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Reviewed, UniProtKB/Swiss-Prot P17220 (PSA2_RAT)

Last modified February 9, 2010. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length234 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 Ref.4.

Tissue specificity

Ubiquitous.

Post-translational modification

Phosphorylated on tyrosine residues; which may be important for nuclear import. Ref.4

Sequence similarities

Belongs to the peptidase T1A family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 234233Proteasome subunit alpha type-2
PRO_0000124079

Amino acid modifications

Modified residue21N-acetylalanine Ref.2
Modified residue71Phosphoserine By similarity
Modified residue241Phosphotyrosine By similarity
Modified residue571Phosphotyrosine By similarity
Modified residue701N6-acetyllysine By similarity
Modified residue761Phosphotyrosine By similarity
Modified residue981Phosphotyrosine By similarity
Modified residue1211Phosphotyrosine Probable
Modified residue1711N6-acetyllysine By similarity

Experimental info

Mutagenesis1211Y → F: Abolishes nuclear localization and phosphorylation. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P17220-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 4ECB56A233583821

FASTA23425,927
        10         20         30         40         50         60 
MAERGYSFSL 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 

« Hide

References

[1]"Molecular cloning of cDNA for proteasomes from rat liver: primary structure of component C3 with a possible tyrosine phosphorylation site."
Tanaka K., Fujiwara T., Kumatori A., Shin S., Yoshimura T., Ichihara A., Tokunaga F., Aruga R., Iwanaga S., Kakizuka A., Nakanishi S.
Biochemistry 29:3777-3785(1990) [PubMed: 2340272] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: Wistar.
Tissue: Liver.
[2]"The NH2-terminal residues of rat liver proteasome (multicatalytic proteinase complex) subunits, C2, C3 and C8, are N alpha-acetylated."
Tokunaga F., Aruga R., Iwanaga S., Tanaka K., Ichihara A., Takao T., Shimonishi Y.
FEBS Lett. 263:373-375(1990) [PubMed: 2335242] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-30.
Tissue: Liver.
[3]Lubec G., Afjehi-Sadat L.
Submitted (NOV-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 5-39 AND 71-84, MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Spinal cord.
[4]"Nuclear multicatalytic proteinase subunit RRC3 is important for growth regulation in hepatocytes."
Benedict C.M., Clawson G.A.
Biochemistry 35:11612-11621(1996) [PubMed: 8794741] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-121, PHOSPHORYLATION AT TYR-121.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02897 mRNA. Translation: AAA40838.1.
IPIIPI00231757.
PIRSNRTC3. A34535.
RefSeqNP_058975.1.
UniGeneRn.1617

3D structure databases

SMRP17220. Positions 2-234.
ModBaseSearch...

Protein family/group databases

MEROPST01.972.

PTM databases

PhosphoSiteP17220.

Proteomic databases

PRIDEP17220.

Genome annotation databases

GeneID29669.
KEGGrno:29669.

Organism-specific databases

CTD29669.
RGD61842. Psma2.

Phylogenomic databases

eggNOGmaNOG09688.
HOVERGENP17220.
OrthoDBEOG9BK7P5.
PhylomeDBP17220.

Enzyme and pathway databases

BRENDA3.4.25.1. 248.

Gene expression databases

GenevestigatorP17220.

Family and domain databases

InterProIPR000426. Proteasome_asu_CS.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
PROSITEPS00388. PROTEASOME_A_1. 1 hit.
PS51475. PROTEASOME_A_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio609987.

Entry information

Entry namePSA2_RAT
AccessionPrimary (citable) accession number: P17220
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: February 9, 2010
This is version 96 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents