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Reviewed, UniProtKB/Swiss-Prot P25161 (PSMD3_DROME)

Last modified November 3, 2009. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
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 namesRecommended name:
    Probable 26S proteasome non-ATPase regulatory subunit 3
      Short name=26S proteasome subunit S3
      Short name=Diphenol oxidase A2 component
      Short name=DOX-A2
Gene names
Name: Dox-A2
ORF Names: CG10484
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

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Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins By similarity.

Subunit structure

The 26S proteasome is composed of a core protease, known as the 20S proteasome, capped at one or both ends by the 19S regulatory complex (RC). The RC is composed of at least 18 different subunits in two subcomplexes, the base and the lid, which form the portions proximal and distal to the 20S proteolytic core, respectively By similarity.

Tissue specificity

Blood (crystal) cells and cuticle.

Sequence similarities

Belongs to the proteasome subunit S3 family.

Contains 1 PCI domain.

Caution

Was originally (Ref.1) thought to be the diphenol oxidase A2 component involved in catecholamine metabolism, melanin formation, and sclerotization of the cuticle.

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Ontologies

Keywords
   Cellular componentProteasome
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from direct assay. Source: FlyBase

regulation of protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentproteasome regulatory particle

Inferred from direct assay. Source: FlyBase

   Molecular functionSUMO binding

Inferred from physical interaction. Source: FlyBase

endopeptidase activity

Inferred from direct assay. Source: FlyBase

enzyme regulator activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q9VTE01EBI-169750,EBI-87041
mod(mdg4)Q86B871EBI-169750,EBI-124784

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 494494Probable 26S proteasome non-ATPase regulatory subunit 3
PRO_0000173821

Regions

Domain319 – 423105PCI

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Sequences

Sequence LengthMass (Da)Tools
P25161-1 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 8659CBCAFF95B735

FASTA49456,004
        10         20         30         40         50         60 
MTNATDIGAN DVEMEVDPTA ETLADEKKNQ DVAAVQEIRE QIRQIEKGVA SKESRFILRV 

        70         80         90        100        110        120 
LRNLPNTRRK LNGVVFRNLA QSIYPAGADR EAAVALMPAV EKDATELPDV PKKQVATKAP 

       130        140        150        160        170        180 
IAEVDAYFYL LLLVKLIDAS DLKRAGISAD ALMAKISIQN RRTLDLIGAK SYFYFSRVAE 

       190        200        210        220        230        240 
LKNSLEGIRS FLHARLRTAT LRNDFEGQAV LINCLLRNYL HYALYDQADK LVKKSVYPES 

       250        260        270        280        290        300 
ASNNEWARFL YYLGRIKAAK LEYSDAHKHL VQALRKSPQH AAIGFRQTVQ KLIIVVELLL 

       310        320        330        340        350        360 
GNIPERVVFR QAGLRQSLGA YFQLTQAVRL GNLKRFGDVV SQYGPKFQLD HTFTLIIRLR 

       370        380        390        400        410        420 
HNVIKTAIRS IGLSYSRISP QDIAKRLMLD SAEDAEFIVS KAIRDGVIEA TLDPAQNFMR 

       430        440        450        460        470        480 
SKESTDIYST REPQLAFHER ISFCLNLHNQ SVKAMRYPPK SYGKDLESAE ERREREQQDL 

       490 
ELAKEMAEDD EDGF

« Hide

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References

« Hide 'large scale' references
[1]"Drosophila melanogaster diphenol oxidase A2: gene structure and homology with the mouse mast-cell tum- transplantation antigen, P91A."
Pentz E.S., Wright T.R.F.
Gene 103:239-242(1991) [PubMed: 1909680] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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: 10731132] [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: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
+Additional computationally mapped references.

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Cross-references

Sequence databases

M63010 Genomic DNA. Translation: AAB00732.1.
AE014134 Genomic DNA. Translation: AAF53749.1.
PIRJH0665.
RefSeqNP_477300.1.
UniGeneDm.4848

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:18295N.
IntActP25161. 2 interactions.
STRINGP25161.

Proteomic databases

PRIDEP25161.

Genome annotation databases

EnsemblFBtr0081147; FBpp0080691; FBgn0000486; Drosophila melanogaster. [Genome view]
GeneID35176.
KEGGdme:Dmel_CG10484.
NMPDRfig|7227.3.peg.2922.

Organism-specific databases

CTD35176.
FlyBaseFBgn0000486. Dox-A2.

Phylogenomic databases

OMALMVIFLM.

Enzyme and pathway databases

BioCycDMEL-XXX-02:DMEL-XXX-02-009443-MON.
BRENDA3.4.25.1. 48.

Gene expression databases

BgeeP25161.
GermOnlineCG10484. Drosophila melanogaster.

Family and domain databases

InterProIPR013586. 26S_Psome_reg_C.
IPR013143. PAM.
IPR000717. PCI.
[Graphical view]
PfamPF01399. PCI. 1 hit.
PF08375. Rpn3_C. 1 hit.
[Graphical view]
SMARTSM00753. PAM. 1 hit.
SM00088. PINT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio792228.

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Entry information

Entry namePSMD3_DROME
AccessionPrimary (citable) accession number: P25161
Secondary accession number(s): Q9VJ09
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: November 3, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

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Relevant documents

Drosophila

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

SIMILARITY comments

Index of protein domains and families

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