PRS10_SCHPO
ID PRS10_SCHPO Reviewed; 388 AA.
AC O74445; Q9Y7R2;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Probable 26S proteasome subunit rpt4;
GN Name=rpt4; ORFNames=SPCC1682.16, SPCC306.01;
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 [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: The 26S proteasome is involved in the ATP-dependent
CC degradation of ubiquitinated proteins. The regulatory (or ATPase)
CC complex confers ATP dependency and substrate specificity to the 26S
CC complex (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; CU329672; CAA20682.1; -; Genomic_DNA.
DR PIR; T41073; T41073.
DR PIR; T41279; T41279.
DR RefSeq; NP_587809.2; NM_001022802.2.
DR AlphaFoldDB; O74445; -.
DR SMR; O74445; -.
DR BioGRID; 275760; 101.
DR STRING; 4896.SPCC1682.16.1; -.
DR iPTMnet; O74445; -.
DR MaxQB; O74445; -.
DR PaxDb; O74445; -.
DR PRIDE; O74445; -.
DR EnsemblFungi; SPCC1682.16.1; SPCC1682.16.1:pep; SPCC1682.16.
DR GeneID; 2539189; -.
DR KEGG; spo:SPCC1682.16; -.
DR PomBase; SPCC1682.16; rpt4.
DR VEuPathDB; FungiDB:SPCC1682.16; -.
DR eggNOG; KOG0651; Eukaryota.
DR HOGENOM; CLU_000688_2_2_1; -.
DR InParanoid; O74445; -.
DR OMA; YNMTTFE; -.
DR PhylomeDB; O74445; -.
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:O74445; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0031597; C:cytosolic proteasome complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISO:PomBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; NAS:PomBase.
DR GO; GO:0036402; F:proteasome-activating activity; ISM:PomBase.
DR GO; GO:0051306; P:mitotic sister chromatid separation; IC:PomBase.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IEA:UniProt.
DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR005937; 26S_Psome_P45-like.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032501; Prot_ATP_ID_OB_C.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01242; 26Sp45; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Nucleotide-binding; Proteasome; Reference proteome.
FT CHAIN 1..388
FT /note="Probable 26S proteasome subunit rpt4"
FT /id="PRO_0000084736"
FT BINDING 173..180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 388 AA; 43608 MW; 86E1E19DD3811F46 CRC64;
MSERDTALEK YKSYLLQHRE WDSKLKDLRF GNRDLVKKYD KTEDDIKSLQ SVGQIIGEVL
KQLDSERFIV KASSGPRYVV GCRNNVDQSH LVQGVRVSLD MTTLTIMRIL PREVDPLVYN
MSIEDPGDIS FAGVGGLNEQ IRELREVIEL PLKNPELFLR VGIKPPKGVL LYGPPGTGKT
LLARAVAASL GVNFLKVVSS AIVDKYIGES ARIIREMFGY AKEHEPCVIF MDEIDAIGGR
RFSEGTSADR EIQRTLMELL NQMDGFDYLG QTKIIMATNR PDTLDPALLR PGRLDRKIEI
PLPNEVGRME ILKIHLEKVS KQGEIDYEAL VKLTDGTNGA DLRNVVTEAG FIAIKEDRDY
VIQSDLMSAA RKVADLKKLE GTIDYQKL
