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Q5E987 (PSA5_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 80. 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-5

EC=3.4.25.1
Gene names
Name:PSMA5
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length241 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 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. PSMA5 interacts directly with the PSMG1-PSMG2 heterodimer which promotes 20S proteasome assembly.

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 – 241241Proteasome subunit alpha type-5
PRO_0000274033

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue161Phosphoserine By similarity
Modified residue551Phosphothreonine By similarity
Modified residue561Phosphoserine By similarity
Glycosylation1981O-linked (GlcNAc) By similarity

Secondary structure

.................................. 241
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q5E987 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 5610CDA00469120A

FASTA24126,411
        10         20         30         40         50         60 
MFLTRSEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGI QTSEGVCLAV EKRITSPLME 

        70         80         90        100        110        120 
PSSIEKIVEI DAHIGCAMSG LIADAKTLID KARVETQNHW FTYNETMTVE SVTQAVSNLA 

       130        140        150        160        170        180 
LQFGEEDADP GAMSRPFGVA LLFGGVDEKG PQLFHMDPSG TFVQCDARAI GSASEGAQSS 

       190        200        210        220        230        240 
LQEVYHKSMT LKEAIKSSLI ILKQVMEEKL NATNIELATV QPGQNFHMFT KEELEEVIKD 


I 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]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.
[3]"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
BT021033 mRNA. Translation: AAX09050.1.
BC102343 mRNA. Translation: AAI02344.1.
RefSeqNP_001015566.1. NM_001015566.1.
UniGeneBt.47769.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IRUX-ray2.75E/S1-241[»]
ProteinModelPortalQ5E987.
SMRQ5E987. Positions 9-241.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000027507.

Protein family/group databases

MEROPST01.975.

Proteomic databases

PaxDbQ5E987.
PRIDEQ5E987.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000027507; ENSBTAP00000027507; ENSBTAG00000020641.
GeneID510155.
KEGGbta:510155.

Organism-specific databases

CTD5686.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00550000074958.
HOGENOMHOG000091085.
HOVERGENHBG003005.
InParanoidQ5E987.
KOK02729.
OMACAMSGLT.
OrthoDBEOG769ZKB.
TreeFamTF106211.

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

EvolutionaryTraceQ5E987.
NextBio20869301.

Entry information

Entry namePSA5_BOVIN
AccessionPrimary (citable) accession number: Q5E987
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: March 15, 2005
Last modified: June 11, 2014
This is version 80 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