PSB10_RAT
ID PSB10_RAT Reviewed; 273 AA.
AC Q4KM35;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Proteasome subunit beta type-10;
DE EC=3.4.25.1;
DE AltName: Full=Low molecular mass protein 10;
DE AltName: Full=Macropain subunit MECl-1;
DE AltName: Full=Multicatalytic endopeptidase complex subunit MECl-1;
DE AltName: Full=Proteasome MECl-1;
DE AltName: Full=Proteasome subunit beta-2i;
DE Flags: Precursor;
GN Name=Psmb10; Synonyms=Lmp10, Mecl1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP INDUCTION BY THP AND DNP.
RX PubMed=16988215; DOI=10.1095/biolreprod.106.053173;
RA Tengowski M.W., Feng D., Sutovsky M., Sutovsky P.;
RT "Differential expression of genes encoding constitutive and inducible 20S
RT proteasomal core subunits in the testis and epididymis of theophylline- or
RT 1,3-dinitrobenzene-exposed rats.";
RL Biol. Reprod. 76:149-163(2007).
CC -!- FUNCTION: The proteasome is a multicatalytic proteinase complex which
CC is characterized by its ability to cleave peptides with Arg, Phe, Tyr,
CC Leu, and Glu adjacent to the leaving group at neutral or slightly basic
CC pH. The proteasome has an ATP-dependent proteolytic activity. This
CC subunit is involved in antigen processing to generate class I binding
CC peptides (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of peptide bonds with very broad specificity.;
CC EC=3.4.25.1;
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC 19S regulatory subunits. The 20S proteasome core is composed of 28
CC subunits that are arranged in four stacked rings, resulting in a
CC barrel-shaped structure. The two end rings are each formed by seven
CC alpha subunits, and the two central rings are each formed by seven beta
CC subunits. The catalytic chamber with the active sites is on the inside
CC of the barrel. Component of the immunoproteasome, where it displaces
CC the equivalent housekeeping subunit PSMB7. Component of the
CC spermatoproteasome, a form of the proteasome specifically found in
CC testis (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}.
CC -!- INDUCTION: Up-regulated by interferon gamma. Up-regulated by
CC theophylline (THP) and down-regulated by 1,3-dinitrobenzene (DNB), two
CC reprotoxic agents thought to induce infertility.
CC {ECO:0000269|PubMed:16988215}.
CC -!- PTM: Autocleaved. The resulting N-terminal Thr residue of the mature
CC subunit is responsible for the nucleophile proteolytic activity.
CC {ECO:0000250|UniProtKB:O35955}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
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DR EMBL; BC098835; AAH98835.1; -; mRNA.
DR RefSeq; NP_001020808.1; NM_001025637.1.
DR AlphaFoldDB; Q4KM35; -.
DR SMR; Q4KM35; -.
DR BioGRID; 253721; 1.
DR STRING; 10116.ENSRNOP00000026462; -.
DR MEROPS; T01.014; -.
DR iPTMnet; Q4KM35; -.
DR PhosphoSitePlus; Q4KM35; -.
DR jPOST; Q4KM35; -.
DR PaxDb; Q4KM35; -.
DR PRIDE; Q4KM35; -.
DR GeneID; 291983; -.
DR KEGG; rno:291983; -.
DR UCSC; RGD:1307428; rat.
DR CTD; 5699; -.
DR RGD; 1307428; Psmb10.
DR VEuPathDB; HostDB:ENSRNOG00000019353; -.
DR eggNOG; KOG0173; Eukaryota.
DR HOGENOM; CLU_035750_3_0_1; -.
DR InParanoid; Q4KM35; -.
DR OMA; RVSYGFY; -.
DR OrthoDB; 977476at2759; -.
DR PhylomeDB; Q4KM35; -.
DR TreeFam; TF106222; -.
DR Reactome; R-RNO-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-RNO-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-RNO-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-RNO-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-RNO-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-RNO-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-RNO-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-RNO-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-RNO-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR Reactome; R-RNO-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-RNO-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-RNO-382556; ABC-family proteins mediated transport.
DR Reactome; R-RNO-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-RNO-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-RNO-4641257; Degradation of AXIN.
DR Reactome; R-RNO-4641258; Degradation of DVL.
DR Reactome; R-RNO-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-RNO-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-RNO-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-RNO-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-RNO-5632684; Hedgehog 'on' state.
DR Reactome; R-RNO-5658442; Regulation of RAS by GAPs.
DR Reactome; R-RNO-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-RNO-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-RNO-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-RNO-5689603; UCH proteinases.
DR Reactome; R-RNO-5689880; Ub-specific processing proteases.
DR Reactome; R-RNO-68867; Assembly of the pre-replicative complex.
DR Reactome; R-RNO-68949; Orc1 removal from chromatin.
DR Reactome; R-RNO-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-RNO-69481; G2/M Checkpoints.
DR Reactome; R-RNO-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-RNO-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-RNO-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-RNO-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-RNO-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-RNO-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-RNO-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-RNO-8951664; Neddylation.
DR Reactome; R-RNO-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-RNO-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:Q4KM35; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000019494; Expressed in pancreas and 20 other tissues.
DR Genevisible; Q4KM35; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; IBA:GO_Central.
DR GO; GO:1990111; C:spermatoproteasome complex; ISS:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0000902; P:cell morphogenesis; ISO:RGD.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0042098; P:T cell proliferation; ISO:RGD.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR034384; Proteasome_beta2/10.
DR InterPro; IPR024689; Proteasome_bsu_C.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11599:SF41; PTHR11599:SF41; 1.
DR Pfam; PF12465; Pr_beta_C; 1.
DR Pfam; PF00227; Proteasome; 1.
DR PRINTS; PR00141; PROTEASOME.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Hydrolase; Nucleus; Phosphoprotein; Protease;
KW Proteasome; Reference proteome; Threonine protease.
FT PROPEP 1..39
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000391410"
FT CHAIN 40..273
FT /note="Proteasome subunit beta type-10"
FT /id="PRO_0000391411"
FT ACT_SITE 40
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 39..40
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:O35955"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P40306"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40306"
SQ SEQUENCE 273 AA; 29038 MW; BA3830BFDDFDC91B CRC64;
MLKQAVEHRG GFSFENCQRN ASLEHVLPGL RVPLARKTGT TIAGLVFRDG VILGADTRAT
NDSVVADKSC EKIHFIAPKI YCCGAGVAAD TEMTTRMAAS KMELHALSTG REPRVATVTR
ILRQTLFRYQ GHVGASLIVG GVDLNGPQLY SVHPHGSYSR LPFTALGSGQ DAAVALLEDR
FQPNMTLEAA QELLVEAITA GILGDLGSGG SVDACVITAG GAKLQRALSS PIEPVQRAGQ
YRFAPGTTPV QTQEVRALTL ELLEETVQAM EVE
