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Protein

Proteasome subunit alpha type-1

Gene

Prosalpha6

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: 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. proteasome-mediated ubiquitin-dependent protein catabolic process Source: FlyBase
  2. ventral furrow formation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

ReactomeiREACT_273531. CDK-mediated phosphorylation and removal of Cdc6.
REACT_274251. degradation of AXIN.
REACT_274764. ER-Phagosome pathway.
REACT_274899. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_283069. Degradation of GLI2 by the proteasome.
REACT_284680. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_285954. APC/C:Cdc20 mediated degradation of Securin.
REACT_287787. Activation of NF-kappaB in B cells.
REACT_289889. GLI3 is processed to GLI3R by the proteasome.
REACT_293133. Degradation of GLI1 by the proteasome.
REACT_299289. degradation of DVL.
REACT_304845. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_307080. Hh ligand biogenesis disease.
REACT_308142. Hedgehog ligand biogenesis.
REACT_320700. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_323570. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_329319. SCF(Skp2)-mediated degradation of p27/p21.
REACT_330960. Hedgehog 'on' state.
REACT_333353. Asymmetric localization of PCP proteins.
REACT_335389. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_335593. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_335971. SCF-beta-TrCP mediated degradation of Emi1.
REACT_336807. Regulation of ornithine decarboxylase (ODC).
REACT_337097. Ubiquitin-dependent degradation of Cyclin D1.
REACT_343999. Orc1 removal from chromatin.
REACT_346613. Separation of Sister Chromatids.
REACT_347454. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_354443. Degradation of beta-catenin by the destruction complex.

Protein family/group databases

MEROPSiT01.976.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-1 (EC:3.4.25.1)
Alternative name(s):
PROS-Dm35
Proteasome 35 kDa subunit
Gene namesi
Name:Prosalpha6
Synonyms:PROS-35, Pros35
ORF Names:CG4904
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0250843. Prosalpha6.

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 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 – 279279Proteasome subunit alpha type-1PRO_0000124068Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei103 – 1031PhosphotyrosineSequence Analysis

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP12881.
PRIDEiP12881.

Expressioni

Gene expression databases

BgeeiP12881.
ExpressionAtlasiP12881. 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

BioGridi60450. 51 interactions.
DIPiDIP-22159N.
IntActiP12881. 13 interactions.
MINTiMINT-1759709.

Structurei

3D structure databases

ProteinModelPortaliP12881.
SMRiP12881. Positions 4-231.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074855.
InParanoidiP12881.
KOiK02725.
OMAiFMKQQCL.
OrthoDBiEOG7WQ7T1.
PhylomeDBiP12881.

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.

P12881-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFRNQYDSDV TVWSPQGRLH QVEYAMEAVK LGTATVGLKN KDYAVLVALC
60 70 80 90 100
KPTSELSDTQ RKIIPIDDHL GISIAGLTAD ARVLSRYLRS ECLNYKHSYD
110 120 130 140 150
TTYPVSRLIT NLGNKMQTTT QRYDRRPYGV GLLVAGYDER GPHIYQVTPS
160 170 180 190 200
ATFFNCKANS IGSRSQSART YLEKNLNKFL DSSKDEIIRH GIRAILGTLP
210 220 230 240 250
TDEQGKDAGQ YDITVAIVGK DQPFTILSNK DSAKHVAIAK ENDNDTPRND
260 270
DDDDRPSPPE EPAAGPRDPE VLVATEQRP
Length:279
Mass (Da):31,059
Last modified:September 30, 1989 - v1
Checksum:i1478BDC2C61EF3F1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti189 – 1891R → H in AAL48800 (PubMed:12537569).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15497 mRNA. Translation: CAA33520.1.
X62285 Genomic DNA. Translation: CAA44173.1.
AE014134 Genomic DNA. Translation: AAF52875.1.
AY071178 mRNA. Translation: AAL48800.1.
PIRiS23450. SNFF5K.
RefSeqiNP_001285798.1. NM_001298869.1.
NP_523532.1. NM_078808.4.
UniGeneiDm.2599.

Genome annotation databases

EnsemblMetazoaiFBtr0079948; FBpp0079538; FBgn0250843.
FBtr0343606; FBpp0310201; FBgn0250843.
GeneIDi34359.
KEGGidme:Dmel_CG4904.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15497 mRNA. Translation: CAA33520.1.
X62285 Genomic DNA. Translation: CAA44173.1.
AE014134 Genomic DNA. Translation: AAF52875.1.
AY071178 mRNA. Translation: AAL48800.1.
PIRiS23450. SNFF5K.
RefSeqiNP_001285798.1. NM_001298869.1.
NP_523532.1. NM_078808.4.
UniGeneiDm.2599.

3D structure databases

ProteinModelPortaliP12881.
SMRiP12881. Positions 4-231.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi60450. 51 interactions.
DIPiDIP-22159N.
IntActiP12881. 13 interactions.
MINTiMINT-1759709.

Protein family/group databases

MEROPSiT01.976.

Proteomic databases

PaxDbiP12881.
PRIDEiP12881.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0079948; FBpp0079538; FBgn0250843.
FBtr0343606; FBpp0310201; FBgn0250843.
GeneIDi34359.
KEGGidme:Dmel_CG4904.

Organism-specific databases

CTDi34359.
FlyBaseiFBgn0250843. Prosalpha6.

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074855.
InParanoidiP12881.
KOiK02725.
OMAiFMKQQCL.
OrthoDBiEOG7WQ7T1.
PhylomeDBiP12881.

Enzyme and pathway databases

ReactomeiREACT_273531. CDK-mediated phosphorylation and removal of Cdc6.
REACT_274251. degradation of AXIN.
REACT_274764. ER-Phagosome pathway.
REACT_274899. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_283069. Degradation of GLI2 by the proteasome.
REACT_284680. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_285954. APC/C:Cdc20 mediated degradation of Securin.
REACT_287787. Activation of NF-kappaB in B cells.
REACT_289889. GLI3 is processed to GLI3R by the proteasome.
REACT_293133. Degradation of GLI1 by the proteasome.
REACT_299289. degradation of DVL.
REACT_304845. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_307080. Hh ligand biogenesis disease.
REACT_308142. Hedgehog ligand biogenesis.
REACT_320700. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_323570. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_329319. SCF(Skp2)-mediated degradation of p27/p21.
REACT_330960. Hedgehog 'on' state.
REACT_333353. Asymmetric localization of PCP proteins.
REACT_335389. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_335593. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_335971. SCF-beta-TrCP mediated degradation of Emi1.
REACT_336807. Regulation of ornithine decarboxylase (ODC).
REACT_337097. Ubiquitin-dependent degradation of Cyclin D1.
REACT_343999. Orc1 removal from chromatin.
REACT_346613. Separation of Sister Chromatids.
REACT_347454. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_354443. Degradation of beta-catenin by the destruction complex.

Miscellaneous databases

GenomeRNAii34359.
NextBioi788106.

Gene expression databases

BgeeiP12881.
ExpressionAtlasiP12881. 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. "The PROS-35 gene encodes the 35 kd protein subunit of Drosophila melanogaster proteasome."
    Haass C., Pesold-Hurt B., Multhaup G., Beyreuther K., Kloetzel P.-M.
    EMBO J. 8:2373-2379(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 4-18 AND 194-206.
    Strain: Oregon-R.
  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(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Oregon-R.
  3. "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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  6. "Proteasome regulation by ADP-ribosylation."
    Cho-Park P.F., Steller H.
    Cell 153:614-627(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PI31.

Entry informationi

Entry nameiPSA1_DROME
AccessioniPrimary (citable) accession number: P12881
Secondary accession number(s): Q8SZ22, Q9VL23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 30, 1989
Last sequence update: September 30, 1989
Last modified: March 31, 2015
This is version 144 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, Direct protein sequencing, 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.