ID   PRS8_SCHPO              Reviewed;         403 AA.
AC   P41836;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=26S proteasome regulatory subunit 8 homolog;
DE   AltName: Full=Protein let1;
GN   Name=let1; ORFNames=SPBC23G7.12c;
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=8056332; DOI=10.1016/0378-1119(94)90006-x;
RA   Michael H., Schmidt H., Fleck O., Gutz H., Liedtke C., Lorentz A.,
RA   Ostermann K.;
RT   "The mating-type region of Schizosaccharomyces pombe contains an essential
RT   gene encoding a protein homologous to human modulators of HIV
RT   transactivation.";
RL   Gene 145:205-210(1994).
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: 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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR   EMBL; U02280; AAA61615.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAA22628.1; -; Genomic_DNA.
DR   PIR; S45176; S45176.
DR   RefSeq; NP_595870.1; NM_001021776.2.
DR   AlphaFoldDB; P41836; -.
DR   SMR; P41836; -.
DR   BioGRID; 277015; 23.
DR   IntAct; P41836; 1.
DR   STRING; 4896.SPBC23G7.12c.1; -.
DR   SwissPalm; P41836; -.
DR   MaxQB; P41836; -.
DR   PaxDb; P41836; -.
DR   PRIDE; P41836; -.
DR   EnsemblFungi; SPBC23G7.12c.1; SPBC23G7.12c.1:pep; SPBC23G7.12c.
DR   GeneID; 2540487; -.
DR   KEGG; spo:SPBC23G7.12c; -.
DR   PomBase; SPBC23G7.12c; -.
DR   VEuPathDB; FungiDB:SPBC23G7.12c; -.
DR   eggNOG; KOG0728; Eukaryota.
DR   HOGENOM; CLU_000688_2_1_1; -.
DR   InParanoid; P41836; -.
DR   OMA; TANCRVA; -.
DR   PhylomeDB; P41836; -.
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:P41836; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
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; ISM: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:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; 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   InterPro; IPR035261; PSMC5.
DR   PANTHER; PTHR23073:SF102; PTHR23073:SF102; 1.
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; Cytoplasm; Nucleotide-binding; Nucleus; Proteasome;
KW   Reference proteome.
FT   CHAIN           1..403
FT                   /note="26S proteasome regulatory subunit 8 homolog"
FT                   /id="PRO_0000084731"
FT   BINDING         186..193
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   403 AA;  45069 MW;  36DEF12C39841315 CRC64;
     MTEVLKTNVL QSNENIVQYY TQKIQDAELA ILQKTQNLRR LEAQRNGLNA RVRLLREEIQ
     LLQEPGSYVG EVIKTMGKNK VLVKVHPEGK YVVDISPDID IKEIKPNIRV ALRNDSYQLI
     KILPNKVDPL VSLMMVEKIP DSTYEMVGGL EKQIKEIKEV IELPVKHPEL FESLGIPQPK
     GILLYGPPGT GKTLLARAVA HHTDCKFIRV SGSELVQKYI GEGSRMVREL FVMAREHAPS
     IIFMDEIDSI GSSRSDSSGG SGDSEVQRTM LELLNQLDGF EATKNIKVIM ATNRIDILDP
     ALLRPGRIDR KIEFPPPSAE ARAEILRIHS RSMNLTRGID LKSIAEKMNG ASGAELKGVC
     TEAGMFALRE RRVHVTQEDF ELAVAKVLNK GDSGEMSLQK LFK