PSB9_RAT
ID PSB9_RAT Reviewed; 219 AA.
AC P28077;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Proteasome subunit beta type-9;
DE EC=3.4.25.1;
DE AltName: Full=Low molecular mass protein 2;
DE AltName: Full=Macropain chain 7;
DE AltName: Full=Multicatalytic endopeptidase complex chain 7;
DE AltName: Full=Proteasome chain 7;
DE AltName: Full=Proteasome subunit beta-1i;
DE AltName: Full=Really interesting new gene 12 protein;
DE Flags: Precursor;
GN Name=Psmb9; Synonyms=Lmp2, Ring12;
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].
RX PubMed=1491007; DOI=10.1093/oxfordjournals.jbchem.a123933;
RA Tamura T., Shimbara N., Aki M., Ishida N., Bey F., Scherrer K., Tanaka K.,
RA Ichihara A.;
RT "Molecular cloning of cDNAs for rat proteasomes: deduced primary structures
RT of four other subunits.";
RL J. Biochem. 112:530-534(1992).
RN [2]
RP PROTEIN SEQUENCE OF 21-41.
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 [3]
RP INDUCTION BY THP, AND TISSUE SPECIFICITY.
RX PubMed=16988215; DOI=10.1095/biolreprod.106.053173;
RA Tengowski M.W., Feng D., Sutovsky M., Sutovsky P.;
RT "Differential expression of genes encoding constitutive and inducible 20S
RT proteasomal core subunits in the testis and epididymis of theophylline- or
RT 1,3-dinitrobenzene-exposed rats.";
RL Biol. Reprod. 76:149-163(2007).
CC -!- FUNCTION: The proteasome is a multicatalytic proteinase complex which
CC is characterized by its ability to cleave peptides with Arg, Phe, Tyr,
CC Leu, and Glu adjacent to the leaving group at neutral or slightly basic
CC pH. The proteasome has an ATP-dependent proteolytic activity. This
CC subunit is involved in antigen processing to generate class I binding
CC peptides.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of peptide bonds with very broad specificity.;
CC EC=3.4.25.1;
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC 19S regulatory subunits. The 20S proteasome core is composed of 28
CC subunits that are arranged in four stacked rings, resulting in a
CC barrel-shaped structure. The two end rings are each formed by seven
CC alpha subunits, and the two central rings are each formed by seven beta
CC subunits. The catalytic chamber with the active sites is on the inside
CC of the barrel. Component of the immunoproteasome, where it displaces
CC the equivalent housekeeping subunit PSMB6. Component of the
CC spermatoproteasome, a form of the proteasome specifically found in
CC testis. Interacts with NCOA2 and NCOA3 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}.
CC Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in the cytoplasmic lobe of elongated
CC spermatids, in residual bodies, and in the acrosomal cap of round
CC spermatids. {ECO:0000269|PubMed:16988215}.
CC -!- INDUCTION: Up-regulated by interferon gamma (at protein level). Up-
CC regulated by theophylline (THP), a reprotoxic agent thought to induce
CC infertility. {ECO:0000269|PubMed:16988215}.
CC -!- PTM: Autocleaved. The resulting N-terminal Thr residue of the mature
CC subunit is responsible for the nucleophile proteolytic activity.
CC {ECO:0000250|UniProtKB:O35955}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D10757; BAA01589.1; -; mRNA.
DR PIR; JX0231; JX0231.
DR PIR; S09088; S09088.
DR RefSeq; NP_036840.2; NM_012708.2.
DR AlphaFoldDB; P28077; -.
DR SMR; P28077; -.
DR STRING; 10116.ENSRNOP00000000532; -.
DR MEROPS; T01.013; -.
DR iPTMnet; P28077; -.
DR PhosphoSitePlus; P28077; -.
DR jPOST; P28077; -.
DR PaxDb; P28077; -.
DR PRIDE; P28077; -.
DR GeneID; 24967; -.
DR KEGG; rno:24967; -.
DR UCSC; RGD:3427; rat.
DR CTD; 5698; -.
DR RGD; 3427; Psmb9.
DR eggNOG; KOG0174; Eukaryota.
DR InParanoid; P28077; -.
DR OrthoDB; 1172133at2759; -.
DR PhylomeDB; P28077; -.
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:P28077; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000502; C:proteasome complex; IDA:RGD.
DR GO; GO:0005839; C:proteasome core complex; ISO:RGD.
DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
DR GO; GO:1990111; C:spermatoproteasome complex; ISS:UniProtKB.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0070628; F:proteasome binding; IDA:RGD.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0019882; P:antigen processing and presentation; ISO:RGD.
DR GO; GO:0071257; P:cellular response to electrical stimulus; IEP:RGD.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
DR GO; GO:0098586; P:cellular response to virus; IEP:RGD.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0014889; P:muscle atrophy; IEP:RGD.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:2000116; P:regulation of cysteine-type endopeptidase activity; ISO:RGD.
DR GO; GO:0043279; P:response to alkaloid; IEP:RGD.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR GO; GO:1901423; P:response to benzene; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0048536; P:spleen development; IEP:RGD.
DR GO; GO:0048538; P:thymus development; IEP:RGD.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR034383; Proteasome_beta9.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11599:SF50; PTHR11599:SF50; 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 Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase; Immunity;
KW Nucleus; Protease; Proteasome; Reference proteome; Threonine protease;
KW Zymogen.
FT PROPEP 1..20
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:2335214"
FT /id="PRO_0000026631"
FT CHAIN 21..219
FT /note="Proteasome subunit beta type-9"
FT /id="PRO_0000026632"
FT ACT_SITE 21
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 20..21
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:O35955"
FT MOD_RES 53
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P28065"
FT MOD_RES 109
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P28065"
SQ SEQUENCE 219 AA; 23324 MW; E713C94AF33836E4 CRC64;
MLQAGAPTAG SFRTGEVHTG TTIMAVEFDG GVVVGSDSRV SAGAAVVNRV FDKLSPLHQR
IYCALSGSAA DAQAIADMAA YQLELHGLEL EEPPLVLAAA NIVKNISYKY REDLLAHLMV
AGWDQHEGGQ VYGTMGGMLI RQPFAIGGSG STYIYGYVDA AYKPGMTPEE CRRFTTDAIT
LAMNRDGSSG GVIYLVTITA DGVDHRVILG DELPKFYDE
