ID   PRS4_YEAST              Reviewed;         437 AA.
AC   P40327;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 83.
DE   RecName: Full=26S protease regulatory subunit 4 homolog;
DE   AltName: Full=TAT-binding homolog 5;
GN   Name=RPT2; Synonyms=YHS4, YTA5; OrderedLocusNames=YDL007W;
GN   ORFNames=D2920;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   MEDLINE=95274317; PubMed=7754704; DOI=10.1002/yea.320100903;
RA   Schnall R., Mannhaupt G., Stucka R., Tauer R., Ehnle S.,
RA   Schwarzlose C., Vetter I., Feldmann H.;
RT   "Identification of a set of yeast genes coding for a novel family of
RT   putative ATPases with high similarity to constituents of the 26S
RT   protease complex.";
RL   Yeast 10:1141-1155(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF LYS-229.
RC   STRAIN=ATCC 200060 / W303;
RX   MEDLINE=95238424; PubMed=7721833; DOI=10.1074/jbc.270.16.9178;
RA   Lucero H.A., Chojnicki E.W.T., Mandiyan S., Nelson H., Nelson N.;
RT   "Cloning and expression of a yeast gene encoding a protein with ATPase
RT   activity and high identity to the subunit 4 of the human 26 S
RT   protease.";
RL   J. Biol. Chem. 270:9178-9184(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   MEDLINE=97313263; 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.,
RA   Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
RA   Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
RA   Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
RA   Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
RA   Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
RA   Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
RA   Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
RA   Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
RA   Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
RA   Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
RA   Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
RA   Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
RA   Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
RA   Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
RA   Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
RA   Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
RA   Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
RA   Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
RA   Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
RA   Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
RA   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   PROTEIN SEQUENCE OF 2-11, AND MYRISTOYLATION AT GLY-2.
RX   PubMed=12504901; DOI=10.1016/S0003-9861(02)00639-2;
RA   Kimura Y., Saeki Y., Yokosawa H., Polevoda B., Sherman F., Hirano H.;
RT   "N-terminal modifications of the 19S regulatory particle subunits of
RT   the yeast proteasome.";
RL   Arch. Biochem. Biophys. 409:341-348(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180, AND MASS
RP   SPECTROMETRY.
RX   PubMed=17563356; DOI=10.1073/pnas.0701622104;
RA   Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
RT   "Proteome-wide identification of in vivo targets of DNA damage
RT   checkpoint kinases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176; THR-178; SER-180;
RP   TYR-181; SER-182; SER-356 AND THR-357, AND MASS SPECTROMETRY.
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
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: The 26S protease is involved in the ATP-dependent
CC       degradation of ubiquitinated proteins. The regulatory (or ATPase)
CC       complex confers ATP dependency and substrate specificity to the
CC       26S complex (By similarity). Has ATPase activity.
CC   -!- INTERACTION:
CC       P16603:NCP1; NbExp=1; IntAct=EBI-13901, EBI-11940;
CC       P38764:RPN1; NbExp=1; IntAct=EBI-13901, EBI-15913;
CC       P33299:RPT1; NbExp=1; IntAct=EBI-13901, EBI-13910;
CC       P33297:RPT5; NbExp=1; IntAct=EBI-13901, EBI-13920;
CC       Q01939:RPT6; NbExp=1; IntAct=EBI-13901, EBI-13914;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). Nucleus (Potential).
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
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DR   EMBL; X81070; CAA56957.1; -; Genomic_DNA.
DR   EMBL; L17040; AAA97498.1; -; Genomic_DNA.
DR   EMBL; Z48432; CAA88352.1; -; Genomic_DNA.
DR   EMBL; Z74055; CAA98563.1; -; Genomic_DNA.
DR   PIR; S46613; S46613.
DR   RefSeq; NP_010277.1; -.
DR   HSSP; P43773; 1G3I.
DR   DIP; DIP:6282N; -.
DR   IntAct; P40327; 30.
DR   PeptideAtlas; P40327; -.
DR   PRIDE; P40327; -.
DR   Ensembl; YDL007W; Saccharomyces cerevisiae.
DR   GeneID; 851557; -.
DR   GenomeReviews; Z71256_GR; YDL007W.
DR   KEGG; sce:YDL007W; -.
DR   NMPDR; fig|4932.3.peg.1019; -.
DR   CYGD; YDL007w; -.
DR   SGD; S000002165; RPT2.
DR   HOGENOM; P40327; -.
DR   OMA; P40327; PKYEPPV.
DR   NextBio; 968983; -.
DR   GermOnline; YDL007W; Saccharomyces cerevisiae.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0008540; C:proteasome regulatory particle, base subcom...; IPI:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IDA:SGD.
DR   GO; GO:0004175; F:endopeptidase activity; TAS:SGD.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:SGD.
DR   InterPro; IPR005937; 26S_Psome_P45.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   Pfam; PF00004; AAA; 1.
DR   SMART; SM00382; AAA; 1.
DR   TIGRFAMs; TIGR01242; 26Sp45; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Lipoprotein; Myristate; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Proteasome.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    437       26S protease regulatory subunit 4
FT                                homolog.
FT                                /FTId=PRO_0000084685.
FT   NP_BIND     223    230       ATP (Potential).
FT   MOD_RES     176    176       Phosphoserine.
FT   MOD_RES     178    178       Phosphothreonine.
FT   MOD_RES     180    180       Phosphoserine.
FT   MOD_RES     181    181       Phosphotyrosine.
FT   MOD_RES     182    182       Phosphoserine.
FT   MOD_RES     356    356       Phosphoserine.
FT   MOD_RES     357    357       Phosphothreonine.
FT   LIPID         2      2       N-myristoyl glycine.
FT   MUTAGEN     229    229       K->Q: 73% loss of ATPase activity.
FT   CONFLICT    347    347       K -> N (in Ref. 2; AAA97498).
SQ   SEQUENCE   437 AA;  48828 MW;  EB735354C3A0EBD4 CRC64;
     MGQGVSSGQD KKKKKGSNQK PKYEPPVQSK FGRKKRKGGP ATAEKLPNIY PSTRCKLKLL
     RMERIKDHLL LEEEFVSNSE ILKPFEKKQE EEKKQLEEIR GNPLSIGTLE EIIDDDHAIV
     TSPTMPDYYV SILSFVDKEL LEPGCSVLLH HKTMSIVGVL QDDADPMVSV MKMDKSPTES
     YSDIGGLESQ IQEIKESVEL PLTHPELYEE MGIKPPKGVI LYGAPGTGKT LLAKAVANQT
     SATFLRIVGS ELIQKYLGDG PRLCRQIFKV AGENAPSIVF IDEIDAIGTK RYDSNSGGER
     EIQRTMLELL NQLDGFDDRG DVKVIMATNK IETLDPALIR PGRIDRKILF ENPDLSTKKK
     ILGIHTSKMN LSEDVNLETL VTTKDDLSGA DIQAMCTEAG LLALRERRMQ VTAEDFKQAK
     ERVMKNKVEE NLEGLYL
//