RPN1_SCHPO
ID RPN1_SCHPO Reviewed; 891 AA.
AC P87048; Q9HDV7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=26S proteasome regulatory subunit rpn1;
DE AltName: Full=19S regulatory cap region of 26S protease subunit 2;
DE AltName: Full=Proteasome non-ATPase subunit mts4;
GN Name=rpn1; Synonyms=mts4; ORFNames=SPBP19A11.03c;
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=9325304; DOI=10.1074/jbc.272.41.25768;
RA Wilkinson C.R., Wallace M., Seeger M., Dubiel W., Gordon C.B.;
RT "Mts4, a non-ATPase subunit of the 26 S protease in fission yeast is
RT essential for mitosis and interacts directly with the ATPase subunit
RT Mts2.";
RL J. Biol. Chem. 272:25768-25777(1997).
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).
RN [3]
RP INTERACTION WITH UBP6.
RX PubMed=15533439; DOI=10.1016/j.jmb.2004.09.057;
RA Stone M., Hartmann-Petersen R., Seeger M., Bech-Otschir D., Wallace M.,
RA Gordon C.;
RT "Uch2/Uch37 is the major deubiquitinating enzyme associated with the 26S
RT proteasome in fission yeast.";
RL J. Mol. Biol. 344:697-706(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, 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: Acts as a regulatory subunit of the 26 proteasome which is
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC -!- SUBUNIT: Component of the 26S proteasome. Interacts with ubp6.
CC {ECO:0000269|PubMed:15533439}.
CC -!- INTERACTION:
CC P87048; P38937: cut8; NbExp=4; IntAct=EBI-1152810, EBI-1152591;
CC -!- SIMILARITY: Belongs to the proteasome subunit S2 family. {ECO:0000305}.
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DR EMBL; Y09819; CAA70948.1; -; mRNA.
DR EMBL; CU329671; CAC19753.1; -; Genomic_DNA.
DR PIR; T52488; T52488.
DR RefSeq; NP_596171.1; NM_001022091.2.
DR AlphaFoldDB; P87048; -.
DR SMR; P87048; -.
DR BioGRID; 277782; 60.
DR IntAct; P87048; 3.
DR STRING; 4896.SPBP19A11.03c.1; -.
DR iPTMnet; P87048; -.
DR MaxQB; P87048; -.
DR PaxDb; P87048; -.
DR PRIDE; P87048; -.
DR EnsemblFungi; SPBP19A11.03c.1; SPBP19A11.03c.1:pep; SPBP19A11.03c.
DR GeneID; 2541268; -.
DR KEGG; spo:SPBP19A11.03c; -.
DR PomBase; SPBP19A11.03c; -.
DR VEuPathDB; FungiDB:SPBP19A11.03c; -.
DR eggNOG; KOG2005; Eukaryota.
DR HOGENOM; CLU_008705_1_0_1; -.
DR InParanoid; P87048; -.
DR OMA; KTVYKHM; -.
DR PhylomeDB; P87048; -.
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:P87048; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:1905754; C:ascospore-type prospore nucleus; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0034399; C:nuclear periphery; IDA:PomBase.
DR GO; GO:0031595; C:nuclear proteasome complex; IPI: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:0034515; C:proteasome storage granule; IBA:GO_Central.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR GO; GO:0051306; P:mitotic sister chromatid separation; IC:PomBase.
DR GO; GO:0010498; P:proteasomal protein catabolic process; EXP:PomBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IPI:PomBase.
DR GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR016643; 26S_Psome_Rpn1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002015; Proteasome/cyclosome_rpt.
DR InterPro; IPR041433; RPN1_C.
DR InterPro; IPR040892; RPN1_N.
DR PANTHER; PTHR10943:SF1; PTHR10943:SF1; 1.
DR Pfam; PF01851; PC_rep; 2.
DR Pfam; PF18051; RPN1_C; 1.
DR Pfam; PF17781; RPN1_RPN2_N; 1.
DR PIRSF; PIRSF015965; 26S_Psome_Rpn1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Proteasome; Reference proteome; Repeat.
FT CHAIN 1..891
FT /note="26S proteasome regulatory subunit rpn1"
FT /id="PRO_0000173814"
FT REPEAT 408..441
FT /note="PC 1"
FT REPEAT 442..478
FT /note="PC 2"
FT REPEAT 479..513
FT /note="PC 3"
FT REPEAT 517..550
FT /note="PC 4"
FT REPEAT 673..704
FT /note="PC 5"
FT REPEAT 705..739
FT /note="PC 6"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 72
FT /note="V -> E (in Ref. 1; CAA70948)"
FT /evidence="ECO:0000305"
FT CONFLICT 870..891
FT /note="PLTSLEGIVILKKNTEDIEMTA -> TFDFVGRYCYFKKKYGGH (in
FT Ref. 1; CAA70948)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 891 AA; 97999 MW; 03FC9AB767745C5A CRC64;
MSSKDISSKS PSGNDALNDK KGTKTSETND RNSTNNTKER DELEDLSEED LQLKNDLELL
VQAVQDATPE LVGSSLTQLK EIIRTSTSSM TAVPKPLKFL RPHYFTLVKI YDSWPQSPQK
TQLADILSVL GMSYSNTSKH ESLKYRLQGV TTDPSLWGHE YVRHLASEIE EEFASRQEEE
APTDDLMELA LTIVPFFLTH NAEADAIDLL QELGAIEKVV PFVELDNASR VCLYITSCVN
LLPFPEDVAM LRTAHAIYRK FDQLTQALNV AIRLDDMSLI KEDCEAATDP LLKKQMSYML
ARQQIPMDMG DEELNDALNN THLSDHFHYL GKELNLMDPK VPEDIFKTHL EVARTGLGAS
GVYSAKQNLA NTFVNALVNA GYSNDRLILV DDEKTSWIYK NKESGLISAT ASIGLLQLWN
VDMGLSLLDK YLYSSEENTK AGALLGIGVT NVAVRNEADP AMAILSEYLE TGSVKLRASA
ILGLGLAYSG ANREDLLDML SPIVTDTDCP MQLSCLAALS LGLIFVGTCN GDVASTILQT
LMEREESAQN DQWGRFMALG LALLFNGKQD LADATVETLK AIEGKIARQA EILVDICSYA
GTGNVLHIQK LLHICSEPPS DDAKESETTI QTFAALGVAT IAMGEDIGAE MVLRHFDHMM
HYGEPSIRKA IPLALGLLSA SNPQMRIFDT LSRYSHDNDL DVAYNAIFAM GLVGAGTSNA
RLAQLLRQLA SYYHKESNAL FMVRIAQGLL YLGKGTMTLN PYHTERQILG QTAFAGLMTV
VLAMLDANTF VLDTSHWLLY AITLAIRPRM LITLGEDGQY LPVSVRVGQA VDVVGQAGRP
KVITGWVTHT TPVLLHHNER AELATEAYTP LTSLEGIVIL KKNTEDIEMT A
