PSB7_PIG
ID PSB7_PIG Reviewed; 277 AA.
AC A1XQU1; A2BD06;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Proteasome subunit beta type-7;
DE EC=3.4.25.1;
DE Flags: Precursor;
GN Name=PSMB7;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Large white X Duroc;
RX PubMed=17416745; DOI=10.1101/gr.6085507;
RA Mikawa S., Morozumi T., Shimanuki S., Hayashi T., Uenishi H., Domukai M.,
RA Okumura N., Awata T.;
RT "Fine mapping of a swine quantitative trait locus for number of vertebrae
RT and analysis of an orphan nuclear receptor, germ cell nuclear factor
RT (NR6A1).";
RL Genome Res. 17:586-593(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Longissimus dorsi muscle;
RA Cai G., Chen Y., Wang C., Li J., Peng G., Zhang H.;
RT "Generation and analysis of cDNA sequences derived from a porcine skeletal
RT muscle library.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
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; AP009124; BAF45330.1; -; Genomic_DNA.
DR EMBL; DQ629163; ABK55647.1; -; mRNA.
DR RefSeq; NP_001090945.1; NM_001097476.2.
DR AlphaFoldDB; A1XQU1; -.
DR SMR; A1XQU1; -.
DR STRING; 9823.ENSSSCP00000005987; -.
DR MEROPS; T01.A02; -.
DR PaxDb; A1XQU1; -.
DR PeptideAtlas; A1XQU1; -.
DR PRIDE; A1XQU1; -.
DR Ensembl; ENSSSCT00000006146; ENSSSCP00000005987; ENSSSCG00000005590.
DR Ensembl; ENSSSCT00005030855; ENSSSCP00005018813; ENSSSCG00005019410.
DR Ensembl; ENSSSCT00015051387; ENSSSCP00015020488; ENSSSCG00015038634.
DR Ensembl; ENSSSCT00025044892; ENSSSCP00025019123; ENSSSCG00025032983.
DR Ensembl; ENSSSCT00030063964; ENSSSCP00030029283; ENSSSCG00030045812.
DR Ensembl; ENSSSCT00035103157; ENSSSCP00035044083; ENSSSCG00035075860.
DR Ensembl; ENSSSCT00040004265; ENSSSCP00040001344; ENSSSCG00040003399.
DR Ensembl; ENSSSCT00045056977; ENSSSCP00045039811; ENSSSCG00045033321.
DR Ensembl; ENSSSCT00050059764; ENSSSCP00050025675; ENSSSCG00050043910.
DR Ensembl; ENSSSCT00055056067; ENSSSCP00055044780; ENSSSCG00055028272.
DR Ensembl; ENSSSCT00060106265; ENSSSCP00060046886; ENSSSCG00060077220.
DR Ensembl; ENSSSCT00065029729; ENSSSCP00065012149; ENSSSCG00065022341.
DR Ensembl; ENSSSCT00070033400; ENSSSCP00070027903; ENSSSCG00070016952.
DR GeneID; 100037992; -.
DR KEGG; ssc:100037992; -.
DR CTD; 5695; -.
DR VGNC; VGNC:91909; PSMB7.
DR eggNOG; KOG0173; Eukaryota.
DR GeneTree; ENSGT00940000157419; -.
DR HOGENOM; CLU_035750_3_0_1; -.
DR InParanoid; A1XQU1; -.
DR OMA; VDKTGPH; -.
DR OrthoDB; 977476at2759; -.
DR TreeFam; TF106222; -.
DR Reactome; R-SSC-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-SSC-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-SSC-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-SSC-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-SSC-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-SSC-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-SSC-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-SSC-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-SSC-202424; Downstream TCR signaling.
DR Reactome; R-SSC-2467813; Separation of Sister Chromatids.
DR Reactome; R-SSC-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-SSC-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-SSC-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-SSC-382556; ABC-family proteins mediated transport.
DR Reactome; R-SSC-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-SSC-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-SSC-4641257; Degradation of AXIN.
DR Reactome; R-SSC-4641258; Degradation of DVL.
DR Reactome; R-SSC-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-SSC-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-SSC-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-SSC-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-SSC-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-SSC-5632684; Hedgehog 'on' state.
DR Reactome; R-SSC-5658442; Regulation of RAS by GAPs.
DR Reactome; R-SSC-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-SSC-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-SSC-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-SSC-5689603; UCH proteinases.
DR Reactome; R-SSC-5689880; Ub-specific processing proteases.
DR Reactome; R-SSC-6798695; Neutrophil degranulation.
DR Reactome; R-SSC-68867; Assembly of the pre-replicative complex.
DR Reactome; R-SSC-68949; Orc1 removal from chromatin.
DR Reactome; R-SSC-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-SSC-69481; G2/M Checkpoints.
DR Reactome; R-SSC-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-SSC-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-SSC-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-SSC-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-SSC-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-SSC-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-SSC-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-SSC-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-SSC-8951664; Neddylation.
DR Reactome; R-SSC-9020702; Interleukin-1 signaling.
DR Reactome; R-SSC-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-SSC-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-SSC-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR Proteomes; UP000008227; Chromosome 1.
DR Proteomes; UP000314985; Chromosome 1.
DR Bgee; ENSSSCG00000005590; Expressed in hindlimb bud and 45 other tissues.
DR ExpressionAtlas; A1XQU1; baseline and differential.
DR Genevisible; A1XQU1; SS.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; 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: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 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Nucleus; Protease; Proteasome; Reference proteome;
KW Threonine protease; Zymogen.
FT PROPEP 1..43
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000311176"
FT CHAIN 44..277
FT /note="Proteasome subunit beta type-7"
FT /id="PRO_0000311177"
FT ACT_SITE 44
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CONFLICT 229
FT /note="L -> F (in Ref. 2; ABK55647)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 277 AA; 29980 MW; D8DFC5B018F6F287 CRC64;
MAAVSVYERP VGGFSFDNCR RNAILEADFA KKGYKLPTAR KTGTTIAGVV YKDGIVLGAD
TRATEGMVVA DKNCSKIHFI SPNIYCCGAG TAADTDMTTQ LISSNLELHS LSTGRLPRVV
TANRMLKQML FRYQGYIGAA LVLGGVDVTG PHLYSIYPHG STDKLPYVTM GSGSLAAMAV
FEDKFRPEME EEEAKQLVSE AIAAGIFNDL GSGSNIDLCV ISKSKLDFLR PYSVPNKKGT
RFGRYRCEKG TTAVLTEKVT ALDIEVLEET VQTMDTS
