PSDE_CAEEL
ID PSDE_CAEEL Reviewed; 312 AA.
AC O76577;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 14;
DE EC=3.4.19.-;
DE AltName: Full=26S proteasome regulatory subunit rpn11;
GN Name=rpn-11; ORFNames=K07D4.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Metalloprotease component of the 26S proteasome that
CC specifically cleaves 'Lys-63'-linked polyubiquitin chains. The 26S
CC proteasome is involved in the ATP-dependent degradation of
CC ubiquitinated proteins. The function of the 'Lys-63'-specific
CC deubiquitination of the proteasome is unclear (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Component of the 19S regulatory cap of the 26S proteasome.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC O76577; O61792: rpn-8; NbExp=5; IntAct=EBI-324401, EBI-324407;
CC -!- SIMILARITY: Belongs to the peptidase M67A family. PSMD14 subfamily.
CC {ECO:0000305}.
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DR EMBL; FO081599; CCD72745.1; -; Genomic_DNA.
DR PIR; T33344; T33344.
DR RefSeq; NP_494712.1; NM_062311.5.
DR AlphaFoldDB; O76577; -.
DR SMR; O76577; -.
DR BioGRID; 39100; 54.
DR IntAct; O76577; 8.
DR STRING; 6239.K07D4.3; -.
DR MEROPS; M67.A11; -.
DR EPD; O76577; -.
DR PaxDb; O76577; -.
DR PeptideAtlas; O76577; -.
DR PRIDE; O76577; -.
DR EnsemblMetazoa; K07D4.3.1; K07D4.3.1; WBGene00004467.
DR EnsemblMetazoa; K07D4.3.2; K07D4.3.2; WBGene00004467.
DR GeneID; 173744; -.
DR KEGG; cel:CELE_K07D4.3; -.
DR UCSC; K07D4.3.1; c. elegans.
DR CTD; 173744; -.
DR WormBase; K07D4.3; CE19527; WBGene00004467; rpn-11.
DR eggNOG; KOG1555; Eukaryota.
DR GeneTree; ENSGT00730000111116; -.
DR HOGENOM; CLU_052991_0_1_1; -.
DR InParanoid; O76577; -.
DR OMA; VFQTRMM; -.
DR OrthoDB; 1031881at2759; -.
DR PhylomeDB; O76577; -.
DR Reactome; R-CEL-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-CEL-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-CEL-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-CEL-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-CEL-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-CEL-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-CEL-382556; ABC-family proteins mediated transport.
DR Reactome; R-CEL-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-CEL-4641258; Degradation of DVL.
DR Reactome; R-CEL-5632684; Hedgehog 'on' state.
DR Reactome; R-CEL-5689603; UCH proteinases.
DR Reactome; R-CEL-5689880; Ub-specific processing proteases.
DR Reactome; R-CEL-5689901; Metalloprotease DUBs.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-68949; Orc1 removal from chromatin.
DR Reactome; R-CEL-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-CEL-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-CEL-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-CEL-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-CEL-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-CEL-8951664; Neddylation.
DR Reactome; R-CEL-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-CEL-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; O76577; -.
DR PRO; PR:O76577; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00004467; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005838; C:proteasome regulatory particle; ISS:WormBase.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IBA:GO_Central.
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:0008237; F:metallopeptidase activity; IBA:GO_Central.
DR GO; GO:0070628; F:proteasome binding; IBA:GO_Central.
DR GO; GO:0010623; P:programmed cell death involved in cell development; IMP:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
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 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Proteasome;
KW Reference proteome; Ubl conjugation pathway; Zinc.
FT CHAIN 1..312
FT /note="26S proteasome non-ATPase regulatory subunit 14"
FT /id="PRO_0000213954"
FT DOMAIN 33..168
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOTIF 115..128
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
SQ SEQUENCE 312 AA; 34596 MW; 3EEA4CFF998D69A1 CRC64;
MERFLRLGGL GGNLGTFGAN PQDSNQVDTS ETVYISSLAL LKMLKHGRAG VPMEVMGLML
GEFVDDYTVN VIDVFAMPQS GTGVSVEAVD PVFQAKMLDM LKQTGRPEMV VGWYHSHPGF
GCWLSGVDIN TQQSFEALSD RAVAVVVDPI QSVKGKVVID AFRTINPQSM ALNQEPRQTT
SNLGHLQKPS IQALIHGLNR HYYSIPIAYR THDLEQKMLL NLNKLSWMDA VSVENYSKCG
EQNKEHLKAM LKLAKNYKKA LEDEKNMTDQ ELAIKNVGKM DPKRHIADEV SKMLNDNIVQ
SLAGMMATTS LQ
