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Protein

Proteasome subunit alpha type-4

Gene

Prosalpha3

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Cleavage of peptide bonds with very broad specificity.PROSITE-ProRule annotation

GO - Molecular functioni

  1. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. cell proliferation Source: FlyBase
  2. mitotic spindle assembly Source: FlyBase
  3. mitotic spindle elongation Source: FlyBase
  4. mitotic spindle organization Source: FlyBase
  5. proteasome-mediated ubiquitin-dependent protein catabolic process Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

ReactomeiREACT_273531. CDK-mediated phosphorylation and removal of Cdc6.
REACT_274251. degradation of AXIN.
REACT_274764. ER-Phagosome pathway.
REACT_274899. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_283069. Degradation of GLI2 by the proteasome.
REACT_284680. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_285954. APC/C:Cdc20 mediated degradation of Securin.
REACT_287787. Activation of NF-kappaB in B cells.
REACT_289889. GLI3 is processed to GLI3R by the proteasome.
REACT_293133. Degradation of GLI1 by the proteasome.
REACT_299289. degradation of DVL.
REACT_304845. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_307080. Hh ligand biogenesis disease.
REACT_308142. Hedgehog ligand biogenesis.
REACT_320700. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_323570. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_329319. SCF(Skp2)-mediated degradation of p27/p21.
REACT_330960. Hedgehog 'on' state.
REACT_333353. Asymmetric localization of PCP proteins.
REACT_335389. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_335593. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_335971. SCF-beta-TrCP mediated degradation of Emi1.
REACT_336807. Regulation of ornithine decarboxylase (ODC).
REACT_337097. Ubiquitin-dependent degradation of Cyclin D1.
REACT_343999. Orc1 removal from chromatin.
REACT_346613. Separation of Sister Chromatids.
REACT_347454. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_354443. Degradation of beta-catenin by the destruction complex.

Protein family/group databases

MEROPSiT01.973.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-4 (EC:3.4.25.1)
Alternative name(s):
PROS-Dm29
Proteasome 29 kDa subunit
Gene namesi
Name:Prosalpha3
Synonyms:PROS-29, Pros29
ORF Names:CG9327
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0261394. Prosalpha3.

Subcellular locationi

  1. Cytoplasm By similarity
  2. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: FlyBase
  2. microtubule associated complex Source: FlyBase
  3. nucleus Source: FlyBase
  4. proteasome complex Source: FlyBase
  5. proteasome core complex Source: FlyBase
  6. proteasome core complex, alpha-subunit complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 264264Proteasome subunit alpha type-4PRO_0000124109Add
BLAST

Proteomic databases

PaxDbiP18053.
PRIDEiP18053.

Expressioni

Gene expression databases

BgeeiP18053.

Interactioni

Subunit structurei

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.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PI31Q9V6372EBI-138951,EBI-144377
Prosalpha2P403013EBI-138951,EBI-98978

Protein-protein interaction databases

BioGridi63019. 41 interactions.
DIPiDIP-19125N.
IntActiP18053. 12 interactions.
MINTiMINT-996465.
STRINGi7227.FBpp0071451.

Structurei

3D structure databases

ProteinModelPortaliP18053.
SMRiP18053. Positions 2-240.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074827.
InParanoidiP18053.
KOiK02728.
OMAiYQVEYAQ.
OrthoDBiEOG7F512J.
PhylomeDBiP18053.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR016050. Proteasome_bsu_CS.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTiSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P18053-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARRYDSRTT IFSPEGRLYQ VEYAMEAISH AGTCLGILAE DGILLAAECR
60 70 80 90 100
STNKLLDSAI PSEKIYRLND NMVCSVAGIT SDANVLTSEL RLIAQRYQFS
110 120 130 140 150
YGEVIPCEQL VSHLCDIKQA YTQYGGKRPF GVSLLYMGWD NKYGYQLYQS
160 170 180 190 200
DPSGNYGGWK ATCIGNNFGA AISMLKQELA DKENVKLTLA DAKDLAIKVL
210 220 230 240 250
SMTLDTTKLT PEKVEMATLQ RVDNKTVYSV LEKPDVEKLI EKYTKVQAEA
260
EAAKKEKQAK QPTK
Length:264
Mass (Da):29,412
Last modified:December 8, 2000 - v2
Checksum:iE5209BC634008B8B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 681L → R in CAA36555 (PubMed:2374736).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52319 mRNA. Translation: CAA36555.1.
AE013599 Genomic DNA. Translation: AAF46651.1.
AY084140 mRNA. Translation: AAL89878.1.
PIRiS10318.
RefSeqiNP_476691.1. NM_057343.5.
UniGeneiDm.712.

Genome annotation databases

EnsemblMetazoaiFBtr0071522; FBpp0071451; FBgn0261394.
GeneIDi37378.
KEGGidme:Dmel_CG9327.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52319 mRNA. Translation: CAA36555.1.
AE013599 Genomic DNA. Translation: AAF46651.1.
AY084140 mRNA. Translation: AAL89878.1.
PIRiS10318.
RefSeqiNP_476691.1. NM_057343.5.
UniGeneiDm.712.

3D structure databases

ProteinModelPortaliP18053.
SMRiP18053. Positions 2-240.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi63019. 41 interactions.
DIPiDIP-19125N.
IntActiP18053. 12 interactions.
MINTiMINT-996465.
STRINGi7227.FBpp0071451.

Protein family/group databases

MEROPSiT01.973.

Proteomic databases

PaxDbiP18053.
PRIDEiP18053.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0071522; FBpp0071451; FBgn0261394.
GeneIDi37378.
KEGGidme:Dmel_CG9327.

Organism-specific databases

CTDi37378.
FlyBaseiFBgn0261394. Prosalpha3.

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074827.
InParanoidiP18053.
KOiK02728.
OMAiYQVEYAQ.
OrthoDBiEOG7F512J.
PhylomeDBiP18053.

Enzyme and pathway databases

ReactomeiREACT_273531. CDK-mediated phosphorylation and removal of Cdc6.
REACT_274251. degradation of AXIN.
REACT_274764. ER-Phagosome pathway.
REACT_274899. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_283069. Degradation of GLI2 by the proteasome.
REACT_284680. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_285954. APC/C:Cdc20 mediated degradation of Securin.
REACT_287787. Activation of NF-kappaB in B cells.
REACT_289889. GLI3 is processed to GLI3R by the proteasome.
REACT_293133. Degradation of GLI1 by the proteasome.
REACT_299289. degradation of DVL.
REACT_304845. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_307080. Hh ligand biogenesis disease.
REACT_308142. Hedgehog ligand biogenesis.
REACT_320700. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_323570. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_329319. SCF(Skp2)-mediated degradation of p27/p21.
REACT_330960. Hedgehog 'on' state.
REACT_333353. Asymmetric localization of PCP proteins.
REACT_335389. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_335593. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_335971. SCF-beta-TrCP mediated degradation of Emi1.
REACT_336807. Regulation of ornithine decarboxylase (ODC).
REACT_337097. Ubiquitin-dependent degradation of Cyclin D1.
REACT_343999. Orc1 removal from chromatin.
REACT_346613. Separation of Sister Chromatids.
REACT_347454. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_354443. Degradation of beta-catenin by the destruction complex.

Miscellaneous databases

ChiTaRSiPros29. fly.
GenomeRNAii37378.
NextBioi803347.
PROiP18053.

Gene expression databases

BgeeiP18053.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR016050. Proteasome_bsu_CS.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTiSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Drosophila PROS-29 gene is a new member of the PROS-gene family."
    Haass C., Pesold-Hurt B., Kloetzel P.-M.
    Nucleic Acids Res. 18:4018-4018(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Oregon-R.
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  5. "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.

Entry informationi

Entry nameiPSA4_DROME
AccessioniPrimary (citable) accession number: P18053
Secondary accession number(s): Q9W2N9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: December 8, 2000
Last modified: April 29, 2015
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.