Reviewed, UniProtKB/Swiss-Prot Q9Z2U1 (PSA5_MOUSE)

Names and origin

Protein names

Recommended name:
    Proteasome subunit alpha type-5
    EC=3.4.25.1
Alternative name(s):
    Proteasome zeta chain
    Macropain zeta chain
    Multicatalytic endopeptidase complex zeta chain

Gene names

Name:

Psma5

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	241 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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. PSMA5 interacts directly with the PSMG1-PSMG2 heterodimer which promotes 20S proteasome assembly By similarity.
Subcellular location	Cytoplasm. Nucleus.
Sequence similarities	Belongs to the peptidase T1A family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus Proteasome
Molecular function	Hydrolase Protease Threonine protease
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell proteasome core complex Inferred from electronic annotation. Source: InterPro
Molecular function	threonine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 241	241	Proteasome subunit alpha type-5		PRO_0000124118
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity
	Modified residue	16	1	Phosphoserine By similarity
	Modified residue	55	1	Phosphothreonine By similarity
	Modified residue	56	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9Z2U1-1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 5610CDA00469120A	FASTA	241	26,411
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete primary structure of mouse 20S proteasomes." Elenich L.A., Nandi D., Kent E.A., McCluskey T.S., Cruz M., Iyer M.N., Woodward E.C., Conn C.W., Ochoa A.L., Ginsburg D.B., Monaco J.J. Immunogenetics 49:835-842(1999) [PubMed: 10436176] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: B10.A.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6 and FVB/N. Tissue: Brain and Mammary tumor.
[3]	Lubec G., Yang J.W., Zigmond M. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 21-32. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF019661 mRNA. Translation: AAC69149.1. BC010709 mRNA. Translation: AAH10709.1. BC083342 mRNA. Translation: AAH83342.1.
IPI	IPI00131407.
RefSeq	NP_036097.1.
UniGene	Mm.208883
3D structure databases
HSSP	HSSP built from PDB template 1RYP based on UniProtKB P32379.
SMR	Q9Z2U1. Positions 8-241.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9Z2U1.
PTM databases
PhosphoSite	Q9Z2U1.
2-D gel databases
REPRODUCTION-2DPAGE	Q9Z2U1.
Proteomic databases
PRIDE	Q9Z2U1.
Genome annotation databases
Ensembl	ENSMUST00000090569; ENSMUSP00000088057; ENSMUSG00000068749; Mus musculus. [Genome view]
GeneID	26442.
KEGG	mmu:26442.
UCSC	uc008qyq.1. mouse.
Organism-specific databases
CTD	26442.
MGI	MGI:1347009. Psma5.
Phylogenomic databases
HOGENOM	Q9Z2U1.
HOVERGEN	Q9Z2U1.
OMA	HIVAATS.
Enzyme and pathway databases
BRENDA	3.4.25.1. 244.
Gene expression databases
Bgee	Q9Z2U1.
Genevestigator	Q9Z2U1.
GermOnline	ENSMUSG00000068749. Mus musculus.
Family and domain databases
InterPro	IPR000426. Proteasome_asu_CS. IPR001353. Proteasome_sua/b. [Graphical view]
Pfam	PF00227. Proteasome. 1 hit. PF10584. Proteasome_A_N. 1 hit. [Graphical view]
PROSITE	PS00388. PROTEASOME_A. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	304525.
SOURCE	Search...

Entry information

Entry name

PSA5_MOUSE

Accession

Primary (citable) accession number: Q9Z2U1

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 8, 2000
Last sequence update:	May 1, 1999
Last modified:	November 3, 2009
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)