RP13B_SCHPO
ID RP13B_SCHPO Reviewed; 388 AA.
AC Q9USM1;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Proteasomal ubiquitin receptor ADRM1 homolog rpn1302 {ECO:0000250|UniProtKB:Q16186};
DE AltName: Full=Regulatory particle non-ATPase 13ba protein {ECO:0000303|PubMed:21098295};
GN Name=rpn1302; Synonyms=rpn13b {ECO:0000303|PubMed:21098295};
GN ORFNames=SPCC16A11.16c;
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: Component 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}.
CC -!- CAUTION: The c-terminal sequence diverges from classical ADRM1 family
CC proteins. {ECO:0000305}.
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DR EMBL; CU329672; CAB53088.1; -; Genomic_DNA.
DR PIR; T41089; T41089.
DR RefSeq; NP_588003.1; NM_001022994.2.
DR AlphaFoldDB; Q9USM1; -.
DR SMR; Q9USM1; -.
DR BioGRID; 275753; 17.
DR STRING; 4896.SPCC16A11.16c.1; -.
DR iPTMnet; Q9USM1; -.
DR MaxQB; Q9USM1; -.
DR PaxDb; Q9USM1; -.
DR EnsemblFungi; SPCC16A11.16c.1; SPCC16A11.16c.1:pep; SPCC16A11.16c.
DR GeneID; 2539182; -.
DR KEGG; spo:SPCC16A11.16c; -.
DR PomBase; SPCC16A11.16c; -.
DR VEuPathDB; FungiDB:SPCC16A11.16c; -.
DR eggNOG; KOG3037; Eukaryota.
DR HOGENOM; CLU_041798_0_0_1; -.
DR InParanoid; Q9USM1; -.
DR OMA; QADHRKG; -.
DR PRO; PR:Q9USM1; -.
DR Proteomes; UP000002485; Chromosome III.
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; 2.30.29.70; -; 1.
DR InterPro; IPR006773; Rpn13/ADRM1.
DR InterPro; IPR044868; Rpn13/ADRM1_Pru.
DR InterPro; IPR038633; Rpn13/ADRM1_Pru_sf.
DR PANTHER; PTHR12225; PTHR12225; 1.
DR Pfam; PF04683; Proteasom_Rpn13; 1.
DR PROSITE; PS51917; PRU; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..388
FT /note="Proteasomal ubiquitin receptor ADRM1 homolog
FT rpn1302"
FT /id="PRO_0000351078"
FT DOMAIN 15..132
FT /note="Pru"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01265"
FT REGION 202..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 388 AA; 43903 MW; B6885C57A4023CC7 CRC64;
MESVFGRVRN ETSERGKYGL VSVKAGKLQR KPGTNILQAD HRKGVIYMQM ASDELLHFYW
KERARVSREV EDDYIIFPEE AEFIKIDECT TGRVYALKFK SSSQIHFYWM QEYSDEKDKE
TASLINQLIA DPVNTTRTIN SHNNSSSRGT DDSSTSQLLQ LFGAASQDAL QDFNWEVLSP
TAEAPAILPR FPNVNESANM YRASSESNLN GPHATAGENG EDHEEATASP LDENIDYTHS
RTLELLEQLQ PLILNETTFV EPFSIDRESH RVITHPRVYP KIFPHSPSDL LRISGRAELS
ENRDFFKHLS SLMEAVAKPE SESLREICNL SLEQVQSASG AELFLHALYD RLVNEGVIVI
SHITQEGSDG EVEEEGDVEM RESNEKDE
