RP13A_SCHPO
ID RP13A_SCHPO Reviewed; 291 AA.
AC Q9Y7Y6;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Proteasomal ubiquitin receptor ADRM1 homolog rpn1301 {ECO:0000250|UniProtKB:Q16186};
DE AltName: Full=Regulatory particle non-ATPase 13a protein {ECO:0000303|PubMed:21098295};
GN Name=rpn1301; Synonyms=rpn13a {ECO:0000303|PubMed:21098295};
GN ORFNames=SPBC342.04;
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 SUBUNIT, AND FUNCTION.
RX PubMed=21098295; DOI=10.1073/pnas.1015530107;
RA Bohn S., Beck F., Sakata E., Walzthoeni T., Beck M., Aebersold R.,
RA Foerster F., Baumeister W., Nickell S.;
RT "Structure of the 26S proteasome from Schizosaccharomyces pombe at
RT subnanometer resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:20992-20997(2010).
CC -!- FUNCTION: Ccomponent of the 26S proteasome, a multiprotein complex
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC This complex plays a key role in the maintenance of protein homeostasis
CC by removing misfolded or damaged proteins, which could impair cellular
CC functions, and by removing proteins whose functions are no longer
CC required (PubMed:21098295). Therefore, the proteasome participates in
CC numerous cellular processes, including cell cycle progression,
CC apoptosis, or DNA damage repair. Within the complex, functions as a
CC proteasomal ubiquitin receptor (Probable).
CC {ECO:0000269|PubMed:21098295, ECO:0000305|PubMed:21098295}.
CC -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex
CC (PubMed:21098295). The 2 S.pombe rpn13 homologs, rpn1301 and rpn1302
CC are present at a 0.2-1 ratio (PubMed:21098295).
CC {ECO:0000269|PubMed:21098295}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- DOMAIN: The Pru (pleckstrin-like receptor for ubiquitin) domain
CC mediates interactions with rpn2 and ubiquitin.
CC {ECO:0000250|UniProtKB:Q16186}.
CC -!- SIMILARITY: Belongs to the ADRM1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAB46774.1; -; Genomic_DNA.
DR PIR; T40277; T40277.
DR RefSeq; NP_596747.1; NM_001023767.2.
DR AlphaFoldDB; Q9Y7Y6; -.
DR SMR; Q9Y7Y6; -.
DR BioGRID; 277496; 10.
DR STRING; 4896.SPBC342.04.1; -.
DR iPTMnet; Q9Y7Y6; -.
DR MaxQB; Q9Y7Y6; -.
DR PaxDb; Q9Y7Y6; -.
DR PRIDE; Q9Y7Y6; -.
DR EnsemblFungi; SPBC342.04.1; SPBC342.04.1:pep; SPBC342.04.
DR GeneID; 2540980; -.
DR KEGG; spo:SPBC342.04; -.
DR PomBase; SPBC342.04; -.
DR VEuPathDB; FungiDB:SPBC342.04; -.
DR eggNOG; KOG3037; Eukaryota.
DR HOGENOM; CLU_041798_0_0_1; -.
DR InParanoid; Q9Y7Y6; -.
DR OMA; SNQRHFF; -.
DR PhylomeDB; Q9Y7Y6; -.
DR Reactome; R-SPO-5689603; UCH proteinases.
DR Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR PRO; PR:Q9Y7Y6; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IDA:PomBase.
DR GO; GO:0061133; F:endopeptidase activator activity; IBA:GO_Central.
DR GO; GO:0070628; F:proteasome binding; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0051306; P:mitotic sister chromatid separation; IC:PomBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IC:PomBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 1.10.2020.20; -; 1.
DR Gene3D; 2.30.29.70; -; 1.
DR InterPro; IPR044867; DEUBAD_dom.
DR InterPro; IPR006773; Rpn13/ADRM1.
DR InterPro; IPR044868; Rpn13/ADRM1_Pru.
DR InterPro; IPR038633; Rpn13/ADRM1_Pru_sf.
DR InterPro; IPR032368; RPN13_DEUBAD.
DR InterPro; IPR038108; RPN13_DEUBAD_sf.
DR PANTHER; PTHR12225; PTHR12225; 1.
DR Pfam; PF04683; Proteasom_Rpn13; 1.
DR Pfam; PF16550; RPN13_C; 1.
DR PROSITE; PS51916; DEUBAD; 1.
DR PROSITE; PS51917; PRU; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Proteasome; Reference proteome.
FT CHAIN 1..291
FT /note="Proteasomal ubiquitin receptor ADRM1 homolog
FT rpn1301"
FT /id="PRO_0000351079"
FT DOMAIN 1..114
FT /note="Pru"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01265"
FT DOMAIN 178..290
FT /note="DEUBAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01264"
FT REGION 135..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 291 AA; 31821 MW; 9CB484A22BF1E4F7 CRC64;
MSLITFKAGK LRRVPGTKLL RADPEKGYIV MNRDAYGLIH FQWAKRNDLE NPEDDIIVFS
SECTFEKVTE CTTGRAYMLK YPSSAHSLFY WMQEASDDND TSYAERINSY IKDQDLLDPA
RSDVATVSDM MEVDTVEQSE PIAQPTESSK ESSEIGAPNS DEINSSEAVR NLLATISAQA
GFGGSTVDLC EILKPSNLTD LLCQEGVIDR LMPYMPPDTP NNLEGVLAIV SSPQYAQALR
SFSQALNSPG GVNIISALGL SLDESANPNE GGALQFLKAI ARFVSRNNGS E
