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Q9V5C6

- PSA3_DROME

UniProt

Q9V5C6 - PSA3_DROME

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Protein

Proteasome subunit alpha type-3

Gene

Prosalpha7

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 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

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

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: FlyBase
  2. proteasome-mediated ubiquitin-dependent protein catabolic process Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

ReactomeiREACT_180649. Activation of NF-kappaB in B cells.
REACT_180655. ER-Phagosome pathway.
REACT_180671. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_180708. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_181662. Separation of Sister Chromatids.
REACT_184330. Asymmetric localization of PCP proteins.
REACT_211248. CDK-mediated phosphorylation and removal of Cdc6.
REACT_215026. degradation of AXIN.
REACT_218589. Orc1 removal from chromatin.
REACT_225883. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_92044. APC/C:Cdc20 mediated degradation of Securin.

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: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0023175. Prosalpha7.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. microtubule associated complex Source: FlyBase
  3. nucleus Source: UniProtKB-KW
  4. proteasome core complex Source: FlyBase
  5. 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.

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. 46 interactions.
DIPiDIP-22157N.
IntActiQ9V5C6. 8 interactions.
MINTiMINT-950398.

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. 1 PublicationCurated
Sequence conflicti30 – 301Missing in AAB82572. 1 PublicationCurated
Sequence conflicti62 – 621D → H in AAB82572. 1 PublicationCurated
Sequence conflicti140 – 15718Missing in AAT27293. 1 PublicationCuratedAdd
BLAST
Sequence conflicti167 – 1671Missing in AAB82572. 1 PublicationCurated
Sequence conflicti182 – 1821M → T in AAB82572. 1 PublicationCurated
Sequence conflicti235 – 25319ARKAG…DNETH → DEDTACGQQDEGRRQRQ in AAB82572. 1 PublicationCuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AF025793 Genomic DNA. Translation: AAB82572.1 .
AE013599 Genomic DNA. Translation: AAF58889.1 .
AY069616 mRNA. Translation: AAL39761.1 .
BT014669 mRNA. Translation: AAT27293.1 .
RefSeqi NP_724834.1. NM_165703.3.
UniGenei Dm.2041.

3D structure databases

ProteinModelPortali Q9V5C6.
SMRi Q9V5C6. Positions 2-237.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 61847. 46 interactions.
DIPi DIP-22157N.
IntActi Q9V5C6. 8 interactions.
MINTi MINT-950398.

Protein family/group databases

MEROPSi T01.977.

Proteomic databases

PaxDbi Q9V5C6.
PRIDEi Q9V5C6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0089998 ; FBpp0089041 ; FBgn0023175 .
GeneIDi 36018.
KEGGi dme:Dmel_CG1519.

Organism-specific databases

CTDi 36018.
FlyBasei FBgn0023175. Prosalpha7.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00550000074912.
InParanoidi Q9V5C6.
KOi K02727.
OMAi VPDGRHF.
OrthoDBi EOG73JKW6.
PhylomeDBi Q9V5C6.

Enzyme and pathway databases

Reactomei REACT_180649. Activation of NF-kappaB in B cells.
REACT_180655. ER-Phagosome pathway.
REACT_180671. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_180708. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_181662. Separation of Sister Chromatids.
REACT_184330. Asymmetric localization of PCP proteins.
REACT_211248. CDK-mediated phosphorylation and removal of Cdc6.
REACT_215026. degradation of AXIN.
REACT_218589. Orc1 removal from chromatin.
REACT_225883. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_92044. APC/C:Cdc20 mediated degradation of Securin.

Miscellaneous databases

GenomeRNAii 36018.
NextBioi 796366.
PROi Q9V5C6.

Gene expression databases

Bgeei Q9V5C6.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view ]
SMARTi SM00948. Proteasome_A_N. 1 hit.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 128 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