RPN10_SCHPO
ID RPN10_SCHPO Reviewed; 243 AA.
AC O94444;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=26S proteasome regulatory subunit rpn10;
GN Name=rpn10; Synonyms=pus1; ORFNames=SPAC637.10c;
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 [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10809753; DOI=10.1074/jbc.275.20.15182;
RA Wilkinson C.R.M., Ferrell K., Penney M., Wallace M., Dubiel W., Gordon C.;
RT "Analysis of a gene encoding Rpn10 of the fission yeast proteasome reveals
RT that the polyubiquitin-binding site of this subunit is essential when
RT Rpn12/Mts3 activity is compromised.";
RL J. Biol. Chem. 275:15182-15192(2000).
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 FUNCTION.
RX PubMed=12560082; DOI=10.1016/s0014-5793(02)03874-7;
RA Hartmann-Petersen R., Hendil K.B., Gordon C.;
RT "Ubiquitin binding proteins protect ubiquitin conjugates from
RT disassembly.";
RL FEBS Lett. 535:77-81(2003).
RN [4]
RP INTERACTION WITH UCH2.
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).
CC -!- FUNCTION: Protects ubiquitin chains against dissambly by
CC deubiquitinating enzymes thereby promoting protein degradation.
CC {ECO:0000269|PubMed:10809753, ECO:0000269|PubMed:12560082}.
CC -!- SUBUNIT: The 26S proteasome is composed of a core protease, known as
CC the 20S proteasome, capped at one or both ends by the 19S regulatory
CC complex (RC). The RC is composed of at least 18 different subunits in
CC two subcomplexes, the base and the lid, which form the portions
CC proximal and distal to the 20S proteolytic core, respectively (By
CC similarity). Interacts with uch2. {ECO:0000250,
CC ECO:0000269|PubMed:15533439}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10809753}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S5A family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAA22589.1; -; Genomic_DNA.
DR PIR; T39002; T39002.
DR RefSeq; NP_594628.1; NM_001020056.2.
DR PDB; 2X5N; X-ray; 1.30 A; A=2-193.
DR PDBsum; 2X5N; -.
DR AlphaFoldDB; O94444; -.
DR SMR; O94444; -.
DR BioGRID; 280096; 27.
DR IntAct; O94444; 1.
DR STRING; 4896.SPAC637.10c.1; -.
DR iPTMnet; O94444; -.
DR MaxQB; O94444; -.
DR PaxDb; O94444; -.
DR PRIDE; O94444; -.
DR EnsemblFungi; SPAC637.10c.1; SPAC637.10c.1:pep; SPAC637.10c.
DR GeneID; 2543682; -.
DR KEGG; spo:SPAC637.10c; -.
DR PomBase; SPAC637.10c; rpn10.
DR VEuPathDB; FungiDB:SPAC637.10c; -.
DR eggNOG; KOG2884; Eukaryota.
DR HOGENOM; CLU_033293_1_0_1; -.
DR InParanoid; O94444; -.
DR OMA; IQGEDGM; -.
DR PhylomeDB; O94444; -.
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-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:O94444; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IMP:PomBase.
DR GO; GO:0008541; C:proteasome regulatory particle, lid subcomplex; IDA:PomBase.
DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IDA:PomBase.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR GO; GO:0043130; F:ubiquitin binding; ISM:PomBase.
DR GO; GO:1990426; P:mitotic recombination-dependent replication fork processing; IMP:PomBase.
DR GO; GO:0051306; P:mitotic sister chromatid separation; IC:PomBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0120290; P:stalled replication fork localization to nuclear periphery; IMP:PomBase.
DR DisProt; DP02129; -.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR027040; Proteasome_su_Rpn10.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10223:SF0; PTHR10223:SF0; 1.
DR Pfam; PF13519; VWA_2; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR PROSITE; PS50330; UIM; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Proteasome; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..243
FT /note="26S proteasome regulatory subunit rpn10"
FT /id="PRO_0000173833"
FT DOMAIN 5..185
FT /note="VWFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 205..224
FT /note="UIM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REGION 223..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:2X5N"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:2X5N"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:2X5N"
FT HELIX 25..43
FT /evidence="ECO:0007829|PDB:2X5N"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:2X5N"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:2X5N"
FT HELIX 69..76
FT /evidence="ECO:0007829|PDB:2X5N"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:2X5N"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:2X5N"
FT HELIX 122..134
FT /evidence="ECO:0007829|PDB:2X5N"
FT STRAND 137..145
FT /evidence="ECO:0007829|PDB:2X5N"
FT HELIX 152..160
FT /evidence="ECO:0007829|PDB:2X5N"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:2X5N"
FT HELIX 178..183
FT /evidence="ECO:0007829|PDB:2X5N"
SQ SEQUENCE 243 AA; 27140 MW; 9ED58AE82687F79E CRC64;
MVLEATMILI DNSEWMINGD YIPTRFEAQK DTVHMIFNQK INDNPENMCG LMTIGDNSPQ
VLSTLTRDYG KFLSAMHDLP VRGNAKFGDG IQIAQLALKH RENKIQRQRI VAFVGSPIVE
DEKNLIRLAK RMKKNNVAID IIHIGELQNE SALQHFIDAA NSSDSCHLVS IPPSPQLLSD
LVNQSPIGQG VVASQNQFEY GVDPNLDVEL ALALELSMAE ERARQEVAAQ KSSEETEDKK
MQE
