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P17220 (PSA2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proteasome subunit alpha type-2

EC=3.4.25.1
Alternative name(s):
Macropain subunit C3
Multicatalytic endopeptidase complex subunit C3
Proteasome component C3
Gene names
Name:Psma2
OrganismRattus norvegicus (Rat) [Reference proteome]
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. CytoplasmP-body By similarity. Note: Colocalizes with TRIM5 in the cytoplasmic bodies By similarity. 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 residue701N6-acetyllysine By similarity
Modified residue761Phosphotyrosine 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 [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-30, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2.
Tissue: Liver.
[3]Lubec G., Afjehi-Sadat L.
Submitted (NOV-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 5-39 AND 71-84, IDENTIFICATION BY 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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-121, PHOSPHORYLATION AT TYR-121.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02897 mRNA. Translation: AAA40838.1.
PIRSNRTC3. A34535.
RefSeqNP_058975.1. NM_017279.1.
UniGeneRn.1617.

3D structure databases

ProteinModelPortalP17220.
SMRP17220. Positions 2-234.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248290. 5 interactions.
IntActP17220. 1 interaction.

Protein family/group databases

MEROPST01.972.

PTM databases

PhosphoSiteP17220.

2D gel databases

World-2DPAGE0004:P17220.

Proteomic databases

PRIDEP17220.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000073834; ENSRNOP00000066950; ENSRNOG00000049920.
GeneID29669.
KEGGrno:29669.
UCSCRGD:61842. rat.

Organism-specific databases

CTD5683.
RGD61842. Psma2.

Phylogenomic databases

GeneTreeENSGT00550000074870.
HOVERGENHBG003005.
KOK02726.
OMAWKATALG.
OrthoDBEOG71VSTG.
PhylomeDBP17220.

Gene expression databases

GenevestigatorP17220.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
InterProIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMSSF56235. SSF56235. 1 hit.
PROSITEPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio609987.
PROP17220.

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: June 11, 2014
This is version 126 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries