Proteasome subunit alpha type-1 - Mus musculus (Mouse)

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Reviewed, UniProtKB/Swiss-Prot Q9R1P4 (PSA1_MOUSE)

Last modified February 9, 2010. Version 81. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Proteasome subunit alpha type-1
    EC=3.4.25.1
Alternative name(s):
    Proteasome component C2
    Macropain subunit C2
    Multicatalytic endopeptidase complex subunit C2
    Proteasome nu chain

Gene names

Name:

Psma1

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

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Protein attributes

Sequence length	263 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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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.
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 bacterial lipopolysaccharide (LPS). Interacts with NOTCH3 By similarity.
Subcellular location	Cytoplasm. Nucleus.
Induction	Up-regulated in liver tumor tissues. Up-regulated by the antioxidant dithiolethione (D3T) in liver, lung and colon (at the protein level).
Post-translational modification	C-terminal extension is partially cleaved off by limited proteolysis leading to a conversion of the proteasome from its latent into its active form.
Sequence similarities	Belongs to the peptidase T1A family.

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Ontologies

Keywords
Biological process	Immune response
Cellular component	Cytoplasm Nucleus Proteasome
Molecular function	Hydrolase Protease Threonine protease
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	negative regulation of inflammatory response to antigenic stimulus Ref.5 Ref.8 Inferred from mutant phenotype. Source: UniProtKB 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, alpha-subunit complex Inferred from electronic annotation. Source: InterPro
Molecular function	lipopolysaccharide binding Ref.5 Inferred from direct assay. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct threonine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
NOTCH3	Q9UM47	1	EBI-991653,EBI-1236377	From a different organism.

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 263

263

Proteasome subunit alpha type-1

PRO_0000124062

Amino acid modifications

Modified residue

N-acetylmethionine By similarity

Modified residue

Phosphoserine By similarity

Cross-link

115

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Cross-link

208

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q9R1P4-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: CC791C56AFBA8043
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FASTA

263

29,547

        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 
ECNLDELVKH GLRALRETLP AEQDLTTKNV SIGIVGKDLE FTIYDDDDVS PFLDGLEERP 

       250        260 
QRKAQPSQAA EEPAEKADEP MEH

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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 mouse Psma1 gene coding for the alpha-type C2 proteasome subunit: structural and functional analysis, mapping, and colocalization with Pde3b on mouse chromosome 7." Hopitzan A., Himmelbauer H., Spevak W., Castanon M.J. Genomics 66:313-323(2000) [PubMed: 10873386] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Skeletal muscle.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N-3. Tissue: Mammary gland.
[4]	Lubec G., Klug S., Yang J.W., Zigmond M. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 63-82 AND 97-107, MASS SPECTROMETRY. Tissue: Brain and Hippocampus.
[5]	"The proteasome as a lipopolysaccharide-binding protein in macrophages: differential effects of proteasome inhibition on lipopolysaccharide-induced signaling events." Qureshi N., Perera P.-Y., Shen J., Zhang G., Lenschat A., Splitter G., Morrison D.C., Vogel S.N. J. Immunol. 171:1515-1525(2003) [PubMed: 12874245] [Abstract] Cited for: FUNCTION, INTERACTION WITH LPS.
[6]	"The up-regulation of proteasome subunits and lysosomal proteases in hepatocellular carcinomas of the HBx gene knockin transgenic mice." Cui F., Wang Y., Wang J., Wei K., Hu J., Liu F., Wang H., Zhao X., Zhang X., Yang X. Proteomics 6:498-504(2006) [PubMed: 16317774] [Abstract] Cited for: INDUCTION.
[7]	"Tissue specific increase of the catalytic subunits of the 26S proteasome by indirect antioxidant dithiolethione in mice: enhanced activity for degradation of abnormal protein." Kwak M.K., Huang B., Chang H., Kim J.A., Kensler T.W. Life Sci. 80:2411-2420(2007) [PubMed: 17521679] [Abstract] Cited for: INDUCTION BY DITHIOLETHIONE.
[8]	"Proteomics of RAW 264.7 macrophages upon interaction with heat-inactivated Candida albicans cells unravel an anti-inflammatory response." Martinez-Solano L., Reales-Calderon J.A., Nombela C., Molero G., Gil C. Proteomics 9:2995-3010(2009) [PubMed: 19526544] [Abstract] Cited for: FUNCTION, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	AF060088 mRNA. Translation: AAD50533.1. AJ272019 mRNA. Translation: CAB95966.1. AJ272272 Genomic DNA. Translation: CAB95969.1. BC005762 mRNA. Translation: AAH05762.1.
IPI	IPI00283862.
RefSeq	NP_036095.1.
UniGene	Mm.121265
3D structure databases
SMR	Q9R1P4. Positions 4-241.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-35147N.
IntAct	Q9R1P4. 18 interactions.
STRING	Q9R1P4.
Protein family/group databases
MEROPS	T01.976.
PTM databases
PhosphoSite	Q9R1P4.
2-D gel databases
REPRODUCTION-2DPAGE	Q9R1P4.
Proteomic databases
PRIDE	Q9R1P4.
Genome annotation databases
Ensembl	ENSMUST00000033008; ENSMUSP00000033008; ENSMUSG00000030751; Mus musculus. [Genome view]
GeneID	26440.
KEGG	mmu:26440.
NMPDR	fig\|10090.3.peg.17468.
UCSC	uc009jhy.1. mouse.
Organism-specific databases
CTD	26440.
MGI	MGI:1347005. Psma1.
Phylogenomic databases
HOGENOM	HBG499923.
HOVERGEN	Q9R1P4.
InParanoid	Q9R1P4.
OMA	IVGKDME.
OrthoDB	EOG941SXB.
PhylomeDB	Q9R1P4.
Enzyme and pathway databases
BRENDA	3.4.25.1. 244.
Gene expression databases
ArrayExpress	Q9R1P4.
Bgee	Q9R1P4.
Genevestigator	Q9R1P4.
GermOnline	ENSMUSG00000030751. 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. 1 hit. PS51475. PROTEASOME_A_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	304517.
SOURCE	Search...

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Entry information

Entry name

PSA1_MOUSE

Accession

Primary (citable) accession number: Q9R1P4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 2000
Last modified:	February 9, 2010
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents