ID PRS4_SCHPO Reviewed; 448 AA.
AC P36612;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 27-MAR-2024, entry version 174.
DE RecName: Full=26S proteasome regulatory subunit 4 homolog;
DE AltName: Full=Protein mts2;
GN Name=mts2; ORFNames=SPBC4.07c;
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].
RC STRAIN=972 / ATCC 24843;
RX PubMed=8247131; DOI=10.1038/366355a0;
RA Gordon C.B., McGurk G., Dillon P., Rosen C., Hastie N.D.;
RT "Defective mitosis due to a mutation in the gene for a fission yeast 26S
RT protease subunit.";
RL Nature 366:355-357(1993).
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.
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; Z29366; CAA82554.1; -; mRNA.
DR EMBL; CU329671; CAB58406.1; -; Genomic_DNA.
DR PIR; S39348; S39348.
DR RefSeq; NP_595480.1; NM_001021391.2.
DR AlphaFoldDB; P36612; -.
DR SMR; P36612; -.
DR BioGRID; 277455; 29.
DR IntAct; P36612; 1.
DR STRING; 284812.P36612; -.
DR iPTMnet; P36612; -.
DR MaxQB; P36612; -.
DR PaxDb; 4896-SPBC4-07c-1; -.
DR EnsemblFungi; SPBC4.07c.1; SPBC4.07c.1:pep; SPBC4.07c.
DR GeneID; 2540939; -.
DR KEGG; spo:SPBC4.07c; -.
DR PomBase; SPBC4.07c; -.
DR VEuPathDB; FungiDB:SPBC4.07c; -.
DR eggNOG; KOG0726; Eukaryota.
DR HOGENOM; CLU_000688_2_3_1; -.
DR InParanoid; P36612; -.
DR OMA; QDDTDPM; -.
DR PhylomeDB; P36612; -.
DR Reactome; R-SPO-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-SPO-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-SPO-5689603; UCH proteinases.
DR Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR PRO; PR:P36612; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005838; C:proteasome regulatory particle; IDA:PomBase.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; NAS:PomBase.
DR GO; GO:0036402; F:proteasome-activating activity; IBA:GO_Central.
DR GO; GO:0010498; P:proteasomal protein catabolic process; EXP:PomBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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_2nd.
DR PANTHER; PTHR23073; 26S PROTEASOME REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR23073:SF24; 26S PROTEASOME REGULATORY SUBUNIT 4; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Nucleus; Proteasome;
KW Reference proteome.
FT CHAIN 1..448
FT /note="26S proteasome regulatory subunit 4 homolog"
FT /id="PRO_0000084684"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 232..239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 448 AA; 50060 MW; 451AEEF6A24C29D4 CRC64;
MGQAQSGNFS NFGDGANGDN KKDQKKDKPK YEPPVPTRTG RRKKKAQSGP DASAKLPTVI
PTTRCRLRLL KMQRIHDHLL MEEEYVQNQE RLKPQDERTQ EERNRVDEIR GTPMSVGTLE
EIIDDDHAIV STAGPEYYVS IMSFVDKDML EPGCSVLLHH KAMSIVGLLL DDTDPMINVM
KLDKAPTESY ADIGGLESQI QEIKEAVELP LTHPELYEEM GIKPPKGVIL YGAPGTGKTL
LAKAVANQTS ATFLRVVGSE LIQKYLGDGP RLVRQLFNAA EEHSPSIVFI DEIDAIGTKR
YDAQSGAERE IQRTMLELLN QLDGFDTSQR DIKVIMATNR ISDLDPALIR PGRIDRKILF
ENPDEATKRK IFTIHTSKMN LGEDVNLEEL IQCKDDLSGA EIKAIVSEAG LLALRERRMR
VVMDDFRQAR EKVLKTKDEG GPAGGLYI
//
