RPN11_SCHPO
ID RPN11_SCHPO Reviewed; 308 AA.
AC P41878; Q10278;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=26S proteasome regulatory subunit rpn11;
DE AltName: Full=Protein pad1;
GN Name=rpn11; Synonyms=bfr2, pad1, sks1; ORFNames=SPAC31G5.13;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7769002; DOI=10.1242/jcs.108.2.569;
RA Shimanuki M., Saka Y., Yanagida M., Toda T.;
RT "A novel essential fission yeast gene pad1+ positively regulates pap1(+)-
RT dependent transcription and is implicated in the maintenance of chromosome
RT structure.";
RL J. Cell Sci. 108:569-579(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7642144; DOI=10.1016/0378-1119(95)00229-y;
RA Usui T., Yoshida M., Honda A., Beppu T., Horinouchi S.;
RT "A K-252a-resistance gene, sks1+, encodes a protein similar to the
RT Caenorhabditis elegans F37 A4.5 gene product and confers multidrug
RT resistance in Schizosaccharomyces pombe.";
RL Gene 161:93-96(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Nagao K., Arioka M., Kadokura H., Yoda K., Yamasaki M.;
RT "The nucleotide sequence of a 9.1 kb DNA fragment of Schizosaccharomyces
RT pombe chromosome reveals the presence of pad1+/sks1+ gene and three
RT previously unknown open reading frames.";
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [5]
RP IDENTIFICATION AS A 26S PROTEASOME SUBUNIT, AND FUNCTION.
RX PubMed=9727008; DOI=10.1074/jbc.273.37.23938;
RA Penney M., Wilkinson C., Wallace M., Javerzat J.-P., Ferrell K., Seeger M.,
RA Dubiel W., McKay S., Allshire R., Gordon C.;
RT "The pad1+ gene encodes a subunit of the 26 S proteasome in fission
RT yeast.";
RL J. Biol. Chem. 273:23938-23945(1998).
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:0000269|PubMed:9727008}.
CC -!- FUNCTION: Transcription factor pap1 is controlled by the functional
CC interaction between the positive regulator pad1 and negative regulator
CC crm1. Both these proteins are also essential for cell viability and for
CC the maintenance of chromosome structure. Pad1 is also responsible for
CC resistance to staurosporine, and other drugs such as cycloheximide and
CC caffeine. {ECO:0000269|PubMed:9727008}.
CC -!- SUBUNIT: The 26S proteasome is composed of a core protease, known as
CC the 20S proteasome, capped at one or both ends by the 19S regulatory
CC complex (RC). The RC is composed of at least 18 different subunits in
CC two subcomplexes, the base and the lid, which form the portions
CC proximal and distal to the 20S proteolytic core, respectively (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M67A family. {ECO:0000305}.
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DR EMBL; D31731; BAA06529.1; -; Genomic_DNA.
DR EMBL; D45047; BAA08087.1; -; Genomic_DNA.
DR EMBL; D84656; BAA12708.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB11697.1; -; Genomic_DNA.
DR PIR; T43293; T43293.
DR PIR; T44427; T44427.
DR RefSeq; NP_594014.1; NM_001019440.2.
DR AlphaFoldDB; P41878; -.
DR SMR; P41878; -.
DR BioGRID; 279475; 51.
DR IntAct; P41878; 1.
DR STRING; 4896.SPAC31G5.13.1; -.
DR MEROPS; M67.A10; -.
DR iPTMnet; P41878; -.
DR MaxQB; P41878; -.
DR PaxDb; P41878; -.
DR PRIDE; P41878; -.
DR EnsemblFungi; SPAC31G5.13.1; SPAC31G5.13.1:pep; SPAC31G5.13.
DR GeneID; 2543040; -.
DR KEGG; spo:SPAC31G5.13; -.
DR PomBase; SPAC31G5.13; rpn11.
DR VEuPathDB; FungiDB:SPAC31G5.13; -.
DR eggNOG; KOG1555; Eukaryota.
DR HOGENOM; CLU_052991_0_1_1; -.
DR InParanoid; P41878; -.
DR OMA; VFQTRMM; -.
DR PhylomeDB; P41878; -.
DR Reactome; R-SPO-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-SPO-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-SPO-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-SPO-382556; ABC-family proteins mediated transport.
DR Reactome; R-SPO-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-SPO-5689603; UCH proteinases.
DR Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR Reactome; R-SPO-5689901; Metalloprotease DUBs.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-68949; Orc1 removal from chromatin.
DR Reactome; R-SPO-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-SPO-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-SPO-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-SPO-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-SPO-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-SPO-8951664; Neddylation.
DR Reactome; R-SPO-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-SPO-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:P41878; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0034399; C:nuclear periphery; IDA:PomBase.
DR GO; GO:0031595; C:nuclear proteasome complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IDA:PomBase.
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; HDA:PomBase.
DR GO; GO:0008237; F:metallopeptidase activity; IBA:GO_Central.
DR GO; GO:0070628; F:proteasome binding; IBA:GO_Central.
DR GO; GO:0051306; P:mitotic sister chromatid separation; IC:PomBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:PomBase.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
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; Zinc.
FT CHAIN 1..308
FT /note="26S proteasome regulatory subunit rpn11"
FT /id="PRO_0000213959"
FT DOMAIN 30..165
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOTIF 112..125
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT CONFLICT 112
FT /note="H -> N (in Ref. 2; BAA06529)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 308 AA; 34572 MW; 57E27C556B34E214 CRC64;
MESLQRLLQG ARMGTGMMGD QPLVDNSECV YISSLALLKM LRHGRHGTPM EVMGLMLGEF
VDDFTVRVVD VFAMPQSGTG VSVEAVDPVF QKNMMDMLKQ TGRPEMVVGW YHSHPGFGCW
LSSVDINTQQ SFEQLTPRAV AVVVDPIQSV KGKVVIDAFR LINPSTLMMG QEPRQTTSNL
GHINKPSIQA LIHGLGRHYY SLRINYKKTE LEEIMLLNLH KQPWAHGLLL ENFNSAAEKN
HASIDKMKSL SEQYTERVQN EVTLSPEQLR IQYVGKQDPK KHLDAEVQKC IDNNISSMLA
CMLDSVAF
