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P40301 (PSA2_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proteasome subunit alpha type-2

EC=3.4.25.1
Alternative name(s):
PROS-Dm25
Proteasome 25 kDa subunit
Gene names
Name:Prosalpha2
Synonyms:PROS-25, Pros25
ORF Names:CG5266
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length234 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.

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 By similarity. Interacts with Rpn6. Ref.5

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Sequence similarities

Belongs to the peptidase T1A family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Prosalpha3P180533EBI-98978,EBI-138951
Prosbeta4Q9VJJ03EBI-98978,EBI-90888

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 234234Proteasome subunit alpha type-2
PRO_0000124083

Sequences

Sequence LengthMass (Da)Tools
P40301 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: BC6F98060BD9D7C2

FASTA23425,907
        10         20         30         40         50         60 
MATERYSFSL TTFSPSGKLV QLEYALAAVS GGAPSVGIIA SNGVVIATEN KHKSPLYEQH 

        70         80         90        100        110        120 
SVHRVEMIYN HIGMVYSGMG PDYRLLVKQA RKIAQTYYLT YKEPIPVSQL VQRVATLMQE 

       130        140        150        160        170        180 
YTQSGGVRPF GVSLLICGWD NDRPYLYQSD PSGAYFAWKA TAMGKNAVNG KTFLEKRYSE 

       190        200        210        220        230 
DLELDDAVHT AILTLKEGFE GKMTADNIEI GICDQNGFQR LDPASIKDYL ASIP 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and genomic organization of the Drosophila proteasome PROS-Dm25 gene."
Seelig A., Troxell M., Kloetzel P.-M.
Biochim. Biophys. Acta 1174:215-217(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Canton-S.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Ovary.
[5]"The proteasomal subunit Rpn6 is a molecular clamp holding the core and regulatory subcomplexes together."
Pathare G.R., Nagy I., Bohn S., Unverdorben P., Hubert A., Korner R., Nickell S., Lasker K., Sali A., Tamura T., Nishioka T., Forster F., Baumeister W., Bracher A.
Proc. Natl. Acad. Sci. U.S.A. 109:149-154(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RPN6.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X70304 Genomic DNA. Translation: CAA49783.1.
AE014297 Genomic DNA. Translation: AAF54814.1.
AY069280 mRNA. Translation: AAL39425.1.
PIRS36116.
RefSeqNP_524328.1. NM_079604.2.
UniGeneDm.2198.

3D structure databases

ProteinModelPortalP40301.
SMRP40301. Positions 2-233.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid66629. 43 interactions.
DIPDIP-20541N.
IntActP40301. 19 interactions.
MINTMINT-795880.
STRING7227.FBpp0082062.

Proteomic databases

PaxDbP40301.
PRIDEP40301.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0082590; FBpp0082062; FBgn0086134.
GeneID41531.
KEGGdme:Dmel_CG5266.

Organism-specific databases

CTD41531.
FlyBaseFBgn0086134. Prosalpha2.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00550000074870.
InParanoidP40301.
KOK02726.
OMAWKATALG.
OrthoDBEOG71VSTG.
PhylomeDBP40301.

Gene expression databases

BgeeP40301.

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

GenomeRNAi41531.
NextBio824277.
PROP40301.

Entry information

Entry namePSA2_DROME
AccessionPrimary (citable) accession number: P40301
Secondary accession number(s): Q9VG71
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase