POC4_YEAST
ID POC4_YEAST Reviewed; 148 AA.
AC Q12245; D6W3M5; Q6Q5F7;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Proteasome chaperone 4;
GN Name=POC4; Synonyms=DMP1; OrderedLocusNames=YPL144W;
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].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8948103;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1483::aid-yea34>3.0.co;2-o;
RA Purnelle B., Coster F., Goffeau A.;
RT "The sequence of 55 kb on the left arm of yeast chromosome XVI identifies a
RT small nuclear RNA, a new putative protein kinase and two new putative
RT regulators.";
RL Yeast 12:1483-1492(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
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 [7]
RP FUNCTION.
RX PubMed=15161972; DOI=10.1073/pnas.0401263101;
RA Askree S.H., Yehuda T., Smolikov S., Gurevich R., Hawk J., Coker C.,
RA Krauskopf A., Kupiec M., McEachern M.J.;
RT "A genome-wide screen for Saccharomyces cerevisiae deletion mutants that
RT affect telomere length.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8658-8663(2004).
RN [8]
RP GENE NAME, FUNCTION, INTERACTION WITH IRC25, AND SUBUNIT.
RX PubMed=17707236; DOI=10.1016/j.molcel.2007.06.025;
RA Le Tallec B., Barrault M.-B., Courbeyrette R., Guerois R.,
RA Marsolier-Kergoat M.-C., Peyroche A.;
RT "20S proteasome assembly is orchestrated by two distinct pairs of
RT chaperones in yeast and in mammals.";
RL Mol. Cell 27:660-674(2007).
RN [9]
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 [10]
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) IN COMPLEX WITH IRC25 AND PUP2, AND
RP FUNCTION.
RX PubMed=18278057; DOI=10.1038/nsmb.1386;
RA Yashiroda H., Mizushima T., Okamoto K., Kameyama T., Hayashi H.,
RA Kishimoto T., Niwa S., Kasahara M., Kurimoto E., Sakata E., Takagi K.,
RA Suzuki A., Hirano Y., Murata S., Kato K., Yamane T., Tanaka K.;
RT "Crystal structure of a chaperone complex that contributes to the assembly
RT of yeast 20S proteasomes.";
RL Nat. Struct. Mol. Biol. 15:228-236(2008).
CC -!- FUNCTION: Involved in 20S proteasome assembly, facilitating the alpha-
CC ring formation. Involved in maintenance of telomere length.
CC {ECO:0000269|PubMed:15161972, ECO:0000269|PubMed:17707236,
CC ECO:0000269|PubMed:18278057}.
CC -!- SUBUNIT: Component of the 20S proteasome chaperone. Forms a heterodimer
CC with IRC25 that binds to proteasome precursors. Interacts with POP2.
CC {ECO:0000269|PubMed:17707236, ECO:0000269|PubMed:18278057}.
CC -!- INTERACTION:
CC Q12245; Q07951: IRC25; NbExp=12; IntAct=EBI-2343020, EBI-31959;
CC Q12245; P40302: PRE5; NbExp=2; IntAct=EBI-2343020, EBI-13955;
CC Q12245; P32379: PUP2; NbExp=2; IntAct=EBI-2343020, EBI-13971;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2210 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PSMG4 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X96770; CAA65549.1; -; Genomic_DNA.
DR EMBL; U43703; AAB68232.1; -; Genomic_DNA.
DR EMBL; Z73500; CAA97848.1; -; Genomic_DNA.
DR EMBL; AY558135; AAS56461.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11291.1; -; Genomic_DNA.
DR PIR; S65155; S65155.
DR RefSeq; NP_015181.1; NM_001183958.1.
DR PDB; 2Z5B; X-ray; 1.96 A; A=1-148.
DR PDB; 2Z5C; X-ray; 2.90 A; A/D=1-148.
DR PDBsum; 2Z5B; -.
DR PDBsum; 2Z5C; -.
DR AlphaFoldDB; Q12245; -.
DR SMR; Q12245; -.
DR BioGRID; 36039; 333.
DR DIP; DIP-8930N; -.
DR IntAct; Q12245; 11.
DR MINT; Q12245; -.
DR STRING; 4932.YPL144W; -.
DR MaxQB; Q12245; -.
DR PaxDb; Q12245; -.
DR PRIDE; Q12245; -.
DR EnsemblFungi; YPL144W_mRNA; YPL144W; YPL144W.
DR GeneID; 855959; -.
DR KEGG; sce:YPL144W; -.
DR SGD; S000006065; POC4.
DR VEuPathDB; FungiDB:YPL144W; -.
DR eggNOG; ENOG502S7JE; Eukaryota.
DR HOGENOM; CLU_133955_0_0_1; -.
DR InParanoid; Q12245; -.
DR OMA; HMATIIS; -.
DR BioCyc; YEAST:G3O-34041-MON; -.
DR EvolutionaryTrace; Q12245; -.
DR PRO; PR:Q12245; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12245; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IMP:SGD.
DR GO; GO:0043248; P:proteasome assembly; IMP:SGD.
DR InterPro; IPR018854; Psome_chaperone_3/4.
DR Pfam; PF10448; POC3_POC4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Reference proteome.
FT CHAIN 1..148
FT /note="Proteasome chaperone 4"
FT /id="PRO_0000238635"
FT CONFLICT 9
FT /note="T -> P (in Ref. 4; AAS56461)"
FT /evidence="ECO:0000305"
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:2Z5B"
FT STRAND 21..30
FT /evidence="ECO:0007829|PDB:2Z5B"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:2Z5B"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:2Z5B"
FT STRAND 55..65
FT /evidence="ECO:0007829|PDB:2Z5B"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:2Z5B"
FT HELIX 91..108
FT /evidence="ECO:0007829|PDB:2Z5B"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:2Z5B"
FT HELIX 125..129
FT /evidence="ECO:0007829|PDB:2Z5B"
FT HELIX 131..146
FT /evidence="ECO:0007829|PDB:2Z5B"
SQ SEQUENCE 148 AA; 16573 MW; 1CC7C6074CF4AC08 CRC64;
MLVKTISRTI ESESGFLQPT LDVIATLPAD DRSKKIPISL VVGFKQEASL NSSSSLSCYY
YAIPLMRDRH INLKSGGSNV VGIPLLDTKD DRIRDMARHM ATIISERFNR PCYVTWSSLP
SEDPSMLVAN HLYILKKCLD LLKTELGE