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P24495 (PSA2_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 99. 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
Short name=xC3
Proteasome component C3
Gene names
Name:psma2
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length234 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

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 By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Sequence similarities

Belongs to the peptidase T1A family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 234233Proteasome subunit alpha type-2
PRO_0000124080

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue1211Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
P24495 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: DAD6E27698410FA2

FASTA23425,834
        10         20         30         40         50         60 
MAERGYSFSL TTFSPSGKLV QIEYALAAVA AGAPSVGIKA TNGVVLATEK KQKSILYDEQ 

        70         80         90        100        110        120 
SAHKVEPITK HIGMVYSGMG PDYRVLVRRA RKLAQQYYLV YQEPIPTAQL VQRVASVMQE 

       130        140        150        160        170        180 
YTQSGGVRPF GVSLLIAGWD EGRPYLFQSD PSGAYFAWKA TAMGKNYVNG KTFLEKRYNE 

       190        200        210        220        230 
DLELEDAIHT AILTLKESFE GQMTEDNIEV GICNEAGFKR LTPAEVKDYL AAIA 

« Hide

References

« Hide 'large scale' references
[1]"Deduced primary structure of a Xenopus proteasome subunit XC3 and expression of its mRNA during early development."
Fujii G., Tashiro K., Emori Y., Saigo K., Tanaka K., Shiokawa K.
Biochem. Biophys. Res. Commun. 178:1233-1239(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]NIH - Xenopus Gene Collection (XGC) project
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S51111 mRNA. Translation: AAB19485.1.
BC072254 mRNA. Translation: AAH72254.1.
PIRJH0421.
RefSeqNP_001084053.1. NM_001090584.1.
UniGeneXl.2546.

3D structure databases

ProteinModelPortalP24495.
SMRP24495. Positions 2-234.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPST01.972.

Proteomic databases

PRIDEP24495.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID399279.
KEGGxla:399279.

Organism-specific databases

CTD5683.
XenbaseXB-GENE-964716. psma2.

Phylogenomic databases

HOVERGENHBG003005.
KOK02726.

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...

Entry information

Entry namePSA2_XENLA
AccessionPrimary (citable) accession number: P24495
Secondary accession number(s): Q6INM4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 99 of the entry and version 2 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