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Proteasome subunit beta type-5 (EC 3.4.25.1) (Macropain epsilon chain) (Multicatalytic endopeptidase complex epsilon chain) (Proteasome chain 6) (Proteasome epsilon chain) (Proteasome subunit X)

 PSB5_RAT                Reviewed;         263 AA.
P28075;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
29-APR-2008, sequence version 3.
23-MAY-2018, entry version 135.
RecName: Full=Proteasome subunit beta type-5;
EC=3.4.25.1 {ECO:0000250|UniProtKB:P28074};
AltName: Full=Macropain epsilon chain;
AltName: Full=Multicatalytic endopeptidase complex epsilon chain;
AltName: Full=Proteasome chain 6;
AltName: Full=Proteasome epsilon chain;
AltName: Full=Proteasome subunit X;
Flags: Precursor;
Name=Psmb5;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Yokota K.Y., Tanaka K.;
Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF 60-77.
PubMed=2335214; DOI=10.1016/0014-5793(90)80220-D;
Lilley K.S., Davison M.D., Rivett A.J.;
"N-terminal sequence similarities between components of the
multicatalytic proteinase complex.";
FEBS Lett. 262:327-329(1990).
[4]
INDUCTION BY THP AND DNB.
PubMed=16988215; DOI=10.1095/biolreprod.106.053173;
Tengowski M.W., Feng D., Sutovsky M., Sutovsky P.;
"Differential expression of genes encoding constitutive and inducible
20S proteasomal core subunits in the testis and epididymis of
theophylline- or 1,3-dinitrobenzene-exposed rats.";
Biol. Reprod. 76:149-163(2007).
-!- FUNCTION: Component of the 20S core proteasome complex involved in
the proteolytic degradation of most intracellular proteins. This
complex plays numerous essential roles within the cell by
associating with different regulatory particles. Associated with
two 19S regulatory particles, forms the 26S proteasome and thus
participates in the ATP-dependent degradation of ubiquitinated
proteins. The 26S proteasome plays a key role in the maintenance
of protein homeostasis by removing misfolded or damaged proteins
that could impair cellular functions, and by removing proteins
whose functions are no longer required. Associated with the PA200
or PA28, the 20S proteasome mediates ubiquitin-independent protein
degradation. This type of proteolysis is required in several
pathways including spermatogenesis (20S-PA200 complex) or
generation of a subset of MHC class I-presented antigenic peptides
(20S-PA28 complex). Within the 20S core complex, PSMB5 displays a
chymotrypsin-like activity. {ECO:0000250|UniProtKB:P28074}.
-!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
specificity. {ECO:0000250|UniProtKB:P28074}.
-!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and
two 19S regulatory subunits. The 20S proteasome core is a barrel-
shaped complex made of 28 subunits that are arranged in four
stacked rings. The two outer rings are each formed by seven alpha
subunits, and the two inner rings are formed by seven beta
subunits. The proteolytic activity is exerted by three beta-
subunits PSMB5, PSMB6 and PSMB7. Directly interacts with POMP.
Interacts with ABCB1 and TAP1. {ECO:0000250|UniProtKB:P28074}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28074}.
Nucleus {ECO:0000250|UniProtKB:P28074}.
-!- INDUCTION: Down-regulated by theophylline (THP) and up-regulated
by 1,3-dinitrobenzene (DNB), two reprotoxic agents thought to
induce infertility. {ECO:0000269|PubMed:16988215}.
-!- SIMILARITY: Belongs to the peptidase T1B family.
{ECO:0000255|PROSITE-ProRule:PRU00809}.
-!- SEQUENCE CAUTION:
Sequence=BAA08204.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA08204.1; Type=Miscellaneous discrepancy; Note=Sequencing error.; Evidence={ECO:0000305};
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EMBL; D45247; BAA08204.1; ALT_SEQ; mRNA.
EMBL; CH474049; EDM14180.1; -; Genomic_DNA.
PIR; S09087; S09087.
RefSeq; NP_001099197.2; NM_001105727.2.
UniGene; Rn.2; -.
PDB; 6EPC; EM; 12.30 A; 5=1-263.
PDB; 6EPD; EM; 15.40 A; 5=1-263.
PDB; 6EPE; EM; 12.80 A; 5=1-263.
PDB; 6EPF; EM; 11.80 A; 5=1-263.
PDBsum; 6EPC; -.
PDBsum; 6EPD; -.
PDBsum; 6EPE; -.
PDBsum; 6EPF; -.
ProteinModelPortal; P28075; -.
SMR; P28075; -.
BioGrid; 248073; 2.
IntAct; P28075; 1.
STRING; 10116.ENSRNOP00000018005; -.
MEROPS; T01.012; -.
SwissPalm; P28075; -.
PaxDb; P28075; -.
PRIDE; P28075; -.
GeneID; 29425; -.
KEGG; rno:29425; -.
UCSC; RGD:61879; rat.
CTD; 5693; -.
RGD; 61879; Psmb5.
eggNOG; KOG0175; Eukaryota.
eggNOG; ENOG410XQRP; LUCA.
HOGENOM; HOG000091082; -.
HOVERGEN; HBG108297; -.
InParanoid; P28075; -.
KO; K02737; -.
PhylomeDB; P28075; -.
PRO; PR:P28075; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
Gene3D; 3.60.20.10; -; 1.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR000243; Pept_T1A_subB.
InterPro; IPR037558; Proteasome_beta_5.
InterPro; IPR016050; Proteasome_bsu_CS.
InterPro; IPR001353; Proteasome_sua/b.
InterPro; IPR023333; Proteasome_suB-type.
PANTHER; PTHR11599:SF51; PTHR11599:SF51; 1.
Pfam; PF00227; Proteasome; 1.
PRINTS; PR00141; PROTEASOME.
SUPFAM; SSF56235; SSF56235; 1.
PROSITE; PS00854; PROTEASOME_BETA_1; 1.
PROSITE; PS51476; PROTEASOME_BETA_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
Hydrolase; Nucleus; Protease; Proteasome; Reference proteome;
Threonine protease; Zymogen.
PROPEP 1 59 Removed in mature form.
{ECO:0000269|PubMed:2335214}.
/FTId=PRO_0000026593.
CHAIN 60 263 Proteasome subunit beta type-5.
/FTId=PRO_0000026594.
ACT_SITE 60 60 Nucleophile.
{ECO:0000250|UniProtKB:P28074}.
BINDING 108 108 Bortezomib; via amide nitrogen.
{ECO:0000250}.
CONFLICT 62 62 T -> I (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 69 69 H -> E (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 73 73 V -> L (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 83 83 P -> A (in Ref. 2; EDM14180).
{ECO:0000305}.
SEQUENCE 263 AA; 28585 MW; 317FC0C827FE65CA CRC64;
MALASVLQRP MPVNQHGFFG LGGRADLLDL GPGSPGDGLS LAAPSWGVPE EPRIEMLHGT
TTLAFKFQHG VIVAADSRAT AGPYIASQTV KKVIEINPYL LGTMAGGAAD CSFWERLLAR
QCRIYELRNK ERISVAAASK LLANMVYQYK GMGLSMGTMI CGWDKRGPGL YYVDSEGNRI
SGTAFSVGSG SVYAFGVMDR GYSYDLQVEE AYDLARRAIY QATYRDAYSG GAVNLYHVRE
DGWIRVSSDN VADLHDKYTS SIP


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