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P22769

- PSA71_DROME

UniProt

P22769 - PSA71_DROME

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Protein

Proteasome subunit alpha type-7-1

Gene

Prosalpha4

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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. 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_230692. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_232776. Regulation of ornithine decarboxylase (ODC).
REACT_233284. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_234235. Hh ligand biogenesis disease.
REACT_234707. SCF(Skp2)-mediated degradation of p27/p21.
REACT_238120. degradation of DVL.
REACT_239151. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_242866. Degradation of beta-catenin by the destruction complex.
REACT_247767. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_250603. SCF-beta-TrCP mediated degradation of Emi1.
REACT_258701. Hedgehog ligand biogenesis.
REACT_260216. Ubiquitin-dependent degradation of Cyclin D1.
REACT_269395. GLI3 is processed to GLI3R by the proteasome.
REACT_271013. Degradation of GLI1 by the proteasome.
REACT_271479. Degradation of GLI2 by the proteasome.
REACT_92044. APC/C:Cdc20 mediated degradation of Securin.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-7-1 (EC:3.4.25.1)
Alternative name(s):
PROS-Dm28.1
Proteasome 28 kDa subunit 1
Gene namesi
Name:Prosalpha4
Synonyms:PROS-28.1, Pros28.1
ORF Names:CG3422
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome X

Organism-specific databases

FlyBaseiFBgn0004066. Prosalpha4.

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 – 249249Proteasome subunit alpha type-7-1PRO_0000124153Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei177 – 1771Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP22769.
PRIDEiP22769.

Expressioni

Gene expression databases

BgeeiP22769.

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; this interaction is reduced by PI31 ADP-ribosylation.By similarity1 Publication

Protein-protein interaction databases

BioGridi58925. 52 interactions.
DIPiDIP-17376N.
IntActiP22769. 5 interactions.
MINTiMINT-994729.
STRINGi7227.FBpp0073989.

Structurei

3D structure databases

ProteinModelPortaliP22769.
SMRiP22769. Positions 5-240.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074753.
HOGENOMiHOG000072912.
InParanoidiP22769.
KOiK02731.
OMAiPLKMLDR.
OrthoDBiEOG71VSTG.
PhylomeDBiP22769.

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.

P22769-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSRYDRAVT IFSPDGHLLQ VEYAQEAVRK GSTAVGVRGA NCVVLGVEKK
60 70 80 90 100
SVAQLQEDRK VRKICMLDNH VVMAFAGLTA DARIMINRAQ VECQSHRLNV
110 120 130 140 150
EDPVTLEYIT RFIAQLKQKY TQSNGRRPFG ISCLIGGFDA DGSAHLFQTE
160 170 180 190 200
PSGIFYEYKA NATGRSAKVV REFFEKSYRE EEVANEHGAV KLAIRALLEV
210 220 230 240
AQSGQNNLEV AIMENGKPLK MLDTDVITDY VKIIEKEKEE ELEKKKQKK
Length:249
Mass (Da):27,973
Last modified:December 8, 2000 - v2
Checksum:i56987932DADD02B3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti224 – 2241T → N in AAA62768. (PubMed:2169443)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57712 mRNA. Translation: AAA62768.1.
X62286 Genomic DNA. Translation: CAA44174.1.
AY542383 Genomic DNA. Translation: AAS86210.1.
AY542384 Genomic DNA. Translation: AAS86211.1.
AY542385 Genomic DNA. Translation: AAS86212.1.
AY542386 Genomic DNA. Translation: AAS86213.1.
AY542387 Genomic DNA. Translation: AAS86214.1.
AY542388 Genomic DNA. Translation: AAS86215.1.
AY542389 Genomic DNA. Translation: AAS86216.1.
AE014298 Genomic DNA. Translation: AAF48573.1.
AY071241 mRNA. Translation: AAL48863.1.
PIRiJQ0681.
S23451.
RefSeqiNP_525092.1. NM_080353.5.
UniGeneiDm.1671.

Genome annotation databases

EnsemblMetazoaiFBtr0074210; FBpp0073989; FBgn0004066.
GeneIDi32584.
KEGGidme:Dmel_CG3422.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M57712 mRNA. Translation: AAA62768.1 .
X62286 Genomic DNA. Translation: CAA44174.1 .
AY542383 Genomic DNA. Translation: AAS86210.1 .
AY542384 Genomic DNA. Translation: AAS86211.1 .
AY542385 Genomic DNA. Translation: AAS86212.1 .
AY542386 Genomic DNA. Translation: AAS86213.1 .
AY542387 Genomic DNA. Translation: AAS86214.1 .
AY542388 Genomic DNA. Translation: AAS86215.1 .
AY542389 Genomic DNA. Translation: AAS86216.1 .
AE014298 Genomic DNA. Translation: AAF48573.1 .
AY071241 mRNA. Translation: AAL48863.1 .
PIRi JQ0681.
S23451.
RefSeqi NP_525092.1. NM_080353.5.
UniGenei Dm.1671.

3D structure databases

ProteinModelPortali P22769.
SMRi P22769. Positions 5-240.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 58925. 52 interactions.
DIPi DIP-17376N.
IntActi P22769. 5 interactions.
MINTi MINT-994729.
STRINGi 7227.FBpp0073989.

Proteomic databases

PaxDbi P22769.
PRIDEi P22769.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0074210 ; FBpp0073989 ; FBgn0004066 .
GeneIDi 32584.
KEGGi dme:Dmel_CG3422.

Organism-specific databases

CTDi 32584.
FlyBasei FBgn0004066. Prosalpha4.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00550000074753.
HOGENOMi HOG000072912.
InParanoidi P22769.
KOi K02731.
OMAi PLKMLDR.
OrthoDBi EOG71VSTG.
PhylomeDBi P22769.

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_230692. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_232776. Regulation of ornithine decarboxylase (ODC).
REACT_233284. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_234235. Hh ligand biogenesis disease.
REACT_234707. SCF(Skp2)-mediated degradation of p27/p21.
REACT_238120. degradation of DVL.
REACT_239151. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_242866. Degradation of beta-catenin by the destruction complex.
REACT_247767. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_250603. SCF-beta-TrCP mediated degradation of Emi1.
REACT_258701. Hedgehog ligand biogenesis.
REACT_260216. Ubiquitin-dependent degradation of Cyclin D1.
REACT_269395. GLI3 is processed to GLI3R by the proteasome.
REACT_271013. Degradation of GLI1 by the proteasome.
REACT_271479. Degradation of GLI2 by the proteasome.
REACT_92044. APC/C:Cdc20 mediated degradation of Securin.

Miscellaneous databases

GenomeRNAii 32584.
NextBioi 779280.

Gene expression databases

Bgeei P22769.

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. "The Drosophila PROS-28.1 gene is a member of the proteasome gene family."
    Haass C., Pesold-Hurt B., Multhaup G., Beyreuther K., Kloetzel P.-M.
    Gene 90:235-241(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular characterization of the genomic regions of the Drosophila alpha-type subunit proteasome genes PROS-Dm28.1 and PROS-Dm35."
    Frentzel S., Troxell M., Haass C., Pesold-Hurt B., Glaetzer K.H., Kloetzel P.-M.
    Eur. J. Biochem. 205:1043-1051(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Oregon-R.
  3. "Rapid evolution through gene duplication and subfunctionalization of the testes-specific alpha4 proteasome subunits in Drosophila."
    Torgerson D.G., Singh R.S.
    Genetics 168:1421-1432(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: b pr tk, CPA-129, CPA-46, Z(H)-12, Z(H)-16 and Z(H)-34.
  4. "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.
  5. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  7. "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-177, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  8. "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 nameiPSA71_DROME
AccessioniPrimary (citable) accession number: P22769
Secondary accession number(s): Q9VXI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: December 8, 2000
Last modified: November 26, 2014
This is version 137 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