21148305,
CC       ECO:0000269|PubMed:21454554, ECO:0000269|PubMed:23178123,
CC       ECO:0000269|PubMed:24261871, ECO:0000269|PubMed:27044889,
CC       ECO:0000269|PubMed:29355480, ECO:0000269|PubMed:31249134,
CC       ECO:0000269|PubMed:31249135, ECO:0000269|PubMed:31445887}.
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:21454554};
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 (PubMed:21454554). 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). {ECO:0000250|UniProtKB:P54811,
CC       ECO:0000269|PubMed:21454554}.
CC   -!- SUBUNIT: Component of the heterotrimeric CDC48-NPL4-UFD1 ATPase complex
CC       (PubMed:16873066). The CDC48-NPL4-UFD1 ATPase complex interacts with
CC       the HRD1 ubiquitin ligase complex composed of the E3 ligase HRD1, its
CC       cofactors HRD3, USA1 and DER1, substrate recruiting factor YOS9 and
CC       CDC48-binding protein UBX2 (PubMed:16873066). Interaction between the
CC       complexes is mediated by interaction between CDC48-NPL4-UFD1 complex
CC       member CDC48 and HRD1 complex member UBX2 (PubMed:16873066). Forms a
CC       complex composed of CDC48, NPL4, UFD1, UFD2 and SHP1 (PubMed:16427015).
CC       Forms a complex composed of CDC48, NPL4, UFD1, DOA1, SHP1 and
CC       deubiquitinase OTU1; within the complex interacts with DOA1/UFD3 and
CC       OTU1 to prevent multiubiquitination of substrates (PubMed:16427015).
CC       Interacts with UFD2, to add further ubiquitin moieties; the interaction
CC       with UFD2 is prevented by DOA1/UFD3 (PubMed:16427015). Forms a complex
CC       composed of CDC48, DOA1, deubiquitinase UBP3 and probably BRE5; within
CC       the complex interacts with DOA1 and UBP3 (PubMed:20508643). Interacts
CC       (via C-terminus) with DOA1 (via PUL domain); the interaction is direct
CC       (PubMed:16428438, PubMed:19805280, PubMed:27044889). Interacts with
CC       NPL4 (PubMed:11733065, PubMed:11598205, PubMed:31249134). Interacts
CC       with SHP1/UBX1, UBX2, UBX3, UBX4, UBX5, UBX6 and UBX7 (PubMed:15258615,
CC       PubMed:31249134). Interacts with VMS1; the interaction recruits CDC48
CC       to the mitochondria in response to mitochondrial stress
CC       (PubMed:21070972, PubMed:21148305). Component of the ribosome quality
CC       control complex (RQC), composed of the E3 ubiquitin ligase RKR1/LTN1,
CC       RQC1 and RQC2, as well as CDC48 and its ubiquitin-binding cofactors
CC       (PubMed:23178123, PubMed:23479637). RQC forms a stable complex with 60S
CC       ribosomal subunits (PubMed:23178123, PubMed:23479637). Interacts with
CC       ASE1 and CDC5; the interaction is likely to result in their degradation
CC       (PubMed:14636562). Component of the DSCc E3 ligase complexes composed
CC       of at least TUL1, DSC2, DSC3, UBX3, CDC48 as well as VLD1 for the
CC       vacuole-localized complex or GLD1 for the Golgi/endosome-localized
CC       complex (PubMed:29355480). {ECO:0000269|PubMed:11598205,
CC       ECO:0000269|PubMed:11733065, ECO:0000269|PubMed:14636562,
CC       ECO:0000269|PubMed:15258615, ECO:0000269|PubMed:16427015,
CC       ECO:0000269|PubMed:16428438, ECO:0000269|PubMed:16873066,
CC       ECO:0000269|PubMed:19805280, ECO:0000269|PubMed:20508643,
CC       ECO:0000269|PubMed:21070972, ECO:0000269|PubMed:21148305,
CC       ECO:0000269|PubMed:23178123, ECO:0000269|PubMed:23479637,
CC       ECO:0000269|PubMed:27044889, ECO:0000269|PubMed:29355480,
CC       ECO:0000269|PubMed:31249134}.
CC   -!- INTERACTION:
CC       P25694; P53741: BRE5; NbExp=4; IntAct=EBI-4308, EBI-28528;
CC       P25694; P25694: CDC48; NbExp=2; IntAct=EBI-4308, EBI-4308;
CC       P25694; P38307: DER1; NbExp=5; IntAct=EBI-4308, EBI-5761;
CC       P25694; P36037: DOA1; NbExp=6; IntAct=EBI-4308, EBI-6017;
CC       P25694; Q08109: HRD1; NbExp=8; IntAct=EBI-4308, EBI-37613;
CC       P25694; Q05787: HRD3; NbExp=6; IntAct=EBI-4308, EBI-31647;
CC       P25694; P33755: NPL4; NbExp=11; IntAct=EBI-4308, EBI-12193;
CC       P25694; P32628: RAD23; NbExp=2; IntAct=EBI-4308, EBI-14668;
CC       P25694; P06778: RAD52; NbExp=4; IntAct=EBI-4308, EBI-14719;
CC       P25694; P34223: SHP1; NbExp=10; IntAct=EBI-4308, EBI-17093;
CC       P25694; Q12306: SMT3; NbExp=3; IntAct=EBI-4308, EBI-17490;
CC       P25694; P40318: SSM4; NbExp=4; IntAct=EBI-4308, EBI-18208;
CC       P25694; Q01477: UBP3; NbExp=4; IntAct=EBI-4308, EBI-19834;
CC       P25694; Q04228: UBX2; NbExp=15; IntAct=EBI-4308, EBI-27730;
CC       P25694; Q12229: UBX3; NbExp=3; IntAct=EBI-4308, EBI-35335;
CC       P25694; P54730: UBX4; NbExp=5; IntAct=EBI-4308, EBI-28127;
CC       P25694; Q06682: UBX5; NbExp=4; IntAct=EBI-4308, EBI-32041;
CC       P25694; P47049: UBX6; NbExp=3; IntAct=EBI-4308, EBI-25866;
CC       P25694; P38349: UBX7; NbExp=4; IntAct=EBI-4308, EBI-21157;
CC       P25694; P53044: UFD1; NbExp=13; IntAct=EBI-4308, EBI-19997;
CC       P25694; P54860: UFD2; NbExp=6; IntAct=EBI-4308, EBI-20003;
CC       P25694; Q04311: VMS1; NbExp=5; IntAct=EBI-4308, EBI-784329;
CC   -!- SUBCELLULAR LOCATION: Microsome {ECO:0000269|PubMed:11733065}.
CC       Endoplasmic reticulum {ECO:0000269|PubMed:21148305}. Cytoplasm
CC       {ECO:0000269|PubMed:21148305}. Note=Bound loosely to components of the
CC       microsomal fraction. {ECO:0000269|PubMed:11733065}.
CC   -!- MISCELLANEOUS: Present with 78400 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR   EMBL; X56956; CAA40276.1; -; Genomic_DNA.
DR   EMBL; Z74174; CAA98694.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11734.1; -; Genomic_DNA.
DR   PIR; S67669; S67669.
DR   RefSeq; NP_010157.1; NM_001180185.1.
DR   PDB; 6OA9; EM; 3.90 A; A/B/C/D/E/F=1-835.
DR   PDB; 6OAA; EM; 4.10 A; B/C/D/E=1-835.
DR   PDB; 6OAB; EM; 3.60 A; A/B/C/D/E=1-835.
DR   PDB; 6OMB; EM; 3.70 A; A/B/C/D/E=1-835.
DR   PDB; 6OPC; EM; 3.70 A; A/B/C/D/E/F=1-835.
DR   PDBsum; 6OA9; -.
DR   PDBsum; 6OAA; -.
DR   PDBsum; 6OAB; -.
DR   PDBsum; 6OMB; -.
DR   PDBsum; 6OPC; -.
DR   SMR; P25694; -.
DR   BioGRID; 31937; 898.
DR   ComplexPortal; CPX-1323; CDC48-CDC23-UFD2 complex.
DR   ComplexPortal; CPX-2946; CDC48-NPL4-UFD1 AAA ATPase complex.
DR   ComplexPortal; CPX-3069; CDC48-NPL4-VMS1 AAA ATPase complex.
DR   ComplexPortal; CPX-3265; Ribosome quality control complex.
DR   DIP; DIP-2704N; -.
DR   IntAct; P25694; 166.
DR   MINT; P25694; -.
DR   STRING; 4932.YDL126C; -.
DR   TCDB; 3.A.16.1.2; the endoplasmic reticular retrotranslocon (er-rt) family.
DR   CarbonylDB; P25694; -.
DR   iPTMnet; P25694; -.
DR   MaxQB; P25694; -.
DR   PaxDb; P25694; -.
DR   PRIDE; P25694; -.
DR   EnsemblFungi; YDL126C_mRNA; YDL126C; YDL126C.
DR   GeneID; 851431; -.
DR   KEGG; sce:YDL126C; -.
DR   SGD; S000002284; CDC48.
DR   VEuPathDB; FungiDB:YDL126C; -.
DR   eggNOG; KOG0730; Eukaryota.
DR   GeneTree; ENSGT00940000165417; -.
DR   HOGENOM; CLU_000688_12_2_1; -.
DR   InParanoid; P25694; -.
DR   OMA; ATECQAN; -.
DR   Reactome; R-SCE-110320; Translesion Synthesis by POLH.
DR   Reactome; R-SCE-3371511; HSF1 activation.
DR   Reactome; R-SCE-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR   Reactome; R-SCE-5358346; Hedgehog ligand biogenesis.
DR   Reactome; R-SCE-5689896; Ovarian tumor domain proteases.
DR   Reactome; R-SCE-6798695; Neutrophil degranulation.
DR   Reactome; R-SCE-8876725; Protein methylation.
DR   PRO; PR:P25694; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P25694; protein.
DR   GO; GO:0036266; C:Cdc48p-Npl4p-Vms1p AAA ATPase complex; IDA:SGD.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0000837; C:Doa10p ubiquitin ligase complex; IDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR   GO; GO:0000839; C:Hrd1p ubiquitin ligase ERAD-L complex; IDA:SGD.
DR   GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0030894; C:replisome; IDA:SGD.
DR   GO; GO:1990112; C:RQC complex; IDA:SGD.
DR   GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140603; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0016887; F:ATPase; IDA:SGD.
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:0019888; F:protein phosphatase regulator activity; IMP:SGD.
DR   GO; GO:0043130; F:ubiquitin binding; IDA:SGD.
DR   GO; GO:0046034; P:ATP metabolic process; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0097352; P:autophagosome maturation; IBA:GO_Central.
DR   GO; GO:0043624; P:cellular protein complex disassembly; IMP:SGD.
DR   GO; GO:0071629; P:cytoplasm protein quality control by the ubiquitin-proteasome system; IMP:SGD.
DR   GO; GO:0006274; P:DNA replication termination; IDA:SGD.
DR   GO; GO:0016320; P:endoplasmic reticulum membrane fusion; IMP:SGD.
DR   GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IMP:SGD.
DR   GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR   GO; GO:0072671; P:mitochondria-associated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR   GO; GO:0051228; P:mitotic spindle disassembly; IMP:SGD.
DR   GO; GO:0051974; P:negative regulation of telomerase activity; IMP:SGD.
DR   GO; GO:0070651; P:nonfunctional rRNA decay; IMP:SGD.
DR   GO; GO:0071630; P:nuclear protein quality control by the ubiquitin-proteasome system; IMP:SGD.
DR   GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IMP:SGD.
DR   GO; GO:2001168; P:positive regulation of histone H2B ubiquitination; IMP:SGD.
DR   GO; GO:0010636; P:positive regulation of mitochondrial fusion; IMP:SGD.
DR   GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:SGD.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:SGD.
DR   GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:SGD.
DR   GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IDA:SGD.
DR   GO; GO:0034517; P:ribophagy; IMP:SGD.
DR   GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IMP:SGD.
DR   GO; GO:1990171; P:SCF complex disassembly in response to cadmium stress; IMP:SGD.
DR   GO; GO:0031134; P:sister chromatid biorientation; IMP:SGD.
DR   GO; GO:0120174; P:stress-induced homeostatically regulated protein degradation pathway; IMP:SGD.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:SGD.
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   3D-structure; ATP-binding; Cell cycle; Chaperone; Cytoplasm;
KW   Endoplasmic reticulum; Hydrolase; Isopeptide bond; Microsome;
KW   Nucleotide-binding; Phosphoprotein; Protein transport; Reference proteome;
KW   Repeat; Transport; Ubl conjugation.
FT   CHAIN           1..835
FT                   /note="Cell division control protein 48"
FT                   /id="PRO_0000084587"
FT   NP_BIND         257..263
FT                   /note="ATP 1"
FT                   /evidence="ECO:0000250|UniProtKB:P55072"
FT   NP_BIND         531..536
FT                   /note="ATP 2"
FT                   /evidence="ECO:0000250|UniProtKB:Q01853"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          720..746
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          792..835
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        792..820
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         358
FT                   /note="ATP 1"
FT                   /evidence="ECO:0000250|UniProtKB:P55072"
FT   BINDING         394
FT                   /note="ATP 1"
FT                   /evidence="ECO:0000250|UniProtKB:P55072"
FT   MOD_RES         472
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         519
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         735
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         770
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358,
FT                   ECO:0007744|PubMed:17330950"
FT   CROSSLNK        305
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CROSSLNK        322
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CROSSLNK        346
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CROSSLNK        522
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CROSSLNK        539
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CROSSLNK        594
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:12872131"
FT   CROSSLNK        673
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:12872131"
FT   MUTAGEN         261
FT                   /note="K->A: Moderate reduction in growth rate."
FT                   /evidence="ECO:0000269|PubMed:21454554"
FT   MUTAGEN         261
FT                   /note="K->T: Probable loss of ATP binding. Complete loss of
FT                   catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:21454554"
FT   MUTAGEN         315
FT                   /note="E->A: Moderate reduction in growth rate."
FT                   /evidence="ECO:0000269|PubMed:21454554"
FT   MUTAGEN         315
FT                   /note="E->D: Severe loss of catalytic activity without
FT                   affecting cooperativity between the 2 ATP-binding regions.
FT                   Slight reduction in growth rate."
FT                   /evidence="ECO:0000269|PubMed:21454554"
FT   MUTAGEN         315
FT                   /note="E->N: Severe reduction in growth rate."
FT                   /evidence="ECO:0000269|PubMed:21454554"
FT   MUTAGEN         315
FT                   /note="E->Q: Severe loss of catalytic activity and
FT                   cooperativity between the 2 ATP-binding regions. Lethal.
FT                   Restores cell growth; when associated with A-358; A-369; S-
FT                   471; A-471 or H-475."
FT                   /evidence="ECO:0000269|PubMed:21454554"
FT   MUTAGEN         358
FT                   /note="N->A: Slight reduction in growth rate. Restores cell
FT                   growth; when associated with Q-315."
FT                   /evidence="ECO:0000269|PubMed:21454554"
FT   MUTAGEN         369
FT                   /note="R->A: No effect on growth rate. Restores cell
FT                   growth; when associated with Q-315."
FT                   /evidence="ECO:0000269|PubMed:21454554"
FT   MUTAGEN         471
FT                   /note="P->A,S: Restores cell growth; when associated with
FT                   Q-315."
FT                   /evidence="ECO:0000269|PubMed:21454554"
FT   MUTAGEN         475
FT                   /note="R->H: Restores cell growth; when associated with Q-
FT                   315."
FT                   /evidence="ECO:0000269|PubMed:21454554"
FT   MUTAGEN         534
FT                   /note="K->A,T: Severe loss of catalytic activity. Lethal."
FT                   /evidence="ECO:0000269|PubMed:21454554"
FT   MUTAGEN         588
FT                   /note="E->D: Moderate reduction in growth rate."
FT                   /evidence="ECO:0000269|PubMed:21454554"
FT   MUTAGEN         588
FT                   /note="E->Q: Lethal."
FT                   /evidence="ECO:0000269|PubMed:21454554"
FT   MUTAGEN         645
FT                   /note="R->A: Lethal."
FT                   /evidence="ECO:0000269|PubMed:21454554"
SQ   SEQUENCE   835 AA;  91996 MW;  02ADDB9A227614D8 CRC64;
     MGEEHKPLLD ASGVDPREED KTATAILRRK KKDNMLLVDD AINDDNSVIA INSNTMDKLE
     LFRGDTVLVK GKKRKDTVLI VLIDDELEDG ACRINRVVRN NLRIRLGDLV TIHPCPDIKY
     ATRISVLPIA DTIEGITGNL FDVFLKPYFV EAYRPVRKGD HFVVRGGMRQ VEFKVVDVEP
     EEYAVVAQDT IIHWEGEPIN REDEENNMNE VGYDDIGGCR KQMAQIREMV ELPLRHPQLF
     KAIGIKPPRG VLMYGPPGTG KTLMARAVAN ETGAFFFLIN GPEVMSKMAG ESESNLRKAF
     EEAEKNAPAI IFIDEIDSIA PKRDKTNGEV ERRVVSQLLT LMDGMKARSN VVVIAATNRP
     NSIDPALRRF GRFDREVDIG IPDATGRLEV LRIHTKNMKL ADDVDLEALA AETHGYVGAD
     IASLCSEAAM QQIREKMDLI DLDEDEIDAE VLDSLGVTMD NFRFALGNSN PSALRETVVE
     SVNVTWDDVG GLDEIKEELK ETVEYPVLHP DQYTKFGLSP SKGVLFYGPP GTGKTLLAKA
     VATEVSANFI SVKGPELLSM WYGESESNIR DIFDKARAAA PTVVFLDELD SIAKARGGSL
     GDAGGASDRV VNQLLTEMDG MNAKKNVFVI GATNRPDQID PAILRPGRLD QLIYVPLPDE
     NARLSILNAQ LRKTPLEPGL ELTAIAKATQ GFSGADLLYI VQRAAKYAIK DSIEAHRQHE
     AEKEVKVEGE DVEMTDEGAK AEQEPEVDPV PYITKEHFAE AMKTAKRSVS DAELRRYEAY
     SQQMKASRGQ FSNFNFNDAP LGTTATDNAN SNNSAPSGAG AAFGSNAEED DDLYS
//
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