ID   PSB2_BOVIN              Reviewed;         201 AA.
AC   Q5E9K0;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Proteasome subunit beta type-2;
GN   Name=PSMB2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF COMPLEX WITH 20S PROTEASOME.
RX   PubMed=12015144; DOI=10.1016/s0969-2126(02)00748-7;
RA   Unno M., Mizushima T., Morimoto Y., Tomisugi Y., Tanaka K., Yasuoka N.,
RA   Tsukihara T.;
RT   "The structure of the mammalian 20S proteasome at 2.75 A resolution.";
RL   Structure 10:609-618(2002).
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       {ECO:0000250|UniProtKB:P49721}.
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:0000269|PubMed:12015144}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P49721}. Nucleus
CC       {ECO:0000250|UniProtKB:P49721}. 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:P49721}.
CC   -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00809}.
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DR   EMBL; BT020855; AAX08872.1; -; mRNA.
DR   EMBL; BT020920; AAX08937.1; -; mRNA.
DR   EMBL; BC102367; AAI02368.1; -; mRNA.
DR   RefSeq; NP_001015615.1; NM_001015615.1.
DR   PDB; 1IRU; X-ray; 2.75 A; K/Y=1-201.
DR   PDB; 7DR6; EM; 4.10 A; I/T=1-201.
DR   PDB; 7DR7; EM; 3.30 A; I/T=1-201.
DR   PDB; 7DRW; EM; 4.20 A; T/l=1-201.
DR   PDBsum; 1IRU; -.
DR   PDBsum; 7DR6; -.
DR   PDBsum; 7DR7; -.
DR   PDBsum; 7DRW; -.
DR   AlphaFoldDB; Q5E9K0; -.
DR   SMR; Q5E9K0; -.
DR   IntAct; Q5E9K0; 1.
DR   STRING; 9913.ENSBTAP00000003072; -.
DR   MEROPS; T01.984; -.
DR   PaxDb; Q5E9K0; -.
DR   PeptideAtlas; Q5E9K0; -.
DR   PRIDE; Q5E9K0; -.
DR   Ensembl; ENSBTAT00000070663; ENSBTAP00000058051; ENSBTAG00000002377.
DR   GeneID; 516919; -.
DR   KEGG; bta:516919; -.
DR   CTD; 5690; -.
DR   VEuPathDB; HostDB:ENSBTAG00000002377; -.
DR   VGNC; VGNC:33446; PSMB2.
DR   eggNOG; KOG0177; Eukaryota.
DR   GeneTree; ENSGT00640000091536; -.
DR   HOGENOM; CLU_035750_12_1_1; -.
DR   InParanoid; Q5E9K0; -.
DR   OMA; RMCTDEL; -.
DR   OrthoDB; 1392180at2759; -.
DR   TreeFam; TF106219; -.
DR   EvolutionaryTrace; Q5E9K0; -.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000002377; Expressed in granulosa cell and 105 other tissues.
DR   ExpressionAtlas; Q5E9K0; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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; ISS:UniProtKB.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR   CDD; cd03758; proteasome_beta_type_2; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR035206; Proteasome_beta2.
DR   InterPro; IPR016050; Proteasome_bsu_CS.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR023333; Proteasome_suB-type.
DR   PANTHER; PTHR11599:SF6; PTHR11599:SF6; 1.
DR   Pfam; PF00227; Proteasome; 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; Nucleus; Proteasome;
KW   Reference proteome.
FT   CHAIN           1..201
FT                   /note="Proteasome subunit beta type-2"
FT                   /id="PRO_0000239852"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P49721"
FT   STRAND          4..8
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   STRAND          10..18
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   STRAND          21..23
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   STRAND          26..31
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   STRAND          35..37
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   STRAND          39..49
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   HELIX           52..71
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   HELIX           77..92
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   STRAND          94..96
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   STRAND          100..108
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   TURN            109..111
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   STRAND          112..118
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   STRAND          124..126
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   STRAND          128..133
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   HELIX           134..146
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   HELIX           153..169
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   STRAND          171..173
FT                   /evidence="ECO:0007829|PDB:7DR7"
FT   STRAND          178..184
FT                   /evidence="ECO:0007829|PDB:1IRU"
FT   STRAND          187..189
FT                   /evidence="ECO:0007829|PDB:1IRU"
SQ   SEQUENCE   201 AA;  22896 MW;  8D195EBA1DBB02DE CRC64;
     MEYLIGIQGP DYVLVASDRV AASNIVQMKD DHDKMFKMSE KILLLCVGEA GDTVQFAEYI
     QKNVQLYKMR NGYELSPTAA ANFTRRNLAD YLRSRTPYHV NLLLAGYDEH EGPALYYMDY
     LAALAKAPFA AHGYGAFLTL SILDRYYTPT ISREKAVELL RKCLEELQKR FILNLPTFSV
     RIIDRNGIHD LDNISFPKQG S