RPN1_CANGA
ID RPN1_CANGA Reviewed; 983 AA.
AC Q6FPV6;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=26S proteasome regulatory subunit RPN1;
GN Name=RPN1; OrderedLocusNames=CAGL0J00605g;
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 26 proteasome which is
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S2 family. {ECO:0000305}.
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DR EMBL; CR380956; CAG60685.1; -; Genomic_DNA.
DR RefSeq; XP_447738.1; XM_447738.1.
DR AlphaFoldDB; Q6FPV6; -.
DR SMR; Q6FPV6; -.
DR STRING; 5478.XP_447738.1; -.
DR EnsemblFungi; CAG60685; CAG60685; CAGL0J00605g.
DR GeneID; 2889882; -.
DR KEGG; cgr:CAGL0J00605g; -.
DR CGD; CAL0133686; CAGL0J00605g.
DR VEuPathDB; FungiDB:CAGL0J00605g; -.
DR eggNOG; KOG2005; Eukaryota.
DR HOGENOM; CLU_008705_1_0_1; -.
DR InParanoid; Q6FPV6; -.
DR OMA; KTVYKHM; -.
DR Proteomes; UP000002428; Chromosome J.
DR GO; GO:1905754; C:ascospore-type prospore nucleus; IEA:EnsemblFungi.
DR GO; GO:0034399; C:nuclear periphery; IEA:EnsemblFungi.
DR GO; GO:0031595; C:nuclear proteasome complex; 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:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; 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; IPR016643; 26S_Psome_Rpn1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002015; Proteasome/cyclosome_rpt.
DR InterPro; IPR041433; RPN1_C.
DR InterPro; IPR040892; RPN1_N.
DR PANTHER; PTHR10943:SF1; PTHR10943:SF1; 1.
DR Pfam; PF01851; PC_rep; 1.
DR Pfam; PF18051; RPN1_C; 1.
DR Pfam; PF17781; RPN1_RPN2_N; 1.
DR PIRSF; PIRSF015965; 26S_Psome_Rpn1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 3: Inferred from homology;
KW Proteasome; Reference proteome; Repeat.
FT CHAIN 1..983
FT /note="26S proteasome regulatory subunit RPN1"
FT /id="PRO_0000173812"
FT REPEAT 415..447
FT /note="PC 1"
FT REPEAT 448..484
FT /note="PC 2"
FT REPEAT 485..519
FT /note="PC 3"
FT REPEAT 520..557
FT /note="PC 4"
FT REPEAT 563..595
FT /note="PC 5"
FT REPEAT 768..799
FT /note="PC 6"
FT REPEAT 800..834
FT /note="PC 7"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..721
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 983 AA; 109675 MW; 5AA3CD4678085013 CRC64;
MSTDKKKEEV PKPETEDLTV KDETKNKDKK KANEEEELSE EDQKLKGDLE MLVQTLLEDD
SKLYETTLTQ LKEFIKNSTS SMTAVPKPLK FLRPFYPDLC KAYDKWSDKD QKSSLADMLS
VLAMTYSDTH QHDSLRFRLL SDTSNIASWG HEYVRHLALE IGEVYNEQVE KEAEDNSTST
ESSPQPPHMN FEFSKDVILQ LSLEIVPYFM KHNGEEDAVD LLLEIEAIEK LPQFVDENTY
KRVCQYMIAC VQLLPPPEDI SFLQTAYSIY LSELQLPEAL SLAIRLGNED MIRSVFDATS
DPIVHQQLAY ILAAQRVPFE HPELQEIIGN TKLSEHFLYL AKELNLLTPK IPEDIYKSHL
DSSKSVFSSA GLDSAQQNLA ASFVNAFLNL GYCNDKMITD NDNWVYKTKG DGMTSAVASI
GSIYQWNIDG LQQLDKYLYV DEPEVKAGGL LGIGIASAGV HHDVEPALLL LQEYINHSDT
KISTAAILGI GIAFAGSKND EVLGLLLPVV SNTENSLELA AIAALALSHV FVGTCNGDIT
TAVMDNFLER TPLELKSEWA RFLALSLGLL YLGQGEHVDD VLETINAIEH PMTSAIEVLI
SSCAYTATGD VLLVQDLLHR LTPKAVKSSD EDEDEDNEEL SQEDMNGISA FLGKKENEIA
EEPQGNEGAD NEMEVDSHQD ETTTGENNVK KEENEEEKTE KSEKTENDEE EEDEEESKDE
GANDELAYAV IGIALITMGE EIGKEMSLRH FGHLMHYGNE HIRRMVPLAM GLVSVADPQM
KVFDTLTRFS HDPDLDVSMN SIFAMGLCGV GTNNARLAQL LRQLASYYSR EQDALFITRL
AQGLVHLGKG TMTMDIFNDA HVLNKVTLAS LLTVLVGLIS PSFILKHHQL FYMLNSGVRP
KFIITLNEEG EQIKVNVRIG QAVETVGQAG KPKTITGWIT QSTPVLLGHG ERAELENDEY
ISYTNNIEGV VILKKNPNFQ EEE
