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Q3T0X5 (PSA1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Gene names
Name:PSMA1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

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.

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

Chain1 – 263263Proteasome subunit alpha type-1
PRO_0000274031

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
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

Secondary structure

..................................... 263
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q3T0X5 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 24142C5BCEFE8DED

FASTA26329,586
        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 GPHIFQTCPS ANYFDCRAMS IGARSQSART YLERHMSEFM 

       190        200        210        220        230        240 
ECNLNELVKH GLRALRETLP AEQDLTTKNV SIGIVGKDLE FTIYDDDDVS PFLEGLEERP 

       250        260 
QRKAQPTQPA DEPAEKADEP MEH 

« Hide

References

« Hide 'large scale' references
[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Ileum.
[2]"The structure of the mammalian 20S proteasome at 2.75 A resolution."
Unno M., Mizushima T., Morimoto Y., Tomisugi Y., Tanaka K., Yasuoka N., Tsukihara T.
Structure 10:609-618(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF COMPLEX WITH THE 20S PROTEASOME.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC102216 mRNA. Translation: AAI02217.1.
RefSeqNP_001030387.1. NM_001035310.2.
UniGeneBt.23202.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IRUX-ray2.75F/T1-263[»]
ProteinModelPortalQ3T0X5.
SMRQ3T0X5. Positions 4-241.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000008621.

Protein family/group databases

MEROPST01.976.

Proteomic databases

PaxDbQ3T0X5.
PRIDEQ3T0X5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000008621; ENSBTAP00000008621; ENSBTAG00000006564.
GeneID515503.
KEGGbta:515503.

Organism-specific databases

CTD5682.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00550000074855.
HOGENOMHOG000091080.
HOVERGENHBG105373.
InParanoidQ3T0X5.
KOK02725.
OMAFMKQQCL.
OrthoDBEOG7WQ7T1.
TreeFamTF106206.

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

EvolutionaryTraceQ3T0X5.
NextBio20871856.

Entry information

Entry namePSA1_BOVIN
AccessionPrimary (citable) accession number: Q3T0X5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: October 11, 2005
Last modified: June 11, 2014
This is version 75 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references