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P22769 (PSA71_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. 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-7-1

EC=3.4.25.1
Alternative name(s):
PROS-Dm28.1
Proteasome 28 kDa subunit 1
Gene names
Name:Prosalpha4
Synonyms:PROS-28.1, Pros28.1
ORF Names:CG3422
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length249 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 PI31; this interaction is reduced by PI31 ADP-ribosylation. Ref.8

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 – 249249Proteasome subunit alpha type-7-1
PRO_0000124153

Amino acid modifications

Modified residue1771Phosphoserine Ref.7

Experimental info

Sequence conflict2241T → N in AAA62768. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P22769 [UniParc].

Last modified December 8, 2000. Version 2.
Checksum: 56987932DADD02B3

FASTA24927,973
        10         20         30         40         50         60 
MSSRYDRAVT IFSPDGHLLQ VEYAQEAVRK GSTAVGVRGA NCVVLGVEKK SVAQLQEDRK 

        70         80         90        100        110        120 
VRKICMLDNH VVMAFAGLTA DARIMINRAQ VECQSHRLNV EDPVTLEYIT RFIAQLKQKY 

       130        140        150        160        170        180 
TQSNGRRPFG ISCLIGGFDA DGSAHLFQTE PSGIFYEYKA NATGRSAKVV REFFEKSYRE 

       190        200        210        220        230        240 
EEVANEHGAV KLAIRALLEV AQSGQNNLEV AIMENGKPLK MLDTDVITDY VKIIEKEKEE 


ELEKKKQKK 

« Hide

References

« Hide 'large scale' references
[1]"The Drosophila PROS-28.1 gene is a member of the proteasome gene family."
Haass C., Pesold-Hurt B., Multhaup G., Beyreuther K., Kloetzel P.-M.
Gene 90:235-241(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular characterization of the genomic regions of the Drosophila alpha-type subunit proteasome genes PROS-Dm28.1 and PROS-Dm35."
Frentzel S., Troxell M., Haass C., Pesold-Hurt B., Glaetzer K.H., Kloetzel P.-M.
Eur. J. Biochem. 205:1043-1051(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Oregon-R.
[3]"Rapid evolution through gene duplication and subfunctionalization of the testes-specific alpha4 proteasome subunits in Drosophila."
Torgerson D.G., Singh R.S.
Genetics 168:1421-1432(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: b pr tk, CPA-129, CPA-46, Z(H)-12, Z(H)-16 and Z(H)-34.
[4]"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.
[5]"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.
[6]"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: Embryo.
[7]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryo.
[8]"Proteasome regulation by ADP-ribosylation."
Cho-Park P.F., Steller H.
Cell 153:614-627(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PI31.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M57712 mRNA. Translation: AAA62768.1.
X62286 Genomic DNA. Translation: CAA44174.1.
AY542383 Genomic DNA. Translation: AAS86210.1.
AY542384 Genomic DNA. Translation: AAS86211.1.
AY542385 Genomic DNA. Translation: AAS86212.1.
AY542386 Genomic DNA. Translation: AAS86213.1.
AY542387 Genomic DNA. Translation: AAS86214.1.
AY542388 Genomic DNA. Translation: AAS86215.1.
AY542389 Genomic DNA. Translation: AAS86216.1.
AE014298 Genomic DNA. Translation: AAF48573.1.
AY071241 mRNA. Translation: AAL48863.1.
PIRJQ0681.
S23451.
RefSeqNP_525092.1. NM_080353.4.
UniGeneDm.1671.

3D structure databases

ProteinModelPortalP22769.
SMRP22769. Positions 5-240.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid58925. 52 interactions.
DIPDIP-17376N.
IntActP22769. 5 interactions.
MINTMINT-994729.
STRING7227.FBpp0073989.

Proteomic databases

PaxDbP22769.
PRIDEP22769.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0074210; FBpp0073989; FBgn0004066.
GeneID32584.
KEGGdme:Dmel_CG3422.

Organism-specific databases

CTD32584.
FlyBaseFBgn0004066. Prosalpha4.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00550000074753.
HOGENOMHOG000072912.
InParanoidP22769.
KOK02731.
OMAPLKMLDR.
OrthoDBEOG71VSTG.
PhylomeDBP22769.

Gene expression databases

BgeeP22769.

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

GenomeRNAi32584.
NextBio779280.

Entry information

Entry namePSA71_DROME
AccessionPrimary (citable) accession number: P22769
Secondary accession number(s): Q9VXI9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: December 8, 2000
Last modified: July 9, 2014
This is version 134 of the entry and version 2 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