SEM1_SCHPO
ID SEM1_SCHPO Reviewed; 71 AA.
AC O14140;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=26S proteasome complex subunit rpn15;
DE AltName: Full=mRNA export factor dss1 {ECO:0000303|PubMed:15990877};
GN Name=rpn15; Synonyms=dss1 {ECO:0000303|PubMed:15990877}, sem1;
GN ORFNames=SPAC3G6.02 {ECO:0000312|PomBase:SPAC3G6.02};
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 FUNCTION, INTERACTION WITH MLO3; RAE1; NUP98 AND NUP146, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15990877; DOI=10.1038/sj.emboj.7600713;
RA Thakurta A.G., Gopal G., Yoon J.H., Kozak L., Dhar R.;
RT "Homolog of BRCA2-interacting Dss1p and Uap56p link Mlo3p and Rae1p for
RT mRNA export in fission yeast.";
RL EMBO J. 24:2512-2523(2005).
RN [3]
RP FUNCTION.
RX PubMed=16149916; DOI=10.1042/bj20051238;
RA Josse L., Harley M.E., Pires I.M., Hughes D.A.;
RT "Fission yeast Dss1 associates with the proteasome and is required for
RT efficient ubiquitin-dependent proteolysis.";
RL Biochem. J. 393:303-309(2006).
RN [4]
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 [5]
RP FUNCTION.
RX PubMed=18023413; DOI=10.1016/j.bbrc.2007.11.024;
RA Mannen T., Andoh T., Tani T.;
RT "Dss1 associating with the proteasome functions in selective nuclear mRNA
RT export in yeast.";
RL Biochem. Biophys. Res. Commun. 365:664-671(2008).
RN [6]
RP FUNCTION, AND INTERACTION WITH RAD24.
RX PubMed=20231270; DOI=10.1074/jbc.m109.083485;
RA Selvanathan S.P., Thakurta A.G., Dhakshnamoorthy J., Zhou M.,
RA Veenstra T.D., Dhar R.;
RT "Schizosaccharomyces pombe Dss1p is a DNA damage checkpoint protein that
RT recruits Rad24p, Cdc25p, and Rae1p to DNA double-strand breaks.";
RL J. Biol. Chem. 285:14122-14133(2010).
RN [7]
RP FUNCTION, INTERACTION WITH UBIQUITIN, AND DOMAIN.
RX PubMed=25306921; DOI=10.1016/j.molcel.2014.09.008;
RA Paraskevopoulos K., Kriegenburg F., Tatham M.H., Roesner H.I., Medina B.,
RA Larsen I.B., Brandstrup R., Hardwick K.G., Hay R.T., Kragelund B.B.,
RA Hartmann-Petersen R., Gordon C.;
RT "Dss1 is a 26S proteasome ubiquitin receptor.";
RL Mol. Cell 56:453-461(2014).
CC -!- FUNCTION: Versatile protein that might stabilize multiple protein
CC complexes involved in diverse pathways. Subunit of the 26S proteasome
CC which plays a role in ubiquitin-dependent proteolysis
CC (PubMed:16149916). Acts as a ubiquitin receptor of the 26S proteasome,
CC by interacting with ubiquitin chains linked by 'Lys-63' and 'Lys-48'
CC (PubMed:25306921). Involved in nuclear export of specific sets of mRNAs
CC (PubMed:18023413). Links the mRNA adapter mlo3 to rae1 for targeting
CC mRNA-protein complex to the proteins of the nucleoporin complex (NPC)
CC (PubMed:15990877). Involved in recombinational repair of DNA. Plays a
CC critical role in linking repair and checkpoint factors to damaged DNA
CC sites by specifically recruiting rad24 and cdc25 to the DSBs
CC (PubMed:20231270). {ECO:0000269|PubMed:15990877,
CC ECO:0000269|PubMed:16149916, ECO:0000269|PubMed:18023413,
CC ECO:0000269|PubMed:20231270, ECO:0000269|PubMed:25306921}.
CC -!- SUBUNIT: Interacts with mlo3, rae1, nup98/nup189 and nup146
CC (PubMed:15990877). Interacts with rad24 (PubMed:20231270). Interacts
CC (via UBSs) with ubiquitin (ubi3/ubi5) (PubMed:25306921).
CC {ECO:0000269|PubMed:15990877, ECO:0000269|PubMed:20231270,
CC ECO:0000269|PubMed:25306921}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- DOMAIN: Two unstructured ubiquitin-binding sites (UBSs) mediate
CC interaction with ubiquitin. UBS-I is the strong and UBS-II the weak
CC binding site. {ECO:0000305|PubMed:25306921}.
CC -!- SIMILARITY: Belongs to the DSS1/SEM1 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB16278.1; -; Genomic_DNA.
DR PIR; T38721; T38721.
DR RefSeq; NP_594968.1; NM_001020399.2.
DR AlphaFoldDB; O14140; -.
DR SMR; O14140; -.
DR BioGRID; 279492; 330.
DR IntAct; O14140; 7.
DR STRING; 4896.SPAC3G6.02.1; -.
DR MaxQB; O14140; -.
DR PaxDb; O14140; -.
DR EnsemblFungi; SPAC3G6.02.1; SPAC3G6.02.1:pep; SPAC3G6.02.
DR GeneID; 2543058; -.
DR KEGG; spo:SPAC3G6.02; -.
DR PomBase; SPAC3G6.02; rpn15.
DR VEuPathDB; FungiDB:SPAC3G6.02; -.
DR eggNOG; KOG4764; Eukaryota.
DR HOGENOM; CLU_141774_1_0_1; -.
DR InParanoid; O14140; -.
DR OMA; TLWENNW; -.
DR PRO; PR:O14140; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0000502; C:proteasome complex; IBA:GO_Central.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IDA:PomBase.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0006406; P:mRNA export from nucleus; IEA:InterPro.
DR GO; GO:0043248; P:proteasome assembly; ISO:PomBase.
DR DisProt; DP01191; -.
DR InterPro; IPR007834; DSS1_SEM1.
DR PANTHER; PTHR16771; PTHR16771; 1.
DR Pfam; PF05160; DSS1_SEM1; 1.
DR SMART; SM01385; DSS1_SEM1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; mRNA transport; Nucleus; Reference proteome; Transport.
FT CHAIN 1..71
FT /note="26S proteasome complex subunit rpn15"
FT /id="PRO_0000122969"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 16..25
FT /note="UBS-II"
FT /evidence="ECO:0000305|PubMed:25306921"
FT REGION 38..49
FT /note="UBS-I"
FT /evidence="ECO:0000305|PubMed:25306921"
FT COMPBIAS 22..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 71 AA; 8111 MW; 3E86B803266EF456 CRC64;
MSRAALPSLE NLEDDDEFED FATENWPMKD TELDTGDDTL WENNWDDEDI GDDDFSVQLQ
AELKKKGVAA N
