POC2_YEAST
ID POC2_YEAST Reviewed; 267 AA.
AC P36040; D6VWZ7;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Proteasome assembly chaperone 2;
DE AltName: Full=Alpha-1-proteinase inhibitor-degradation deficient protein 66;
DE AltName: Full=Proteasome biogenesis-associated protein 2;
GN Name=ADD66; Synonyms=PBA2, POC2; OrderedLocusNames=YKL206C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [2]
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 [3]
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 [4]
RP PROTEIN SEQUENCE OF 40-76; 79-86; 179-187 AND 243-259, GENE NAME,
RP INTERACTION WITH PBA1, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17431397; DOI=10.1038/sj.emboj.7601681;
RA Li X., Kusmierczyk A.R., Wong P., Emili A., Hochstrasser M.;
RT "Beta-subunit appendages promote 20S proteasome assembly by overcoming an
RT Ump1-dependent checkpoint.";
RL EMBO J. 26:2339-2349(2007).
RN [5]
RP GENE NAME, FUNCTION, AND DELETION MUTANT.
RX PubMed=12711700; DOI=10.1242/jcs.00439;
RA Palmer E.A., Kruse K.B., Fewell S.W., Buchanan S.M., Brodsky J.L.,
RA McCracken A.A.;
RT "Differential requirements of novel A1PiZ degradation deficient (ADD) genes
RT in ER-associated protein degradation.";
RL J. Cell Sci. 116:2361-2373(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, AND SUBCELLULAR LOCATION.
RX PubMed=17634286; DOI=10.1091/mbc.e07-01-0034;
RA Scott C.M., Kruse K.B., Schmidt B.Z., Perlmutter D.H., McCracken A.A.,
RA Brodsky J.L.;
RT "ADD66, a gene involved in the endoplasmic reticulum-associated degradation
RT of alpha-1-antitrypsin-Z in yeast, facilitates proteasome activity and
RT assembly.";
RL Mol. Biol. Cell 18:3776-3787(2007).
RN [8]
RP GENE NAME, FUNCTION, INTERACTION WITH PBA1, 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).
CC -!- FUNCTION: Involved in 20S proteasome assembly. Required for maximal
CC proteasome activity. Affects the chymotrypsin-like activity of the
CC proteasome. Can be degraded by the proteasome. Involved in the
CC endoplasmic reticulum-associated degradation (ERAD).
CC {ECO:0000269|PubMed:12711700, ECO:0000269|PubMed:17634286,
CC ECO:0000269|PubMed:17707236}.
CC -!- SUBUNIT: Component of the 20S proteasome chaperone. Forms a heterodimer
CC with PBA1 that binds to proteasome precursors.
CC {ECO:0000269|PubMed:17431397, ECO:0000269|PubMed:17707236}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17634286}.
CC -!- MISCELLANEOUS: Present with 2940 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: Deletion induces the unfolded protein response (UPR).
CC -!- SIMILARITY: Belongs to the PSMG2 family. {ECO:0000305}.
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DR EMBL; Z28206; CAA82051.1; -; Genomic_DNA.
DR EMBL; AY558394; AAS56720.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA08963.1; -; Genomic_DNA.
DR PIR; S38044; S38044.
DR RefSeq; NP_012716.1; NM_001179771.1.
DR PDB; 4G4S; X-ray; 2.49 A; P=1-267.
DR PDB; 7LS6; EM; 3.17 A; P=1-267.
DR PDB; 7LSX; EM; 3.61 A; P=1-267.
DR PDBsum; 4G4S; -.
DR PDBsum; 7LS6; -.
DR PDBsum; 7LSX; -.
DR AlphaFoldDB; P36040; -.
DR SMR; P36040; -.
DR BioGRID; 33917; 176.
DR DIP; DIP-6515N; -.
DR IntAct; P36040; 3.
DR MINT; P36040; -.
DR STRING; 4932.YKL206C; -.
DR iPTMnet; P36040; -.
DR MaxQB; P36040; -.
DR PaxDb; P36040; -.
DR PRIDE; P36040; -.
DR EnsemblFungi; YKL206C_mRNA; YKL206C; YKL206C.
DR GeneID; 853629; -.
DR KEGG; sce:YKL206C; -.
DR SGD; S000001689; ADD66.
DR VEuPathDB; FungiDB:YKL206C; -.
DR eggNOG; KOG3112; Eukaryota.
DR GeneTree; ENSGT00390000018415; -.
DR HOGENOM; CLU_062640_2_1_1; -.
DR InParanoid; P36040; -.
DR OMA; HPFVGPL; -.
DR BioCyc; YEAST:G3O-31965-MON; -.
DR PRO; PR:P36040; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36040; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043248; P:proteasome assembly; IMP:SGD.
DR Gene3D; 3.40.50.10900; -; 2.
DR InterPro; IPR019151; Proteasome_assmbl_chaperone_2.
DR InterPro; IPR016562; Proteasome_assmbl_chp_2_euk.
DR InterPro; IPR038389; PSMG2_sf.
DR PANTHER; PTHR12970; PTHR12970; 1.
DR Pfam; PF09754; PAC2; 1.
DR PIRSF; PIRSF010044; UCP010044; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Direct protein sequencing;
KW Reference proteome.
FT CHAIN 1..267
FT /note="Proteasome assembly chaperone 2"
FT /id="PRO_0000203132"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:4G4S"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:4G4S"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:4G4S"
FT STRAND 28..35
FT /evidence="ECO:0007829|PDB:4G4S"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:7LS6"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:7LS6"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:4G4S"
FT STRAND 67..75
FT /evidence="ECO:0007829|PDB:4G4S"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:4G4S"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:4G4S"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:4G4S"
FT HELIX 95..108
FT /evidence="ECO:0007829|PDB:4G4S"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:4G4S"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:4G4S"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:7LS6"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:7LS6"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:7LS6"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:7LS6"
FT TURN 148..151
FT /evidence="ECO:0007829|PDB:7LS6"
FT HELIX 152..158
FT /evidence="ECO:0007829|PDB:7LS6"
FT STRAND 172..179
FT /evidence="ECO:0007829|PDB:7LS6"
FT HELIX 183..188
FT /evidence="ECO:0007829|PDB:4G4S"
FT STRAND 204..212
FT /evidence="ECO:0007829|PDB:7LS6"
FT HELIX 220..228
FT /evidence="ECO:0007829|PDB:4G4S"
FT HELIX 247..251
FT /evidence="ECO:0007829|PDB:4G4S"
FT HELIX 258..266
FT /evidence="ECO:0007829|PDB:4G4S"
SQ SEQUENCE 267 AA; 30739 MW; D635C3EBC2E37C11 CRC64;
MSCLVLPLVS VGNIPQLSID WLLNSQANEW EYLEALDSKY LVEFVGPLDR PEDGSDSLYK
DADMKYSSAL EVFYNKKRGL FAIQQRTPLV SVNYLNNFIV EIILPFLSKY NISEICIWDS
LYAMEDENGV IVRPQEVYSL GEFYFDDEAE LLSNLHLNDQ ESMVNNWLHF TPTSFQDKIS
VDQPIFKILF QILNASQRPK ALRSIKYCSC LANEGDNSLD SQQFLQWIIS QKVIKNAPPI
VKFVRPISWQ GAYGMADARD KFVDLYN
