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POC3_YEAST
ID   POC3_YEAST              Reviewed;         179 AA.
AC   Q07951; D6VY23;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Proteasome chaperone 3;
DE   AltName: Full=Increased recombination centers protein 25;
GN   Name=IRC25; Synonyms=DMP2, POC3; OrderedLocusNames=YLR021W;
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=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
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   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   [5]
RP   GENE NAME, FUNCTION, INTERACTION WITH POC4, 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   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) IN COMPLEX WITH POC4 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. {ECO:0000269|PubMed:17707236,
CC       ECO:0000269|PubMed:18278057}.
CC   -!- SUBUNIT: Component of the 20S proteasome chaperone. Forms a heterodimer
CC       with POC4 that binds to proteasome precursors. Interacts with POP2.
CC       {ECO:0000269|PubMed:17707236, ECO:0000269|PubMed:18278057}.
CC   -!- INTERACTION:
CC       Q07951; Q12245: POC4; NbExp=12; IntAct=EBI-31959, EBI-2343020;
CC   -!- MISCELLANEOUS: Present with 1820 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the PSMG3 family. {ECO:0000305}.
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DR   EMBL; Z73193; CAA97544.1; -; Genomic_DNA.
DR   EMBL; AY558201; AAS56527.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09339.1; -; Genomic_DNA.
DR   PIR; S64843; S64843.
DR   RefSeq; NP_013121.1; NM_001181908.1.
DR   PDB; 2Z5B; X-ray; 1.96 A; B=1-179.
DR   PDB; 2Z5C; X-ray; 2.90 A; B/E=1-179.
DR   PDBsum; 2Z5B; -.
DR   PDBsum; 2Z5C; -.
DR   AlphaFoldDB; Q07951; -.
DR   SMR; Q07951; -.
DR   BioGRID; 31295; 273.
DR   DIP; DIP-4747N; -.
DR   IntAct; Q07951; 4.
DR   MINT; Q07951; -.
DR   STRING; 4932.YLR021W; -.
DR   MaxQB; Q07951; -.
DR   PaxDb; Q07951; -.
DR   PRIDE; Q07951; -.
DR   EnsemblFungi; YLR021W_mRNA; YLR021W; YLR021W.
DR   GeneID; 850708; -.
DR   KEGG; sce:YLR021W; -.
DR   SGD; S000004011; IRC25.
DR   VEuPathDB; FungiDB:YLR021W; -.
DR   eggNOG; ENOG502S42X; Eukaryota.
DR   HOGENOM; CLU_133914_0_0_1; -.
DR   InParanoid; Q07951; -.
DR   OMA; SNDMKLP; -.
DR   BioCyc; YEAST:G3O-32182-MON; -.
DR   EvolutionaryTrace; Q07951; -.
DR   PRO; PR:Q07951; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q07951; 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:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; 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; Reference proteome.
FT   CHAIN           1..179
FT                   /note="Proteasome chaperone 3"
FT                   /id="PRO_0000247202"
FT   STRAND          3..10
FT                   /evidence="ECO:0007829|PDB:2Z5B"
FT   STRAND          26..33
FT                   /evidence="ECO:0007829|PDB:2Z5B"
FT   STRAND          38..44
FT                   /evidence="ECO:0007829|PDB:2Z5B"
FT   STRAND          50..56
FT                   /evidence="ECO:0007829|PDB:2Z5B"
FT   HELIX           84..91
FT                   /evidence="ECO:0007829|PDB:2Z5B"
FT   STRAND          95..102
FT                   /evidence="ECO:0007829|PDB:2Z5B"
FT   HELIX           109..122
FT                   /evidence="ECO:0007829|PDB:2Z5B"
FT   STRAND          140..145
FT                   /evidence="ECO:0007829|PDB:2Z5B"
FT   HELIX           147..149
FT                   /evidence="ECO:0007829|PDB:2Z5B"
FT   HELIX           162..176
FT                   /evidence="ECO:0007829|PDB:2Z5B"
SQ   SEQUENCE   179 AA;  20061 MW;  6CA25E8ED0491EE2 CRC64;
     MISYEFQTHL PKGKDSSLNA SSENKELYVQ ATHFNNTILL QIRLNGEMDS TYEVSSKGLN
     PILDINVPLA GNLGNTGGDY DDEEEEFVRD HLSDYQVVTK LGDSADPKVP VVCVQIAELY
     RRVILPEVSG TMAQDNMQFS LLISMSSKIW RATKEQSADD NDFGKLVFVL KCIKDMYAK
 
 
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