PSB4_RAT
ID PSB4_RAT Reviewed; 263 AA.
AC P34067; P28071; P97719;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Proteasome subunit beta type-4;
DE AltName: Full=Macropain beta chain;
DE AltName: Full=Multicatalytic endopeptidase complex beta chain;
DE AltName: Full=Proteasome beta chain;
DE AltName: Full=Proteasome chain 3;
DE Short=RN3;
DE Flags: Precursor;
GN Name=Psmb4;
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] OF 1-140.
RX PubMed=8645151; DOI=10.1042/bj3150733;
RA Thomson S., Rivett A.J.;
RT "Processing of N3, a mammalian proteasome beta-type subunit.";
RL Biochem. J. 315:733-738(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-263.
RX PubMed=8482379; DOI=10.1016/0014-5793(93)81553-c;
RA Thomson S., Balson D.F., Rivett A.J.;
RT "cDNA cloning of a new type of subunit of mammalian proteasomes.";
RL FEBS Lett. 322:135-138(1993).
RN [3]
RP PROTEIN SEQUENCE OF 45-55.
RX PubMed=2335214; DOI=10.1016/0014-5793(90)80220-d;
RA Lilley K.S., Davison M.D., Rivett A.J.;
RT "N-terminal sequence similarities between components of the multicatalytic
RT proteinase complex.";
RL FEBS Lett. 262:327-329(1990).
RN [4]
RP PROTEIN SEQUENCE OF 60-79 AND 109-130, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (NOV-2006) to UniProtKB.
RN [5]
RP INDUCTION.
RX PubMed=16483544; DOI=10.1016/j.bbrc.2006.01.163;
RA Razeghi P., Baskin K.K., Sharma S., Young M.E., Stepkowski S., Essop M.F.,
RA Taegtmeyer H.;
RT "Atrophy, hypertrophy, and hypoxemia induce transcriptional regulators of
RT the ubiquitin proteasome system in the rat heart.";
RL Biochem. Biophys. Res. Commun. 342:361-364(2006).
CC -!- FUNCTION: Non-catalytic component of the 20S core proteasome complex
CC involved in the proteolytic degradation of most intracellular proteins.
CC This complex plays numerous essential roles within the cell by
CC associating with different regulatory particles. Associated with two
CC 19S regulatory particles, forms the 26S proteasome and thus
CC participates in the ATP-dependent degradation of ubiquitinated
CC proteins. The 26S proteasome plays a key role in the maintenance of
CC protein homeostasis by removing misfolded or damaged proteins that
CC could impair cellular functions, and by removing proteins whose
CC functions are no longer required. Associated with the PA200 or PA28,
CC the 20S proteasome mediates ubiquitin-independent protein degradation.
CC This type of proteolysis is required in several pathways including
CC spermatogenesis (20S-PA200 complex) or generation of a subset of MHC
CC class I-presented antigenic peptides (20S-PA28 complex).
CC SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300
CC repressor SNIP1. {ECO:0000250|UniProtKB:P28070}.
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 Forms a ternary complex with SMAD1 and OAZ1 before PSMB4 is
CC incorporated into the 20S proteasome. Interacts with PRPF19.
CC {ECO:0000250|UniProtKB:P28070}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28070}. Nucleus
CC {ECO:0000250|UniProtKB:P28070}. 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:P28070}.
CC -!- INDUCTION: Up-regulated in cardiac hypertrophy and hypoxemia.
CC {ECO:0000269|PubMed:16483544}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
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DR EMBL; S82190; AAB47113.2; -; mRNA.
DR EMBL; L17127; AAA42054.1; -; mRNA.
DR PIR; S09084; S09084.
DR PIR; S32507; S32507.
DR PDB; 6EPC; EM; 12.30 A; 7=1-263.
DR PDB; 6EPD; EM; 15.40 A; 7=1-263.
DR PDB; 6EPE; EM; 12.80 A; 7=1-263.
DR PDB; 6EPF; EM; 11.80 A; 7=1-263.
DR PDB; 6TU3; EM; 2.70 A; N/b=1-263.
DR PDBsum; 6EPC; -.
DR PDBsum; 6EPD; -.
DR PDBsum; 6EPE; -.
DR PDBsum; 6EPF; -.
DR PDBsum; 6TU3; -.
DR AlphaFoldDB; P34067; -.
DR SMR; P34067; -.
DR BioGRID; 248653; 3.
DR IntAct; P34067; 1.
DR STRING; 10116.ENSRNOP00000028484; -.
DR MEROPS; T01.987; -.
DR iPTMnet; P34067; -.
DR PhosphoSitePlus; P34067; -.
DR World-2DPAGE; 0004:P34067; -.
DR jPOST; P34067; -.
DR PaxDb; P34067; -.
DR PeptideAtlas; P34067; -.
DR PRIDE; P34067; -.
DR UCSC; RGD:61877; rat.
DR RGD; 61877; Psmb4.
DR eggNOG; KOG0185; Eukaryota.
DR InParanoid; P34067; -.
DR PhylomeDB; P34067; -.
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:P34067; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0036064; C:ciliary basal body; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
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:0001530; F:lipopolysaccharide binding; ISO:RGD.
DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; ISO:RGD.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR CDD; cd03760; proteasome_beta_type_4; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR016295; Proteasome_beta4.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11599:SF5; PTHR11599:SF5; 1.
DR Pfam; PF00227; Proteasome; 1.
DR PIRSF; PIRSF001213; Psome_endopept_beta; 1.
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; Acetylation; Cytoplasm; Direct protein sequencing; Nucleus;
KW Phosphoprotein; Proteasome; Reference proteome.
FT PROPEP 1..44
FT /evidence="ECO:0000269|PubMed:2335214"
FT /id="PRO_0000026583"
FT CHAIN 45..263
FT /note="Proteasome subunit beta type-4"
FT /id="PRO_0000026584"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P28070"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28070"
FT MOD_RES 101
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P28070"
FT CONFLICT 41
FT /note="P -> S (in Ref. 2; AAA42054)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="V -> L (in Ref. 2; AAA42054)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="F -> S (in Ref. 1; AAB47113)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="F -> L (in Ref. 1; AAB47113)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="N -> I (in Ref. 2; AAA42054)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="I -> F (in Ref. 1; AAB47113)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="V -> L (in Ref. 1; AAB47113)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="F -> L (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 101..120
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 129..145
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 191..200
FT /evidence="ECO:0007829|PDB:6TU3"
FT HELIX 206..223
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 231..237
FT /evidence="ECO:0007829|PDB:6TU3"
FT STRAND 240..247
FT /evidence="ECO:0007829|PDB:6TU3"
SQ SEQUENCE 263 AA; 29197 MW; C8FCB91265F8FB90 CRC64;
MEAFWESRTG HWAGGPAPGQ FYRVPSTPSC LMDPMSAPAR PITRTQNPMV TGTSVLGVKF
DCGVVIAADM LGSYGSLARF RNISRIMRVN DSTMLGASGD YADFQYLKQV LGQMVIDEEL
FGDGHSYSPR AIHSWLTRAM YSRRSKMNPL WNTKVIGGYA GGESFLGYVD MLGVAYEAPS
LATGYGAYLA QPLLREVLEK QPVLSQTEAR ELVERCMRVL YYRDARSYNR FQVATVTEKG
VEIEGPLSAQ TNWDIAHMIS GFE
