ID   RPN2_CANGA              Reviewed;         941 AA.
AC   Q6FIP2;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=26S proteasome regulatory subunit RPN2;
GN   Name=RPN2; OrderedLocusNames=CAGL0M12859g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Acts as a regulatory subunit of the 26S proteasome which is
CC       involved in the ATP-dependent degradation of ubiquitinated proteins.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the proteasome subunit S1 family. {ECO:0000305}.
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DR   EMBL; CR380959; CAG62882.1; -; Genomic_DNA.
DR   RefSeq; XP_449902.1; XM_449902.1.
DR   AlphaFoldDB; Q6FIP2; -.
DR   SMR; Q6FIP2; -.
DR   STRING; 5478.XP_449902.1; -.
DR   PRIDE; Q6FIP2; -.
DR   EnsemblFungi; CAG62882; CAG62882; CAGL0M12859g.
DR   GeneID; 2891453; -.
DR   KEGG; cgr:CAGL0M12859g; -.
DR   CGD; CAL0136353; CAGL0M12859g.
DR   VEuPathDB; FungiDB:CAGL0M12859g; -.
DR   eggNOG; KOG2062; Eukaryota.
DR   HOGENOM; CLU_002323_0_0_1; -.
DR   InParanoid; Q6FIP2; -.
DR   OMA; MIMVQQN; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IEA:EnsemblFungi.
DR   GO; GO:0034515; C:proteasome storage granule; IEA:EnsemblFungi.
DR   GO; GO:0004175; F:endopeptidase activity; IEA:EnsemblFungi.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:EnsemblFungi.
DR   GO; GO:0043248; P:proteasome assembly; IEA:EnsemblFungi.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR016642; 26S_Psome_Rpn2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002015; Proteasome/cyclosome_rpt.
DR   InterPro; IPR035266; PSMD1.
DR   InterPro; IPR040623; RPN2_C.
DR   PANTHER; PTHR10943:SF2; PTHR10943:SF2; 1.
DR   Pfam; PF01851; PC_rep; 3.
DR   Pfam; PF18004; RPN2_C; 1.
DR   PIRSF; PIRSF015947; 26S_Psome_Rpn2; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   3: Inferred from homology;
KW   Proteasome; Reference proteome; Repeat.
FT   CHAIN           1..941
FT                   /note="26S proteasome regulatory subunit RPN2"
FT                   /id="PRO_0000173806"
FT   REPEAT          363..396
FT                   /note="PC 1"
FT   REPEAT          400..437
FT                   /note="PC 2"
FT   REPEAT          442..476
FT                   /note="PC 3"
FT   REPEAT          477..511
FT                   /note="PC 4"
FT   REPEAT          513..546
FT                   /note="PC 5"
FT   REPEAT          547..582
FT                   /note="PC 6"
FT   REPEAT          583..615
FT                   /note="PC 7"
FT   REPEAT          617..651
FT                   /note="PC 8"
FT   REPEAT          652..689
FT                   /note="PC 9"
FT   REPEAT          695..731
FT                   /note="PC 10"
FT   REGION          808..854
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        814..854
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   941 AA;  104059 MW;  FE8EE869E7AEC8A8 CRC64;
     MSLTTAAPLL ALLKEKDAEV KAYALQSINE GVDQFWSEVS NDLPEIEALY DDNGFQDRKM
     AALIASKVYY NLGEYESAVK YALAAEEKFD IDEKTQYVET IVSKSIEMYI KLATEIYNKS
     GEQVNLDPKL TIVFEKMMTK CTQANEYKLA LGIALEAFRL DVVKSILQER LGEDQEGGSM
     KLMSYVLTAA TTTVFNSKFK DEILRLLFDL LMPLKNADYF ITSKVVVNLN DPELATQLFE
     KLHDEEQIEV SYQIAFDLVS SASQHLLEKL HHNLSERSYD SGLLEILTGI PTCDYYNTFL
     LNKKNIDISL LNKSKSSLDG KFSLFHTAVS VSNGYMHAGT TDNSFIKANL SWLGKAQNWA
     KFSATASLGV IHKGNLIDGK KVMAPYLPGS RSSSRFIKGG SLYGLGLIYA GFGRDIVDYL
     KTHLIENSGT TGDEDVDVLL HGASLGVGLA AMGTANNEVY EALKDVLYND VATSGEAAAF
     GIGLTLLGTG DETAINDLFT YAQETSHGNI TRGLSMALAL INYGRQEQAD ELIDKMLASE
     NSLIRYGGAF SIALAYVGTG NNKVVKKLLH LAVSDSNDDV RRAAVTALGF VLLRDYTTVP
     RIVQLLAESH NAHDRCGAAF ALGIACAGKG LQAAIDVLEP MTKDPADFVR QAAMISLSLV
     MIQQTEKMNP KVASINSHFL SVITNKHQEG LAKFGACVAL GIMNAGGRNV TIQLENAETG
     TLDTKSVVGL AMFTQFWYWF PMAHFLSLSF TPTTIVGVRG SDLNIPKFDM NCYAREDVFS
     YPKMFEESAD KEVEKVATAI LSTTARAKAR AKKTKKEKDT NEDDKKKKEK DLKKEETKKD
     DAKKESEAEE DFNKNRYSSK PYKIENMSRV LPQQLKYVQF IKEERFTPVR KFKGTNGVVV
     LKDNKPSEPA SIIETVRQSK DVNAPLPTPF KVTEELDFEK I