ID   RPN2_ASHGO              Reviewed;         930 AA.
AC   Q75CF3;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=26S proteasome regulatory subunit RPN2;
GN   Name=RPN2; OrderedLocusNames=ACL033C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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}.
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; AE016816; AAS51195.1; -; Genomic_DNA.
DR   RefSeq; NP_983371.1; NM_208724.1.
DR   AlphaFoldDB; Q75CF3; -.
DR   SMR; Q75CF3; -.
DR   STRING; 33169.AAS51195; -.
DR   PRIDE; Q75CF3; -.
DR   EnsemblFungi; AAS51195; AAS51195; AGOS_ACL033C.
DR   GeneID; 4619496; -.
DR   KEGG; ago:AGOS_ACL033C; -.
DR   eggNOG; KOG2062; Eukaryota.
DR   HOGENOM; CLU_002323_0_0_1; -.
DR   InParanoid; Q75CF3; -.
DR   OMA; MIMVQQN; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central.
DR   GO; GO:0034515; C:proteasome storage granule; IBA:GO_Central.
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; IBA:GO_Central.
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..930
FT                   /note="26S proteasome regulatory subunit RPN2"
FT                   /id="PRO_0000173805"
FT   REPEAT          358..391
FT                   /note="PC 1"
FT   REPEAT          395..428
FT                   /note="PC 2"
FT   REPEAT          437..471
FT                   /note="PC 3"
FT   REPEAT          472..506
FT                   /note="PC 4"
FT   REPEAT          508..541
FT                   /note="PC 5"
FT   REPEAT          542..577
FT                   /note="PC 6"
FT   REPEAT          578..610
FT                   /note="PC 7"
FT   REPEAT          612..646
FT                   /note="PC 8"
FT   REPEAT          647..684
FT                   /note="PC 9"
FT   REPEAT          690..722
FT                   /note="PC 10"
FT   REGION          806..840
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          911..930
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        809..840
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   930 AA;  102914 MW;  53105ACC9135C8EF CRC64;
     MSVITAAPLL ALLREDDHTV KSYALHSINE VVDQLWSEVS NDITDIEALY EDSKFEDRKL
     AALVVSKIYY NLGEYESAVR YALAAEEYFD INEKSRYVET IVSQSIEMYI KLATENYGKE
     KSEIDLQLVS IFERMLNKCI TAGEYKLALG IALESYRLDV VTNILTQQTS EPNMLKLITY
     VLIAATTTVS NTHFKINILY ALFDILIRLK APDYFAVSKI IVNLNDSKLA ARLFDKLVSE
     KNTEIAYQIA FDLVTSASQG LLNELVATLS TGEGNDRLVE ILSGLPTCDF YNTFLHANKR
     IDRSLLNKSK SSMDGKFSLF HTAVSVSNAF MHAGTTDDTF VRANLQWLGK AQNWAKFTAT
     ASLGIIHQGN LTGGKKIMEP YLPGSRASSR YIKGGSLYGL GLIYAGYGKE IIGYLKDQIV
     ENSSNATDDD VDVLLHGASL GIGLAGMSSN STEIFEALKE VLYADSANSG AAAALGIGLT
     MLGSGDETVA ENLYTYAQET SHGEITKGLA IALALLNYGR EELADETIKK MLEHENDSMR
     YGAVYTIALA YAGTSSNEAV KKLLHVAVSD SNDDVRRASV TALGFVLIRD YTTVPRIVEL
     LSESHNPHVR CGTAFALGVA CAGRGLQAAI DVLEPLTNDP VDFVRQAAMI ALSMILIQQT
     EKTNVKVRDV NEQLRNVIAN KHQEGLAKFG ACVAQGIINA GGRNVTIQLE NSEMGTLNTK
     SVIGLAMFTQ FWYWFPLAHF LSLSFTPTTT IGVRSHDLKI PKFSFHCHTK EGIFDYPPMF
     EEDIDKSIEK VATAVLSTTA KAKARAKKSK KDKAVEPDKS KEEIKVENEQ RDKKEHDADV
     PEEEFKIKYT STYYKVENMT RVVPQQLKYI AFPKDERFTP VRKFKGSNGV IVLSDKTPDE
     PVEVIKTVRQ EKETDAPLPA PFKVQDDLEF