UniProt functional annotation for P28063



	UniProt functional annotation for P28063

UniProt code: P28063.

Organism: Mus musculus (Mouse).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.

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. May participate in the inflammatory response pathway. Required for adipocyte differentiation (PubMed:21881205, PubMed:22341445, PubMed:8066463). May be involved in the generation of spliced peptides resulting from the ligation of two separate proteasomal cleavage products that are not contiguous in the parental protein (By similarity). {ECO:0000250|UniProtKB:P28062, ECO:0000269|PubMed:21881205, ECO:0000269|PubMed:22341445, ECO:0000269|PubMed:8066463}.

Catalytic activity: Reaction=Cleavage of peptide bonds with very broad specificity.; EC=3.4.25.1;

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 housekeeping subunit PSMB5. Component of the spermatoproteasome, a form of the proteasome specifically found in testis. Directly interacts with POMP. Interacts with TAP1. {ECO:0000269|PubMed:16857966, ECO:0000269|PubMed:22341445, ECO:0000269|PubMed:23706739}.

Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}.

Tissue specificity: Detected in liver (at protein level). Expressed in spleen, thymus, lung, liver, heart and, at a very low level, in kidney. Not expressed in brain nor testis. {ECO:0000269|PubMed:22341445, ECO:0000269|PubMed:8406612}.

Induction: Up-regulated by interferon gamma (at protein level). Up- regulated by IRF1. Down-regulated in spleen by deoxynivalenol (DON), a mycotoxin that alters immune functions. Down-regulated by the selective inhibitor PR-957. Up-regulated by heat shock treatment. Down-regulated by EGR1 in neuronal cells. {ECO:0000269|PubMed:15371230, ECO:0000269|PubMed:15907481, ECO:0000269|PubMed:16452686, ECO:0000269|PubMed:17142736, ECO:0000269|PubMed:19525961}.

Ptm: Autocleaved. The resulting N-terminal Thr residue of the mature subunit is responsible for the nucleophile proteolytic activity. {ECO:0000250|UniProtKB:O35955}.

Polymorphism: The allele, LMP7k/LMP7s/LMPf/LMP7r/LMPcas4/LMPg7 found in strains NMRI, B10.BR, SJL, A.CA, B10.RIII, B10.cas4 and NOD may be post-translationally modified. Allele LMP7q is found in strain DBA/1J. {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8854085}.

Similarity: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE- ProRule:PRU00809}.

Sequence caution: Sequence=CAA45780.1; Type=Erroneous initiation; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Mus musculus (Mouse).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus.



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. May participate in the inflammatory response pathway. Required for adipocyte differentiation (PubMed:21881205, PubMed:22341445, PubMed:8066463). May be involved in the generation of spliced peptides resulting from the ligation of two separate proteasomal cleavage products that are not contiguous in the parental protein (By similarity). {ECO:0000250\|UniProtKB:P28062, ECO:0000269\|PubMed:21881205, ECO:0000269\|PubMed:22341445, ECO:0000269\|PubMed:8066463}.


Catalytic activity:		Reaction=Cleavage of peptide bonds with very broad specificity.; EC=3.4.25.1;
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 housekeeping subunit PSMB5. Component of the spermatoproteasome, a form of the proteasome specifically found in testis. Directly interacts with POMP. Interacts with TAP1. {ECO:0000269\|PubMed:16857966, ECO:0000269\|PubMed:22341445, ECO:0000269\|PubMed:23706739}.
Subcellular location:		Cytoplasm {ECO:0000255\|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}.
Tissue specificity:		Detected in liver (at protein level). Expressed in spleen, thymus, lung, liver, heart and, at a very low level, in kidney. Not expressed in brain nor testis. {ECO:0000269\|PubMed:22341445, ECO:0000269\|PubMed:8406612}.
Induction:		Up-regulated by interferon gamma (at protein level). Up- regulated by IRF1. Down-regulated in spleen by deoxynivalenol (DON), a mycotoxin that alters immune functions. Down-regulated by the selective inhibitor PR-957. Up-regulated by heat shock treatment. Down-regulated by EGR1 in neuronal cells. {ECO:0000269\|PubMed:15371230, ECO:0000269\|PubMed:15907481, ECO:0000269\|PubMed:16452686, ECO:0000269\|PubMed:17142736, ECO:0000269\|PubMed:19525961}.
Ptm:		Autocleaved. The resulting N-terminal Thr residue of the mature subunit is responsible for the nucleophile proteolytic activity. {ECO:0000250\|UniProtKB:O35955}.
Polymorphism:		The allele, LMP7k/LMP7s/LMPf/LMP7r/LMPcas4/LMPg7 found in strains NMRI, B10.BR, SJL, A.CA, B10.RIII, B10.cas4 and NOD may be post-translationally modified. Allele LMP7q is found in strain DBA/1J. {ECO:0000269\|PubMed:15489334, ECO:0000269\|PubMed:8854085}.
Similarity:		Belongs to the peptidase T1B family. {ECO:0000255\|PROSITE- ProRule:PRU00809}.
Sequence caution:		Sequence=CAA45780.1; Type=Erroneous initiation; Evidence={ECO:0000305};