RPN11_CANGA
ID RPN11_CANGA Reviewed; 306 AA.
AC Q6FKS1;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=26S proteasome regulatory subunit RPN11;
GN Name=RPN11; OrderedLocusNames=CAGL0L09152g;
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 peptidase M67A family. {ECO:0000305}.
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DR EMBL; CR380958; CAG62143.1; -; Genomic_DNA.
DR RefSeq; XP_449173.1; XM_449173.1.
DR AlphaFoldDB; Q6FKS1; -.
DR SMR; Q6FKS1; -.
DR STRING; 5478.XP_449173.1; -.
DR MEROPS; M67.001; -.
DR EnsemblFungi; CAG62143; CAG62143; CAGL0L09152g.
DR GeneID; 2891118; -.
DR KEGG; cgr:CAGL0L09152g; -.
DR CGD; CAL0135776; CAGL0L09152g.
DR VEuPathDB; FungiDB:CAGL0L09152g; -.
DR eggNOG; KOG1555; Eukaryota.
DR HOGENOM; CLU_052991_0_1_1; -.
DR InParanoid; Q6FKS1; -.
DR OMA; VFQTRMM; -.
DR Proteomes; UP000002428; Chromosome L.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0005739; C:mitochondrion; IEA:EnsemblFungi.
DR GO; GO:0034399; C:nuclear periphery; IEA:EnsemblFungi.
DR GO; GO:0031595; C:nuclear proteasome complex; IEA:EnsemblFungi.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IEA:EnsemblFungi.
DR GO; GO:0034515; C:proteasome storage granule; IEA:EnsemblFungi.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0061578; F:Lys63-specific deubiquitinase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR GO; GO:0000266; P:mitochondrial fission; IEA:EnsemblFungi.
DR GO; GO:0016559; P:peroxisome fission; IEA:EnsemblFungi.
DR GO; GO:0043248; P:proteasome assembly; IEA:EnsemblFungi.
DR GO; GO:1902906; P:proteasome storage granule assembly; IEA:EnsemblFungi.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR035299; PSMD14.
DR InterPro; IPR024969; Rpn11/EIF3F_C.
DR PANTHER; PTHR10410:SF22; PTHR10410:SF22; 1.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF13012; MitMem_reg; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR PROSITE; PS50249; MPN; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Proteasome;
KW Reference proteome; Zinc.
FT CHAIN 1..306
FT /note="26S proteasome regulatory subunit RPN11"
FT /id="PRO_0000213958"
FT DOMAIN 27..162
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOTIF 109..122
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ SEQUENCE 306 AA; 34424 MW; A46C785BD840B19B CRC64;
MERLQRLMMN TKVGAADANK DDTKETVYIS SIALLKMLKH GRAGVPMEVM GLMLGEFVDE
YTVNVVDVFA MPQSGTGVSV EAVDDVFQAR MMDMLKQTGR DQMVVGWYHS HPGFGCWLSS
VDVNTQKSFE QLNNRAVAVV VDPIQSVKGK VVIDAFRLID TGALINNQEP RQTTSNSGLM
NKANIQALIH GLNRHYYSLN IDYHKTPAET KMLLNLHKEQ WQSGLKMQDY QEKETENLEA
TKRMVAVAQQ YSKRIEEEKE LSEEELKTRY VGKQDPKKHL AKTAENTLEE NTVSVLTAGV
NSIAIK
