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Protein

Proteasome subunit alpha type-6

Gene

Prosalpha1

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

Protein family/group databases

MEROPSiT01.971.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-6 (EC:3.4.25.1)
Alternative name(s):
20S proteasome subunit alpha-1
Gene namesi
Name:Prosalpha1
Synonyms:Prosalpha6
ORF Names:CG18495
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0263121. Prosalpha1.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
  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-6PRO_0000124134Add
BLAST

Proteomic databases

PaxDbiQ9XZJ4.
PRIDEiQ9XZJ4.

Expressioni

Gene expression databases

ExpressionAtlasiQ9XZJ4. differential.

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

Protein-protein interaction databases

BioGridi69878. 49 interactions.
IntActiQ9XZJ4. 11 interactions.
MINTiMINT-1330620.
STRINGi7227.FBpp0087968.

Structurei

3D structure databases

ProteinModelPortaliQ9XZJ4.
SMRiQ9XZJ4. Positions 2-243.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074807.
InParanoidiQ9XZJ4.
KOiK02730.
OMAiRMANINQ.
OrthoDBiEOG70PBZH.
PhylomeDBiQ9XZJ4.

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.

Q9XZJ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRGSSAGFD RHITIFSPEG RLYQVEYAFK AIAQENITTV ALKSGDCAVV
60 70 80 90 100
ATQKKVTEKN IVPETVTHLF RITKDIGCAM TGRIADSRSQ VQKARYEAAN
110 120 130 140 150
FRYKYGYEMP VDVLCRRIAD INQVYTQNAE MRPLGCSMVL IAYDNEIGPS
160 170 180 190 200
VYKTDPAGYF SGFKACSVGA KTLEANSYLE KKYKPNLSEE KAIQLAISCL
210 220 230 240
SSVLAIDFKP NGIEIGVVSK SDPTFRILDE REIEEHLTKI AEKD
Length:244
Mass (Da):27,162
Last modified:December 8, 2000 - v2
Checksum:iD217B272CA339D05
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941A → G in AAD33944 (Ref. 1) Curated
Sequence conflicti122 – 1221N → T in AAD33944 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF144749 mRNA. Translation: AAD33944.1.
AE013599 Genomic DNA. Translation: AAF59183.1.
AY118637 mRNA. Translation: AAM50006.1.
RefSeqiNP_001163078.1. NM_001169607.1.
NP_524837.2. NM_080098.4.
NP_724614.1. NM_165565.3.
NP_724616.1. NM_165567.4.
UniGeneiDm.36589.

Genome annotation databases

EnsemblMetazoaiFBtr0088894; FBpp0087968; FBgn0050382.
FBtr0088895; FBpp0087969; FBgn0263121.
FBtr0088896; FBpp0087970; FBgn0263121.
FBtr0302223; FBpp0291433; FBgn0050382.
GeneIDi246582.
45780.
KEGGidme:Dmel_CG18495.
dme:Dmel_CG30382.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF144749 mRNA. Translation: AAD33944.1.
AE013599 Genomic DNA. Translation: AAF59183.1.
AY118637 mRNA. Translation: AAM50006.1.
RefSeqiNP_001163078.1. NM_001169607.1.
NP_524837.2. NM_080098.4.
NP_724614.1. NM_165565.3.
NP_724616.1. NM_165567.4.
UniGeneiDm.36589.

3D structure databases

ProteinModelPortaliQ9XZJ4.
SMRiQ9XZJ4. Positions 2-243.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi69878. 49 interactions.
IntActiQ9XZJ4. 11 interactions.
MINTiMINT-1330620.
STRINGi7227.FBpp0087968.

Protein family/group databases

MEROPSiT01.971.

Proteomic databases

PaxDbiQ9XZJ4.
PRIDEiQ9XZJ4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0088894; FBpp0087968; FBgn0050382.
FBtr0088895; FBpp0087969; FBgn0263121.
FBtr0088896; FBpp0087970; FBgn0263121.
FBtr0302223; FBpp0291433; FBgn0050382.
GeneIDi246582.
45780.
KEGGidme:Dmel_CG18495.
dme:Dmel_CG30382.

Organism-specific databases

CTDi45780.
FlyBaseiFBgn0263121. Prosalpha1.

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074807.
InParanoidiQ9XZJ4.
KOiK02730.
OMAiRMANINQ.
OrthoDBiEOG70PBZH.
PhylomeDBiQ9XZJ4.

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.

Miscellaneous databases

NextBioi843091.
PROiQ9XZJ4.

Gene expression databases

ExpressionAtlasiQ9XZJ4. differential.

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. "Drosophila melanogaster 20S proteasome subunit alpha1 cDNA."
    Belote J.
    Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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 nameiPSA6_DROME
AccessioniPrimary (citable) accession number: Q9XZJ4
Secondary accession number(s): Q0E9G1, Q9V324
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: December 8, 2000
Last modified: February 4, 2015
This is version 119 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

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.