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Q9XYN7 (PSB3_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. 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 beta type-3

EC=3.4.25.1
Alternative name(s):
20S proteasome subunit beta-3
Gene names
Name:Prosbeta3
ORF Names:CG11980
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length205 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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. Ref.1

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.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Sequence similarities

Belongs to the peptidase T1B family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 205205Proteasome subunit beta type-3
PRO_0000148062

Sequences

Sequence LengthMass (Da)Tools
Q9XYN7 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 3AE365887AF3A247

FASTA20523,234
        10         20         30         40         50         60 
MSILAYNGGC VVAMRGKDCV AIATDHRFGI QAQTISTDFK KVFHIGPRMF LGLTGLQTDI 

        70         80         90        100        110        120 
LTVRDRLMFR KNLYETRENR EMCPKPFSAM MSSFLYEHRF GPYFIEPVVA GLDPKTMEPF 

       130        140        150        160        170        180 
ICNMDLIGCP NAPDDFVVAG TCAEQLYGMC ETLWKPDLEP DQLFEVIAQS IVNAFDRDAM 

       190        200 
SGWGATVYII EKDKITERTL KTRMD 

« Hide

References

« Hide 'large scale' references
[1]"The dominant temperature-sensitive lethal DTS7 of Drosophila melanogaster encodes an altered 20S proteasome beta-type subunit."
Smyth K.A., Belote J.M.
Genetics 151:211-220(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Strain: Samarkand.
[2]"Widespread adaptive evolution of Drosophila genes with sex-biased expression."
Proeschel M., Zhang Z., Parsch J.
Genetics 174:893-900(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ZBMEL131, ZBMEL145, ZBMEL157, ZBMEL186, ZBMEL191, ZBMEL82, ZBMEL84 and ZBMEL95.
[3]"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.
[4]"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.
[5]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF116898 Genomic DNA. Translation: AAD22968.1.
AM294562 Genomic DNA. Translation: CAL26545.1.
AM294563 Genomic DNA. Translation: CAL26546.1.
AM294564 Genomic DNA. Translation: CAL26547.1.
AM294565 Genomic DNA. Translation: CAL26548.1.
AM294566 Genomic DNA. Translation: CAL26549.1.
AM294567 Genomic DNA. Translation: CAL26550.1.
AM294568 Genomic DNA. Translation: CAL26551.1.
AM294569 Genomic DNA. Translation: CAL26552.1.
AE014297 Genomic DNA. Translation: AAF54320.1.
AY095029 mRNA. Translation: AAM11357.1.
RefSeqNP_649858.1. NM_141601.2.
UniGeneDm.6972.

3D structure databases

ProteinModelPortalQ9XYN7.
SMRQ9XYN7. Positions 2-205.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid66247. 57 interactions.
DIPDIP-18901N.
IntActQ9XYN7. 16 interactions.
MINTMINT-306832.
STRING7227.FBpp0081488.

Proteomic databases

PaxDbQ9XYN7.
PRIDEQ9XYN7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0082010; FBpp0081488; FBgn0026380.
GeneID41079.
KEGGdme:Dmel_CG11981.

Organism-specific databases

CTD41079.
FlyBaseFBgn0026380. Prosbeta3.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00550000074820.
InParanoidQ9XYN7.
KOK02735.
OMAMDLIGCP.
OrthoDBEOG783MWB.
PhylomeDBQ9XYN7.

Gene expression databases

BgeeQ9XYN7.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
InterProIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
[Graphical view]
SUPFAMSSF56235. SSF56235. 1 hit.
PROSITEPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi41079.
NextBio822046.
PROQ9XYN7.

Entry information

Entry namePSB3_DROME
AccessionPrimary (citable) accession number: Q9XYN7
Secondary accession number(s): A0APH4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 111 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