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Q27575

- PSA73_DROME

UniProt

Q27575 - PSA73_DROME

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Protein

Proteasome subunit alpha type-7-1B

Gene
Prosalpha4T2, Pros28.1B, CG4569
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.

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

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-SubCell
  2. nucleus Source: UniProtKB-SubCell
  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.

Structurei

3D structure databases

ProteinModelPortaliQ27575.
SMRiQ27575. Positions 5-244.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.

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

MAQRYDRAVT IYSPDGHLLQ VEYAQEAVRR GSTVMGLRTN NAIVIGVEKR    50
SVGDLQEERM VRKICMLDDH VVMTFSGLTA DARILVSRAQ MEAQSHRLNF 100
EKPTTVEYIT RYIAQLKQNY TQSNGRRPFG LSCLVGGFDE DGTPHLFQTD 150
PSGIFYEWRA NTTGRSSQPV RDYMEKHADE ILTIADEAAA IKHIVRTLVS 200
VSSLNHTQME VAVLKYRQPL RMIDHQVLAD LERTVRREIE DEAEASRRPR 250
AP 252
Length:252
Mass (Da):28,720
Last modified:December 8, 2000 - v2
Checksum:i00116788A4813146
GO

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 42QR → HG in AAC47281. 1 Publication
Sequence conflicti188 – 1903AAA → RG in AAC47281. 1 Publication
Sequence conflicti215 – 2151K → N in AAL90194. 1 Publication
Sequence conflicti243 – 2497AEASRRP → PSESA in AAC47281. 1 Publication
Sequence conflicti245 – 2451A → V in AAL90194. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_611920.1. NM_138076.3.
UniGeneiDm.772.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_611920.1. NM_138076.3.
UniGenei Dm.772.

3D structure databases

ProteinModelPortali Q27575.
SMRi Q27575. Positions 5-244.
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.

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: July 9, 2014
This is version 117 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