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P18053

- PSA4_DROME

UniProt

P18053 - PSA4_DROME

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Protein

Proteasome subunit alpha type-4

Gene

Prosalpha3

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. cell proliferation Source: FlyBase
  2. mitotic spindle elongation Source: FlyBase
  3. mitotic spindle organization Source: FlyBase
  4. proteasome-mediated ubiquitin-dependent protein catabolic process Source: FlyBase
  5. spindle assembly involved in mitosis 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

MEROPSiT01.973.

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: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0261394. Prosalpha3.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: FlyBase
  2. microtubule associated complex Source: FlyBase
  3. nucleus Source: FlyBase
  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 – 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. 6 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.
OMAiRNDKQAY.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
X52319 mRNA. Translation: CAA36555.1 .
AE013599 Genomic DNA. Translation: AAF46651.1 .
AY084140 mRNA. Translation: AAL89878.1 .
PIRi S10318.
RefSeqi NP_476691.1. NM_057343.5.
UniGenei Dm.712.

3D structure databases

ProteinModelPortali P18053.
SMRi P18053. Positions 2-240.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 63019. 41 interactions.
DIPi DIP-19125N.
IntActi P18053. 6 interactions.
MINTi MINT-996465.
STRINGi 7227.FBpp0071451.

Protein family/group databases

MEROPSi T01.973.

Proteomic databases

PaxDbi P18053.
PRIDEi P18053.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0071522 ; FBpp0071451 ; FBgn0261394 .
GeneIDi 37378.
KEGGi dme:Dmel_CG9327.

Organism-specific databases

CTDi 37378.
FlyBasei FBgn0261394. Prosalpha3.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00550000074827.
InParanoidi P18053.
KOi K02728.
OMAi RNDKQAY.
OrthoDBi EOG7F512J.
PhylomeDBi P18053.

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

ChiTaRSi Pros29. drosophila.
GenomeRNAii 37378.
NextBioi 803347.
PROi P18053.

Gene expression databases

Bgeei P18053.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR016050. Proteasome_bsu_CS.
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-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: October 29, 2014
This is version 141 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