PSB7_RAT
ID PSB7_RAT Reviewed; 277 AA.
AC Q9JHW0;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Proteasome subunit beta type-7;
DE EC=3.4.25.1;
DE AltName: Full=Macropain chain Z;
DE AltName: Full=Multicatalytic endopeptidase complex chain Z;
DE AltName: Full=Proteasome subunit Z;
DE Flags: Precursor;
GN Name=Psmb7;
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 [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Kang J.S., Liu H.L., Li R.X.;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 [3]
RP PROTEIN SEQUENCE OF 44-72; 165-184 AND 226-237, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Component of the 20S core proteasome complex involved in the
CC proteolytic degradation of most intracellular proteins. This complex
CC plays numerous essential roles within the cell by associating with
CC different regulatory particles. Associated with two 19S regulatory
CC particles, forms the 26S proteasome and thus participates in the ATP-
CC dependent degradation of ubiquitinated proteins. The 26S proteasome
CC plays a key role in the maintenance of protein homeostasis by removing
CC misfolded or damaged proteins that could impair cellular functions, and
CC by removing proteins whose functions are no longer required. Associated
CC with the PA200 or PA28, the 20S proteasome mediates ubiquitin-
CC independent protein degradation. This type of proteolysis is required
CC in several pathways including spermatogenesis (20S-PA200 complex) or
CC generation of a subset of MHC class I-presented antigenic peptides
CC (20S-PA28 complex). Within the 20S core complex, PSMB7 displays a
CC trypsin-like activity. {ECO:0000250|UniProtKB:Q99436}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of peptide bonds with very broad specificity.;
CC EC=3.4.25.1; Evidence={ECO:0000250|UniProtKB:Q99436};
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC 19S regulatory subunits. The 20S proteasome core is a barrel-shaped
CC complex made of 28 subunits that are arranged in four stacked rings.
CC The two outer rings are each formed by seven alpha subunits, and the
CC two inner rings are formed by seven beta subunits. The proteolytic
CC activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7.
CC {ECO:0000250|UniProtKB:Q99436}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q99436}. Nucleus
CC {ECO:0000250|UniProtKB:Q99436}. Note=Translocated from the cytoplasm
CC into the nucleus following interaction with AKIRIN2, which bridges the
CC proteasome with the nuclear import receptor IPO9.
CC {ECO:0000250|UniProtKB:Q99436}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
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DR EMBL; AF285103; AAF97811.1; -; mRNA.
DR EMBL; BC060551; AAH60551.1; -; mRNA.
DR PIR; S09082; S09082.
DR RefSeq; NP_445984.1; NM_053532.1.
DR PDB; 6EPC; EM; 12.30 A; 2=1-277.
DR PDB; 6EPD; EM; 15.40 A; 2=1-277.
DR PDB; 6EPE; EM; 12.80 A; 2=1-277.
DR PDB; 6EPF; EM; 11.80 A; 2=1-277.
DR PDB; 6TU3; EM; 2.70 A; I/W=1-277.
DR PDBsum; 6EPC; -.
DR PDBsum; 6EPD; -.
DR PDBsum; 6EPE; -.
DR PDBsum; 6EPF; -.
DR PDBsum; 6TU3; -.
DR AlphaFoldDB; Q9JHW0; -.
DR SMR; Q9JHW0; -.
DR BioGRID; 250112; 2.
DR IntAct; Q9JHW0; 1.
DR STRING; 10116.ENSRNOP00000016876; -.
DR MEROPS; T01.011; -.
DR iPTMnet; Q9JHW0; -.
DR PhosphoSitePlus; Q9JHW0; -.
DR World-2DPAGE; 0004:Q9JHW0; -.
DR jPOST; Q9JHW0; -.
DR PaxDb; Q9JHW0; -.
DR PRIDE; Q9JHW0; -.
DR GeneID; 85492; -.
DR KEGG; rno:85492; -.
DR UCSC; RGD:621093; rat.
DR CTD; 5695; -.
DR RGD; 621093; Psmb7.
DR VEuPathDB; HostDB:ENSRNOG00000011732; -.
DR eggNOG; KOG0173; Eukaryota.
DR InParanoid; Q9JHW0; -.
DR OMA; VDKTGPH; -.
DR OrthoDB; 977476at2759; -.
DR PhylomeDB; Q9JHW0; -.
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-6798695; Neutrophil degranulation.
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:Q9JHW0; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000011732; Expressed in skeletal muscle tissue and 20 other tissues.
DR ExpressionAtlas; Q9JHW0; baseline and differential.
DR Genevisible; Q9JHW0; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0000502; C:proteasome complex; ISO:RGD.
DR GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
DR GO; GO:0019774; C:proteasome core complex, beta-subunit 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:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR035216; Proteasome_beta7.
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:SF42; PTHR11599:SF42; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Hydrolase; Nucleus;
KW Protease; Proteasome; Reference proteome; Threonine protease; Zymogen.
FT PROPEP 1..43
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000026649"
FT CHAIN 44..277
FT /note="Proteasome subunit beta type-7"
FT /id="PRO_0000026650"
FT ACT_SITE 44
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 92..113
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 119..132
FT /evidence="ECO:0007829|PDB:6TU3"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 191..208
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 216..224
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 226..233
FT /evidence="ECO:0007829|PDB:6TU3"
SQ SEQUENCE 277 AA; 29927 MW; 6F26D115159A0A41 CRC64;
MAAVSVFQAP VGGFSFDNCR RNAVLEADFA KKGFKLPKAR KTGTTIAGVV YKDGIVLGAD
TRATEGMVVA DKNCSKIHFI SPNIYCCGAG TAADTDMTTQ LISSNLELHS LTTGRLPRVV
TANRMLKQML FRYQGYIGAA LVLGGVDVTG PHLYSIYPHG STDKLPYVTM GSGSLAAMAV
FEDKFRPDME EEEAKKLVSE AIAAGIFNDL GSGSNIDLCV ISKSKLDFLR PYSVPNKKGT
RFGRYRCEKG TTAVLTEKVT PLELEVLEEI VQTMDTS
