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Q27575

- PSA73_DROME

UniProt

Q27575 - PSA73_DROME

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Protein

Proteasome subunit alpha type-7-1B

Gene

Prosalpha4T2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 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. ubiquitin-dependent protein catabolic process Source: InterPro
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-7-1B (EC:3.4.25.1)
Alternative name(s):
Testis-specific alpha4-t2 proteasome subunit
Testis-specific proteasome 28 kDa subunit 1B
Gene namesi
Name:Prosalpha4T2
Synonyms:Pros28.1B
ORF Names:CG4569
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0017556. Prosalpha4T2.

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, 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 – 252252Proteasome subunit alpha type-7-1BPRO_0000124155Add
BLAST

Expressioni

Tissue specificityi

Testis specific.

Gene expression databases

BgeeiQ27575.

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

Structurei

3D structure databases

ProteinModelPortaliQ27575.
SMRiQ27575. Positions 5-245.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074753.
InParanoidiQ27575.
KOiK02731.
OMAiRTKDCIV.
OrthoDBiEOG71VSTG.
PhylomeDBiQ27575.

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.

Q27575-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAQRYDRAVT IYSPDGHLLQ VEYAQEAVRR GSTVMGLRTN NAIVIGVEKR
60 70 80 90 100
SVGDLQEERM VRKICMLDDH VVMTFSGLTA DARILVSRAQ MEAQSHRLNF
110 120 130 140 150
EKPTTVEYIT RYIAQLKQNY TQSNGRRPFG LSCLVGGFDE DGTPHLFQTD
160 170 180 190 200
PSGIFYEWRA NTTGRSSQPV RDYMEKHADE ILTIADEAAA IKHIVRTLVS
210 220 230 240 250
VSSLNHTQME VAVLKYRQPL RMIDHQVLAD LERTVRREIE DEAEASRRPR

AP
Length:252
Mass (Da):28,720
Last modified:December 8, 2000 - v2
Checksum:i00116788A4813146
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 42QR → HG in AAC47281. (PubMed:8878681)Curated
Sequence conflicti188 – 1903AAA → RG in AAC47281. (PubMed:8878681)Curated
Sequence conflicti215 – 2151K → N in AAL90194. (PubMed:12537569)Curated
Sequence conflicti243 – 2497AEASRRP → PSESA in AAC47281. (PubMed:8878681)Curated
Sequence conflicti245 – 2451A → V in AAL90194. (PubMed:12537569)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti45 – 451I → L in strain: S-23.
Natural varianti191 – 1911I → V in strain: S-23.
Natural varianti213 – 2131V → E in strain: S-23.
Natural varianti241 – 2411D → A in strain: S-23.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U46009 Genomic DNA. Translation: AAC47281.1.
AY542417 Genomic DNA. Translation: AAS86225.1.
AY542418 Genomic DNA. Translation: AAS86226.1.
AY542421 Genomic DNA. Translation: AAS86229.1.
AY542422 Genomic DNA. Translation: AAS86230.1.
AY542423 Genomic DNA. Translation: AAS86231.1.
AY542424 Genomic DNA. Translation: AAS86232.1.
AY542425 Genomic DNA. Translation: AAS86233.1.
AY542426 Genomic DNA. Translation: AAS86234.1.
AY542427 Genomic DNA. Translation: AAS86235.1.
AE013599 Genomic DNA. Translation: AAF47215.1.
AY089456 mRNA. Translation: AAL90194.1.
PIRiS72226.
RefSeqiNP_001286844.1. NM_001299915.1.
NP_611920.1. NM_138076.4.

Genome annotation databases

EnsemblMetazoaiFBtr0072350; FBpp0072257; FBgn0017556.
GeneIDi37910.
KEGGidme:Dmel_CG4569.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U46009 Genomic DNA. Translation: AAC47281.1 .
AY542417 Genomic DNA. Translation: AAS86225.1 .
AY542418 Genomic DNA. Translation: AAS86226.1 .
AY542421 Genomic DNA. Translation: AAS86229.1 .
AY542422 Genomic DNA. Translation: AAS86230.1 .
AY542423 Genomic DNA. Translation: AAS86231.1 .
AY542424 Genomic DNA. Translation: AAS86232.1 .
AY542425 Genomic DNA. Translation: AAS86233.1 .
AY542426 Genomic DNA. Translation: AAS86234.1 .
AY542427 Genomic DNA. Translation: AAS86235.1 .
AE013599 Genomic DNA. Translation: AAF47215.1 .
AY089456 mRNA. Translation: AAL90194.1 .
PIRi S72226.
RefSeqi NP_001286844.1. NM_001299915.1.
NP_611920.1. NM_138076.4.

3D structure databases

ProteinModelPortali Q27575.
SMRi Q27575. Positions 5-245.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0072350 ; FBpp0072257 ; FBgn0017556 .
GeneIDi 37910.
KEGGi dme:Dmel_CG4569.

Organism-specific databases

CTDi 37910.
FlyBasei FBgn0017556. Prosalpha4T2.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00550000074753.
InParanoidi Q27575.
KOi K02731.
OMAi RTKDCIV.
OrthoDBi EOG71VSTG.
PhylomeDBi Q27575.

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 37910.
NextBioi 805998.

Gene expression databases

Bgeei Q27575.

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. "Duplicated proteasome subunit genes in Drosophila melanogaster encoding testes-specific isoforms."
    Yuan X., Miller M., Belote J.M.
    Genetics 144:147-157(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Testis.
  2. "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: CPA-129, CPA-46, S-23, Z(H)12, Z(H)16 and Z(H)34.
  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(2000) [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: Testis.

Entry informationi

Entry nameiPSA73_DROME
AccessioniPrimary (citable) accession number: Q27575
Secondary accession number(s): Q6QH11, Q8T3X2, Q9W162
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: December 8, 2000
Last modified: November 26, 2014
This is version 120 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