PSA5_SCHPO
ID PSA5_SCHPO Reviewed; 247 AA.
AC Q9UT97;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Probable proteasome subunit alpha type-5;
GN Name=pup2; ORFNames=SPAC323.02c;
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).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-55, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: The proteasome is a multicatalytic proteinase complex which
CC is characterized by its ability to cleave peptides with Arg, Phe, Tyr,
CC Leu, and Glu adjacent to the leaving group at neutral or slightly basic
CC pH. The proteasome has an ATP-dependent proteolytic activity (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC 19S regulatory subunits. The 20S proteasome core is composed of 28
CC subunits that are arranged in four stacked rings, resulting in a
CC barrel-shaped structure. The two end rings are each formed by seven
CC alpha subunits, and the two central rings are each formed by seven beta
CC subunits. The catalytic chamber with the active sites is on the inside
CC of the barrel (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC ProRule:PRU00808}.
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DR EMBL; CU329670; CAB53405.1; -; Genomic_DNA.
DR PIR; T38639; T38639.
DR RefSeq; NP_594372.1; NM_001019793.2.
DR AlphaFoldDB; Q9UT97; -.
DR SMR; Q9UT97; -.
DR BioGRID; 279634; 9.
DR IntAct; Q9UT97; 3.
DR MINT; Q9UT97; -.
DR STRING; 4896.SPAC323.02c.1; -.
DR MEROPS; T01.975; -.
DR iPTMnet; Q9UT97; -.
DR MaxQB; Q9UT97; -.
DR PaxDb; Q9UT97; -.
DR PRIDE; Q9UT97; -.
DR EnsemblFungi; SPAC323.02c.1; SPAC323.02c.1:pep; SPAC323.02c.
DR GeneID; 2543205; -.
DR KEGG; spo:SPAC323.02c; -.
DR PomBase; SPAC323.02c; pup2.
DR VEuPathDB; FungiDB:SPAC323.02c; -.
DR eggNOG; KOG0176; Eukaryota.
DR HOGENOM; CLU_035750_4_2_1; -.
DR InParanoid; Q9UT97; -.
DR OMA; FQVEYAR; -.
DR PhylomeDB; Q9UT97; -.
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-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:Q9UT97; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005839; C:proteasome core complex; IBA:GO_Central.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IDA: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:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd03753; proteasome_alpha_type_5; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR023332; Proteasome_alpha-type.
DR InterPro; IPR033812; Proteasome_alpha_type_5.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR Pfam; PF00227; Proteasome; 1.
DR Pfam; PF10584; Proteasome_A_N; 1.
DR SMART; SM00948; Proteasome_A_N; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Proteasome; Reference proteome.
FT CHAIN 1..247
FT /note="Probable proteasome subunit alpha type-5"
FT /id="PRO_0000124128"
FT MOD_RES 55
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 247 AA; 27573 MW; 713E1AB3A3ADE658 CRC64;
MFMTRSEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGV KTKDAVVLGV EKRLTSPLME
SHSVEKLFEI DSHIGCAISG LTADARTIIE HARVQTQNHR FTYDEPQGIE STTQSICDLA
LRFGEGEDGE ERIMSRPFGV ALLIAGIDEH GPQLYHSEPS GTYFRYEAKA IGSGSEPAKS
ELVKEFHKDM TLEEAEVLIL KVLRQVMEEK LDSKNVQLAK VTAEGGFHIY NDEEMADAVA
REQQRMD
