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P18420 (PSA1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 124. 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-1

EC=3.4.25.1
Alternative name(s):
Macropain subunit C2
Multicatalytic endopeptidase complex subunit C2
Proteasome component C2
Proteasome nu chain
Gene names
Name:Psma1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length263 AA.
Sequence statusComplete.
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. Mediates the lipopolysaccharide-induced signal macrophage proteasome. Might be involved in the anti-inflammatory response of macrophages during the interaction with C.albicans heat-inactivated cells 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. Interacts with NOTCH3 By similarity.

Subcellular location

Cytoplasm. Nucleus.

Tissue specificity

Ubiquitous.

Post-translational modification

Proteolytically cleaved from a C-terminal extension in the course of the conversion of the proteasome from its latent form into its active form.

Sequence similarities

Belongs to the peptidase T1A family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 263263Proteasome subunit alpha type-1
PRO_0000124064

Amino acid modifications

Modified residue11N-acetylmethionine Ref.3
Modified residue141Phosphoserine By similarity
Glycosylation1101O-linked (GlcNAc) By similarity
Cross-link115Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link208Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Sequences

Sequence LengthMass (Da)Tools
P18420 [UniParc].

Last modified February 1, 1991. Version 2.
Checksum: 68660696B43A4051

FASTA26329,518
        10         20         30         40         50         60 
MFRNQYDNDV TVWSPQGRIH QIEYAMEAVK QGSATVGLKS KTHAVLVALK RAQSELAAHQ 

        70         80         90        100        110        120 
KKILHVDNHI GISIAGLTAD ARLLCNFMRQ ECLDSRFVFD RPLPVSRLVS LIGSKTQIPT 

       130        140        150        160        170        180 
QRYGRRPYGV GLLIAGYDDM GPHVFQTCPS ANYFDCRAMS IGARSQSART YLERHMSEFM 

       190        200        210        220        230        240 
QCNLDELVKH GLRALRETLP AEQDLTTKNV SIGIVGKDLE FTIYDDDDVS PFLDGLEERP 

       250        260 
QRKAQPSQAA DEPAEKADEP MEH 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of cDNA for proteasomes (multicatalytic proteinase complexes) from rat liver: primary structure of the largest component (C2)."
Fujiwara T., Tanaka K., Kumatori A., Shin S., Yoshimura T., Ichihara A., Tokunaga F., Aruga R., Iwanaga S., Kakizuka A., Nakanishi S.
Biochemistry 28:7332-7340(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.
[2]"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: Pituitary.
[3]"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 1-30, ACETYLATION AT MET-1.
Tissue: Liver.
[4]Lubec G., Chen W.-Q.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 63-82 AND 97-107, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M29859 mRNA. Translation: AAA41943.1.
D90265 mRNA. Translation: BAA14312.1.
BC062233 mRNA. Translation: AAH62233.1.
PIRSNRTC2. A32968.
RefSeqNP_058974.1. NM_017278.1.
UniGeneRn.2668.

3D structure databases

ProteinModelPortalP18420.
SMRP18420. Positions 4-241.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248289. 1 interaction.
IntActP18420. 1 interaction.
STRING10116.ENSRNOP00000015946.

Protein family/group databases

MEROPST01.976.

2D gel databases

World-2DPAGE0004:P18420.

Proteomic databases

PaxDbP18420.
PRIDEP18420.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000015946; ENSRNOP00000015946; ENSRNOG00000011745.
GeneID29668.
KEGGrno:29668.
UCSCRGD:61841. rat.

Organism-specific databases

CTD5682.
RGD61841. Psma1.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00550000074855.
HOGENOMHOG000091080.
HOVERGENHBG105373.
InParanoidP18420.
KOK02725.
OMAFMKQQCL.
OrthoDBEOG7WQ7T1.
PhylomeDBP18420.
TreeFamTF106206.

Gene expression databases

GenevestigatorP18420.

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

NextBio609983.
PROP18420.

Entry information

Entry namePSA1_RAT
AccessionPrimary (citable) accession number: P18420
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: February 1, 1991
Last modified: June 11, 2014
This is version 124 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