Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q95083

- PSA5_DROME

UniProt

Q95083 - PSA5_DROME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Proteasome subunit alpha type-5

Gene

Prosalpha5

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript 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 process 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-5 (EC:3.4.25.1)
Gene namesi
Name:Prosalpha5
Synonyms:ProsMA5
ORF Names:CG10938
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0016697. Prosalpha5.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
  3. proteasome core complex Source: FlyBase
  4. 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 – 244244Proteasome subunit alpha type-5PRO_0000124121Add
BLAST

Proteomic databases

PaxDbiQ95083.
PRIDEiQ95083.

Expressioni

Gene expression databases

BgeeiQ95083.

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).By similarity

Protein-protein interaction databases

BioGridi62645. 37 interactions.
DIPiDIP-19014N.
IntActiQ95083. 2 interactions.
MINTiMINT-966233.
STRINGi7227.FBpp0086066.

Structurei

3D structure databases

ProteinModelPortaliQ95083.
SMRiQ95083. Positions 8-243.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074958.
InParanoidiQ95083.
KOiK02729.
OMAiCAMSGLT.
OrthoDBiEOG769ZKB.
PhylomeDBiQ95083.

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.

Q95083-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFLTRSEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGI CTPEGVVLAV
60 70 80 90 100
EKRITSPLMV PSTVEKIVEV DKHIGCATSG LMADARTLIE RARVECQNHW
110 120 130 140 150
FVYNERMSIE SCAQAVSTLA IQFGDSGDSD GAAAMSRPFG VAILFAGIEA
160 170 180 190 200
GQPQLWHMDP SGTFVRHGAK AIGSGSEGAQ QNLQDLFRPD LTLDEAIDIS
210 220 230 240
LNTLKQVMEE KLNSTNVEVM TMTKEREFYM FTKEEVEQHI KNIA
Length:244
Mass (Da):26,884
Last modified:December 8, 2000 - v2
Checksum:iC58F3232A17FB711
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti166 – 1661R → G in AAB93421. (PubMed:9409776)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U64721 Genomic DNA. Translation: AAB93421.1.
AE013599 Genomic DNA. Translation: AAF57875.1.
AY061404 mRNA. Translation: AAL28952.1.
RefSeqiNP_477202.2. NM_057854.4.
NP_725669.1. NM_166221.4.
UniGeneiDm.3609.

Genome annotation databases

EnsemblMetazoaiFBtr0086910; FBpp0086066; FBgn0016697.
FBtr0086911; FBpp0086067; FBgn0016697.
GeneIDi36951.
KEGGidme:Dmel_CG10938.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U64721 Genomic DNA. Translation: AAB93421.1 .
AE013599 Genomic DNA. Translation: AAF57875.1 .
AY061404 mRNA. Translation: AAL28952.1 .
RefSeqi NP_477202.2. NM_057854.4.
NP_725669.1. NM_166221.4.
UniGenei Dm.3609.

3D structure databases

ProteinModelPortali Q95083.
SMRi Q95083. Positions 8-243.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 62645. 37 interactions.
DIPi DIP-19014N.
IntActi Q95083. 2 interactions.
MINTi MINT-966233.
STRINGi 7227.FBpp0086066.

Proteomic databases

PaxDbi Q95083.
PRIDEi Q95083.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0086910 ; FBpp0086066 ; FBgn0016697 .
FBtr0086911 ; FBpp0086067 ; FBgn0016697 .
GeneIDi 36951.
KEGGi dme:Dmel_CG10938.

Organism-specific databases

CTDi 36951.
FlyBasei FBgn0016697. Prosalpha5.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00550000074958.
InParanoidi Q95083.
KOi K02729.
OMAi CAMSGLT.
OrthoDBi EOG769ZKB.
PhylomeDBi Q95083.

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 36951.
NextBioi 801184.
PROi Q95083.

Gene expression databases

Bgeei Q95083.

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. "Molecular cloning of the Drosophila melanogaster gene alpha5_dm encoding a 20S proteasome alpha-type subunit."
    Zaiss D., Belote J.M.
    Gene 201:99-105(1997) [PubMed] [Europe PMC] [Abstract]
    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.

Entry informationi

Entry nameiPSA5_DROME
AccessioniPrimary (citable) accession number: Q95083
Secondary accession number(s): Q0E942, Q9V809
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 8, 2000
Last modified: November 26, 2014
This is version 127 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