Reviewed, UniProtKB/Swiss-Prot P49722 (PSA2_MOUSE)

Names and origin

Protein names

Recommended name:
    Proteasome subunit alpha type-2
    EC=3.4.25.1
Alternative name(s):
    Proteasome component C3
    Macropain subunit C3
    Multicatalytic endopeptidase complex subunit C3

Gene names

Name:	Psma2
Synonyms:	Lmpc3

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	234 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

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. PSMA2 may have a potential regulatory effect on another component(s) of the proteasome complex through tyrosine phosphorylation.
Catalytic activity	Cleavage of peptide bonds with very broad specificity.
Subunit structure	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.
Subcellular location	Cytoplasm. Nucleus.
Post-translational modification	Phosphorylated on tyrosine residues; which may be important for nuclear import By similarity.
Sequence similarities	Belongs to the peptidase T1A family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus Proteasome
Molecular function	Hydrolase Protease Threonine protease
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell proteasome core complex Inferred from electronic annotation. Source: InterPro
Molecular function	threonine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 234	233	Proteasome subunit alpha type-2		PRO_0000124078
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	24	1	Phosphotyrosine By similarity
	Modified residue	57	1	Phosphotyrosine By similarity
	Modified residue	70	1	N6-acetyllysine By similarity
	Modified residue	76	1	Phosphotyrosine Ref.3
	Modified residue	98	1	Phosphotyrosine By similarity
	Modified residue	121	1	Phosphotyrosine By similarity
	Modified residue	171	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P49722-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 0E1D5BC52F29FF3F	FASTA	234	25,926
	10 20 30 40 50 60 MAKRGYSFSL TTFSPSGKLV QIEYALAAVA GGAPSVGIKA ANGVVLATEK KQKSILYDER 70 80 90 100 110 120 SVHKVEPITK HIGLVYSGMG PDYRVLVHRA RKLAQQYYLV YQEPIPTAQL VQRVASVMQE 130 140 150 160 170 180 YTQSGGVRPF GVSLLICGWN EGRPYLFQSD PSGAYFAWKA TAMGKNYVNG KTFLEKRYNE 190 200 210 220 230 DLELEDAIHT AILTLKESFE GQMTEDNIEV GICNEAGFRR LTPTEVRDYL AAIA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of mouse proteasome subunit MC3 and identification of proteasome subtypes with different cleavage characteristics. Proteasome subunits, proteasome subpopulations." Seelig A., Boes B., Kloetzel P.-M. Enzyme Protein 47:330-342(1993) [PubMed: 7697131] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 5-39; 71-84; 93-113 AND 178-196, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain and Hippocampus.
[3]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-76, MASS SPECTROMETRY. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X70303 mRNA. Translation: CAA49782.1.
IPI	IPI00890001.
UniGene	Mm.252255
3D structure databases
HSSP	HSSP built from PDB template 1RYP based on UniProtKB P23639.
ModBase	Search...
Protein-protein interaction databases
STRING	P49722.
Protein family/group databases
MEROPS	T01.972.
PTM databases
PhosphoSite	P49722.
2-D gel databases
SWISS-2DPAGE	P49722.
REPRODUCTION-2DPAGE	P49722.
Proteomic databases
PRIDE	P49722.
Genome annotation databases
Ensembl	ENSMUST00000082305; ENSMUSP00000106140; ENSMUSG00000015671; Mus musculus. [Genome view]
Organism-specific databases
MGI	MGI:104885. Psma2.
Phylogenomic databases
HOVERGEN	P49722.
Enzyme and pathway databases
BRENDA	3.4.25.1. 244.
Gene expression databases
ArrayExpress	P49722.
Bgee	P49722.
Genevestigator	P49722.
GermOnline	ENSMUSG00000015671. Mus musculus.
Family and domain databases
InterPro	IPR000426. Proteasome_asu_CS. IPR001353. Proteasome_sua/b. [Graphical view]
Pfam	PF00227. Proteasome. 1 hit. PF10584. Proteasome_A_N. 1 hit. [Graphical view]
PROSITE	PS00388. PROTEASOME_A. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

PSA2_MOUSE

Accession

Primary (citable) accession number: P49722

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	October 13, 2009
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)