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Protein

Proteasome subunit alpha type-3

Gene

Prosalpha7

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 (By similarity).By similarity

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

  • cellular response to DNA damage stimulus Source: FlyBase
  • proteasomal ubiquitin-independent protein catabolic process Source: GO_Central
  • 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_299289. degradation of DVL.
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.
REACT_359614. Degradation of GLI1 by the proteasome.
REACT_361037. CLEC7A (Dectin-1) signaling.
REACT_362328. Dectin-1 mediated noncanonical NF-kB signaling.

Protein family/group databases

MEROPSiT01.977.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-3 (EC:3.4.25.1)
Alternative name(s):
20S proteasome subunit alpha-7
Gene namesi
Name:Prosalpha7
ORF Names:CG1519
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0023175. Prosalpha7.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • microtubule associated complex Source: FlyBase
  • nucleus Source: UniProtKB-SubCell
  • proteasome complex Source: FlyBase
  • proteasome core complex Source: FlyBase
  • 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 – 253253Proteasome subunit alpha type-3PRO_0000124097Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei248 – 2481Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9V5C6.
PRIDEiQ9V5C6.

Expressioni

Gene expression databases

BgeeiQ9V5C6.
GenevisibleiQ9V5C6. DM.

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 ntc.By similarity1 Publication

Protein-protein interaction databases

BioGridi61847. 47 interactions.
DIPiDIP-22157N.
IntActiQ9V5C6. 9 interactions.
MINTiMINT-950398.
STRINGi7227.FBpp0089041.

Structurei

3D structure databases

ProteinModelPortaliQ9V5C6.
SMRiQ9V5C6. Positions 2-237.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074912.
InParanoidiQ9V5C6.
KOiK02727.
OMAiVPDGRHF.
OrthoDBiEOG73JKW6.
PhylomeDBiQ9V5C6.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
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.

Q9V5C6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTIGTGYDL SASQFSPDGR VFQIDYASKA VEKSGTVIGI RGKDAVVLAV
60 70 80 90 100
EKIITSKLYE PDAGGRIFTI EKNIGMAVAG LVADGNFVAD IARQEAANYR
110 120 130 140 150
QQFEQAIPLK HLCHRVAGYV HAYTLYSAVR PFGLSIILAS WDEVEGPQLY
160 170 180 190 200
KIEPSGSSFG YFACASGKAK QLAKTEMEKL KMDMRTDELV ESAGEIIYKV
210 220 230 240 250
HDELKDKDFR FEMGLVGRVT GGLHLINPSE LTEKARKAGD AANKDEDSDN

ETH
Length:253
Mass (Da):27,675
Last modified:May 1, 2000 - v1
Checksum:i7B19D8DA350E2B7E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171P → A in AAB82572 (Ref. 1) Curated
Sequence conflicti30 – 301Missing in AAB82572 (Ref. 1) Curated
Sequence conflicti62 – 621D → H in AAB82572 (Ref. 1) Curated
Sequence conflicti140 – 15718Missing in AAT27293 (Ref. 5) CuratedAdd
BLAST
Sequence conflicti167 – 1671Missing in AAB82572 (Ref. 1) Curated
Sequence conflicti182 – 1821M → T in AAB82572 (Ref. 1) Curated
Sequence conflicti235 – 25319ARKAG…DNETH → DEDTACGQQDEGRRQRQ in AAB82572 (Ref. 1) CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF025793 Genomic DNA. Translation: AAB82572.1.
AE013599 Genomic DNA. Translation: AAF58889.1.
AY069616 mRNA. Translation: AAL39761.1.
BT014669 mRNA. Translation: AAT27293.1.
RefSeqiNP_724834.1. NM_165703.3.
UniGeneiDm.2041.

Genome annotation databases

EnsemblMetazoaiFBtr0089998; FBpp0089041; FBgn0023175.
GeneIDi36018.
KEGGidme:Dmel_CG1519.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF025793 Genomic DNA. Translation: AAB82572.1.
AE013599 Genomic DNA. Translation: AAF58889.1.
AY069616 mRNA. Translation: AAL39761.1.
BT014669 mRNA. Translation: AAT27293.1.
RefSeqiNP_724834.1. NM_165703.3.
UniGeneiDm.2041.

3D structure databases

ProteinModelPortaliQ9V5C6.
SMRiQ9V5C6. Positions 2-237.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61847. 47 interactions.
DIPiDIP-22157N.
IntActiQ9V5C6. 9 interactions.
MINTiMINT-950398.
STRINGi7227.FBpp0089041.

Protein family/group databases

MEROPSiT01.977.

Proteomic databases

PaxDbiQ9V5C6.
PRIDEiQ9V5C6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0089998; FBpp0089041; FBgn0023175.
GeneIDi36018.
KEGGidme:Dmel_CG1519.

Organism-specific databases

CTDi36018.
FlyBaseiFBgn0023175. Prosalpha7.

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074912.
InParanoidiQ9V5C6.
KOiK02727.
OMAiVPDGRHF.
OrthoDBiEOG73JKW6.
PhylomeDBiQ9V5C6.

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_299289. degradation of DVL.
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.
REACT_359614. Degradation of GLI1 by the proteasome.
REACT_361037. CLEC7A (Dectin-1) signaling.
REACT_362328. Dectin-1 mediated noncanonical NF-kB signaling.

Miscellaneous databases

GenomeRNAii36018.
NextBioi796366.
PROiQ9V5C6.

Gene expression databases

BgeeiQ9V5C6.
GenevisibleiQ9V5C6. DM.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
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. "Cloning of the Drosophila melanogaster alpha7 proteasome subunit gene."
    Belote J.M., Smyth K.A., Katz E., Miller M.
    Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
    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.
    , 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. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Testis.
  6. "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-248, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  7. "A conserved F box regulatory complex controls proteasome activity in Drosophila."
    Bader M., Benjamin S., Wapinski O.L., Smith D.M., Goldberg A.L., Steller H.
    Cell 145:371-382(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NTC.

Entry informationi

Entry nameiPSA3_DROME
AccessioniPrimary (citable) accession number: Q9V5C6
Secondary accession number(s): O17313, Q8MKU6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: May 1, 2000
Last modified: July 22, 2015
This is version 137 of the entry and version 1 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.