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P18422 (PSA3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 125. 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-3

EC=3.4.25.1
Alternative name(s):
Macropain subunit C8
Multicatalytic endopeptidase complex subunit C8
Proteasome component C8
Proteasome subunit K
Gene names
Name:Psma3
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length255 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.

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. Interacts with AURKB By similarity.

Subcellular location

Cytoplasm. Nucleus.

Tissue specificity

Ubiquitous.

Sequence similarities

Belongs to the peptidase T1A family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 255254Proteasome subunit alpha type-3
PRO_0000124093

Amino acid modifications

Modified residue21N-acetylserine Ref.4
Modified residue571N6-acetyllysine By similarity
Modified residue2061N6-acetyllysine By similarity
Modified residue2301N6-acetyllysine By similarity
Modified residue2431Phosphoserine By similarity
Modified residue2501Phosphoserine Ref.6

Sequences

Sequence LengthMass (Da)Tools
P18422 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: F07FCB33A2E79FA7

FASTA25528,419
        10         20         30         40         50         60 
MSSIGTGYDL SASTFSPDGR VFQVEYAMKA VENSSTAIGI RCKDGVVFGV EKLVLSKLYE 

        70         80         90        100        110        120 
EGSNKRLFNV DRHVGMAVAG LLADARSLAD IAREEASNFR SNFGYNIPLK HLADRVAMYV 

       130        140        150        160        170        180 
HAYTLYSAVR PFGCSFMLGS YSVNDGAQLY MIDPSGVSYG YWGCAIGKAR QAAKTEIEKL 

       190        200        210        220        230        240 
QMKEMTCRDV VKEVAKIIYI VHDEVKDKAF ELELSWVGEL TKGRHEIVPK DVREEAEKYA 

       250 
KESLKEEDES DDDNM 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of cDNAs for two subunits of rat multicatalytic proteinase. Existence of N-terminal conserved and C-terminal diverged sequences among subunits."
Sorimachi H., Tsukahara T., Kawasaki H., Ishiura S., Emori Y., Sugita H., Suzuki K.
Eur. J. Biochem. 193:775-781(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.
[2]"cDNA cloning and sequencing of component C8 of proteasomes from rat hepatoma cells."
Tanaka K., Kanayama H., Tamura T., Lee D.H., Kumatori A., Fujiwara T., Ichihara A., Tokunaga F., Aruga R., Iwanaga S.
Biochem. Biophys. Res. Commun. 171:676-683(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[4]"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 2-29, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2.
Tissue: Liver.
[5]Lubec G., Chen W.-Q.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 30-41; 44-52; 67-93; 101-110 AND 197-206, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus.
[6]"Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X55985 mRNA. Translation: CAA39457.1.
D90258 mRNA. Translation: BAA14302.1.
M58593 mRNA. Translation: AAA40840.1.
BC081817 mRNA. Translation: AAH81817.1.
PIRSNRTC8. S14004.
RefSeqNP_001004094.1. NM_001004094.1.
NP_058976.1. NM_017280.2.
UniGeneRn.3997.

3D structure databases

ProteinModelPortalP18422.
SMRP18422. Positions 2-246.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248291. 1 interaction.
STRING10116.ENSRNOP00000010753.

Protein family/group databases

MEROPST01.977.

PTM databases

PhosphoSiteP18422.

2D gel databases

World-2DPAGE0004:P18422.

Proteomic databases

PaxDbP18422.
PRIDEP18422.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000010753; ENSRNOP00000010753; ENSRNOG00000007851.
GeneID29670.
408248.
KEGGrno:29670.
rno:408248.
UCSCRGD:61844. rat.

Organism-specific databases

CTD408248.
5684.
RGD61844. Psma3.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00550000074912.
HOGENOMHOG000091086.
HOVERGENHBG105566.
InParanoidP18422.
KOK02727.
OMAVPDGRHF.
OrthoDBEOG73JKW6.
PhylomeDBP18422.
TreeFamTF106208.

Gene expression databases

GenevestigatorP18422.

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

NextBio609991.
PROP18422.

Entry information

Entry namePSA3_RAT
AccessionPrimary (citable) accession number: P18422
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 125 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