RPN12_SCHPO
ID RPN12_SCHPO Reviewed; 270 AA.
AC P50524; Q9UUC3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=26S proteasome regulatory subunit rpn12;
GN Name=rpn12; Synonyms=mts3; ORFNames=SPBC16G5.01, SPBC342.07;
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 [MRNA].
RX PubMed=8621436; DOI=10.1074/jbc.271.10.5704;
RA Gordon C.B., McGurk G., Wallace M., Hastie N.D.;
RT "A conditional lethal mutant in the fission yeast 26 S protease subunit
RT mts3+ is defective in metaphase to anaphase transition.";
RL J. Biol. Chem. 271:5704-5711(1996).
RN [2]
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).
CC -!- FUNCTION: Acts as a regulatory subunit of the 26S proteasome which is
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC -!- INTERACTION:
CC P50524; P38937: cut8; NbExp=2; IntAct=EBI-1152607, EBI-1152591;
CC -!- SIMILARITY: Belongs to the proteasome subunit S14 family.
CC {ECO:0000305}.
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DR EMBL; X92682; CAA63366.1; -; mRNA.
DR EMBL; CU329671; CAB46777.1; -; Genomic_DNA.
DR PIR; T40280; T40280.
DR RefSeq; NP_596750.2; NM_001023770.2.
DR PDB; 4B0Z; X-ray; 1.58 A; A/B=1-224.
DR PDBsum; 4B0Z; -.
DR AlphaFoldDB; P50524; -.
DR SMR; P50524; -.
DR BioGRID; 276569; 30.
DR IntAct; P50524; 2.
DR STRING; 4896.SPBC16G5.01.1; -.
DR iPTMnet; P50524; -.
DR MaxQB; P50524; -.
DR PaxDb; P50524; -.
DR PRIDE; P50524; -.
DR EnsemblFungi; SPBC16G5.01.1; SPBC16G5.01.1:pep; SPBC16G5.01.
DR GeneID; 2540025; -.
DR KEGG; spo:SPBC16G5.01; -.
DR PomBase; SPBC16G5.01; rpn12.
DR VEuPathDB; FungiDB:SPBC16G5.01; -.
DR eggNOG; KOG3151; Eukaryota.
DR HOGENOM; CLU_046003_2_1_1; -.
DR InParanoid; P50524; -.
DR OMA; VYIRHPL; -.
DR PhylomeDB; P50524; -.
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-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:P50524; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0034399; C:nuclear periphery; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IDA:PomBase.
DR GO; GO:0051306; P:mitotic sister chromatid separation; IC:PomBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IGI:PomBase.
DR InterPro; IPR006746; 26S_Psome_Rpn12.
DR InterPro; IPR033464; CSN8_PSD8_EIF3K.
DR InterPro; IPR000717; PCI_dom.
DR PANTHER; PTHR12387; PTHR12387; 1.
DR Pfam; PF10075; CSN8_PSD8_EIF3K; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Proteasome; Reference proteome.
FT CHAIN 1..270
FT /note="26S proteasome regulatory subunit rpn12"
FT /id="PRO_0000173850"
FT DOMAIN 65..237
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT HELIX 7..14
FT /evidence="ECO:0007829|PDB:4B0Z"
FT HELIX 18..34
FT /evidence="ECO:0007829|PDB:4B0Z"
FT HELIX 44..63
FT /evidence="ECO:0007829|PDB:4B0Z"
FT HELIX 67..81
FT /evidence="ECO:0007829|PDB:4B0Z"
FT HELIX 91..104
FT /evidence="ECO:0007829|PDB:4B0Z"
FT HELIX 108..117
FT /evidence="ECO:0007829|PDB:4B0Z"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:4B0Z"
FT HELIX 128..141
FT /evidence="ECO:0007829|PDB:4B0Z"
FT HELIX 145..153
FT /evidence="ECO:0007829|PDB:4B0Z"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:4B0Z"
FT HELIX 161..182
FT /evidence="ECO:0007829|PDB:4B0Z"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:4B0Z"
FT HELIX 188..194
FT /evidence="ECO:0007829|PDB:4B0Z"
FT HELIX 200..210
FT /evidence="ECO:0007829|PDB:4B0Z"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:4B0Z"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:4B0Z"
SQ SEQUENCE 270 AA; 30899 MW; C1BC6571722A034D CRC64;
MSTLDLNHLA DLYDRKDWNA CKKELLKLKV ELAKQNLFVP TSDKEKASFA RNVFEYGVLV
SIQTCDIESF ARYASQVIPF YHDSLVPSSR MGLVTGLNLL YLLSENRIAE FHTALESVPD
KSLFERDPYV EWVISLEQNV MEGAFDKVAS MIRSCNFPEF SYFMKIVMSM VRNEIATCAE
KVYSEIPLSN ATSLLYLENT KETEKLAEER GWDIRDGVIY FPKEANALET EDGMLIDEED
ELELPPTASK HTISSIRQLL SYTSELEQIV
