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Proteasome subunit beta type-9 (EC 3.4.25.1) (Low molecular mass protein 2) (Macropain chain 7) (Multicatalytic endopeptidase complex chain 7) (Proteasome chain 7) (Proteasome subunit beta-1i) (Really interesting new gene 12 protein)

 PSB9_RAT                Reviewed;         219 AA.
P28077;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 2.
22-NOV-2017, entry version 132.
RecName: Full=Proteasome subunit beta type-9;
EC=3.4.25.1;
AltName: Full=Low molecular mass protein 2;
AltName: Full=Macropain chain 7;
AltName: Full=Multicatalytic endopeptidase complex chain 7;
AltName: Full=Proteasome chain 7;
AltName: Full=Proteasome subunit beta-1i;
AltName: Full=Really interesting new gene 12 protein;
Flags: Precursor;
Name=Psmb9; Synonyms=Lmp2, Ring12;
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].
PubMed=1491007; DOI=10.1093/oxfordjournals.jbchem.a123933;
Tamura T., Shimbara N., Aki M., Ishida N., Bey F., Scherrer K.,
Tanaka K., Ichihara A.;
"Molecular cloning of cDNAs for rat proteasomes: deduced primary
structures of four other subunits.";
J. Biochem. 112:530-534(1992).
[2]
PROTEIN SEQUENCE OF 21-41.
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).
[3]
INDUCTION BY THP, AND TISSUE SPECIFICITY.
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: The proteasome is a multicatalytic proteinase complex
which is characterized by its ability to cleave peptides with Arg,
Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or
slightly basic pH. The proteasome has an ATP-dependent proteolytic
activity. This subunit is involved in antigen processing to
generate class I binding peptides.
-!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
specificity.
-!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and
two 19S regulatory subunits. The 20S proteasome core is composed
of 28 subunits that are arranged in four stacked rings, resulting
in a barrel-shaped structure. The two end rings are each formed by
seven alpha subunits, and the two central rings are each formed by
seven beta subunits. The catalytic chamber with the active sites
is on the inside of the barrel. Component of the immunoproteasome,
where it displaces the equivalent houskeeping subunit PSMB6.
Component of the spermatoproteasome, a form of the proteasome
specifically found in testis. Interacts with NCOA2 and NCOA3 (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-
ProRule:PRU00809}. Nucleus {ECO:0000250}.
-!- TISSUE SPECIFICITY: Detected in the cytoplasmic lobe of elongated
spermatids, in residual bodies, and in the acrosomal cap of round
spermatids. {ECO:0000269|PubMed:16988215}.
-!- INDUCTION: Up-regulated by interferon gamma (at protein level).
Up-regulated by theophylline (THP), a reprotoxic agent thought to
induce infertility. {ECO:0000269|PubMed:16988215}.
-!- PTM: Autocleaved. The resulting N-terminal Thr residue of the
mature subunit is responsible for the nucleophile proteolytic
activity. {ECO:0000250|UniProtKB:O35955}.
-!- SIMILARITY: Belongs to the peptidase T1B family.
{ECO:0000255|PROSITE-ProRule:PRU00809}.
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EMBL; D10757; BAA01589.1; -; mRNA.
PIR; JX0231; JX0231.
PIR; S09088; S09088.
RefSeq; NP_036840.2; NM_012708.2.
UniGene; Rn.13686; -.
ProteinModelPortal; P28077; -.
SMR; P28077; -.
STRING; 10116.ENSRNOP00000000532; -.
MEROPS; T01.013; -.
iPTMnet; P28077; -.
PhosphoSitePlus; P28077; -.
PaxDb; P28077; -.
PRIDE; P28077; -.
GeneID; 24967; -.
KEGG; rno:24967; -.
UCSC; RGD:3427; rat.
CTD; 5698; -.
RGD; 3427; Psmb9.
eggNOG; KOG0174; Eukaryota.
eggNOG; ENOG410XS23; LUCA.
HOGENOM; HOG000091079; -.
HOVERGEN; HBG000123; -.
InParanoid; P28077; -.
KO; K02741; -.
PhylomeDB; P28077; -.
PRO; PR:P28077; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0000502; C:proteasome complex; IDA:RGD.
GO; GO:0005839; C:proteasome core complex; ISO:RGD.
GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
GO; GO:1990111; C:spermatoproteasome complex; ISS:UniProtKB.
GO; GO:0070628; F:proteasome binding; IDA:RGD.
GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0019882; P:antigen processing and presentation; ISO:RGD.
GO; GO:0071257; P:cellular response to electrical stimulus; IEP:RGD.
GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
GO; GO:0098586; P:cellular response to virus; IEP:RGD.
GO; GO:0001889; P:liver development; IEP:RGD.
GO; GO:0014889; P:muscle atrophy; IEP:RGD.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IEA:InterPro.
GO; GO:2000116; P:regulation of cysteine-type endopeptidase activity; ISO:RGD.
GO; GO:0043279; P:response to alkaloid; IEP:RGD.
GO; GO:1901423; P:response to benzene; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0048536; P:spleen development; IEP:RGD.
GO; GO:0048538; P:thymus development; IEP:RGD.
Gene3D; 3.60.20.10; -; 1.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR000243; Pept_T1A_subB.
InterPro; IPR034383; Proteasome_beta9.
InterPro; IPR016050; Proteasome_bsu_CS.
InterPro; IPR001353; Proteasome_sua/b.
InterPro; IPR023333; Proteasome_suB-type.
PANTHER; PTHR11599:SF50; PTHR11599:SF50; 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;
Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
Hydrolase; Immunity; Nucleus; Protease; Proteasome;
Reference proteome; Threonine protease; Zymogen.
PROPEP 1 20 Removed in mature form.
{ECO:0000269|PubMed:2335214}.
/FTId=PRO_0000026631.
CHAIN 21 219 Proteasome subunit beta type-9.
/FTId=PRO_0000026632.
ACT_SITE 21 21 Nucleophile. {ECO:0000250}.
SITE 20 21 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:O35955}.
MOD_RES 53 53 N6-acetyllysine.
{ECO:0000250|UniProtKB:P28065}.
MOD_RES 109 109 N6-acetyllysine.
{ECO:0000250|UniProtKB:P28065}.
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


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