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Q24178 (PSA72_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proteasome subunit alpha type-7-1A

EC=3.4.25.1
Alternative name(s):
Testis-specific alpha4-t1 proteasome subunit
Testis-specific proteasome 28 kDa subunit 1A
Gene names
Name:Prosalpha4T1
Synonyms:Pros28.1A
ORF Names:CG17268
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length249 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 activity

Cleavage of peptide bonds with very broad specificity.

Subunit structure

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.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Tissue specificity

Testis specific.

Sequence similarities

Belongs to the peptidase T1A family.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
Proteasome
   Coding sequence diversityPolymorphism
   Molecular functionHydrolase
Protease
Threonine protease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

proteasome core complex, alpha-subunit complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionthreonine-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 249249Proteasome subunit alpha type-7-1A
PRO_0000124154

Natural variations

Natural variant291R → P in strain: CPA-46.
Natural variant2361N → K in strain: CPA-46.

Experimental info

Sequence conflict241A → G in AAC47280. Ref.1
Sequence conflict1231C → V in AAC47280. Ref.1
Sequence conflict127 – 1282RP → PS in AAC47280. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q24178 [UniParc].

Last modified December 8, 2000. Version 2.
Checksum: 18B642DE3F1AE453

FASTA24927,940
        10         20         30         40         50         60 
MSSRYGRALT IFSPDGHLLQ VEYAQEAVRK GSTAVGVRGA NCVVLGVEKS SVSEMQEDRT 

        70         80         90        100        110        120 
VRKISMLDRH VALAFAGLTA DARILINRGQ VECQSHRLNF ENQVTLEYIT RYLAQLKQKY 

       130        140        150        160        170        180 
TQCNGRRPFG ISCLIGGIDA DGSARLFHTE PSGIFHEYKA TATGRWANTV REFFEKAYSD 

       190        200        210        220        230        240 
HEVTTKCDAI KLAMRALLEV TQMSQMRLEV AVLENGKPMK MLDSVVISEI VKIVQNEKEL 


QAKAHKMKR 

« Hide

References

« Hide 'large scale' references
[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].
[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, 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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[5]Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. expand/collapse author list , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U46008 Genomic DNA. Translation: AAC47280.1.
AY542403 Genomic DNA. Translation: AAS86247.1.
AY542404 Genomic DNA. Translation: AAS86248.1.
AY542405 Genomic DNA. Translation: AAS86249.1.
AY542406 Genomic DNA. Translation: AAS86250.1.
AY542407 Genomic DNA. Translation: AAS86251.1.
AY542408 Genomic DNA. Translation: AAS86252.1.
AY542409 Genomic DNA. Translation: AAS86253.1.
AE014297 Genomic DNA. Translation: AAF55802.1.
AY075276 mRNA. Translation: AAL68143.1.
PIRS72225.
RefSeqNP_650910.1. NM_142653.3.
UniGeneDm.5563.

3D structure databases

ProteinModelPortalQ24178.
SMRQ24178. Positions 5-231.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid67432. 1 interaction.
DIPDIP-19969N.
MINTMINT-1548416.

Proteomic databases

PaxDbQ24178.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0083928; FBpp0083336; FBgn0017557.
GeneID42457.
KEGGdme:Dmel_CG17268.

Organism-specific databases

CTD42457.
FlyBaseFBgn0265606. Prosalpha4T1.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00550000074753.
InParanoidQ24178.
KOK02731.
OMAHEYKATA.
PhylomeDBQ24178.

Gene expression databases

BgeeQ24178.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
InterProIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMSSF56235. SSF56235. 1 hit.
PROSITEPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi42457.
NextBio828889.

Entry information

Entry namePSA72_DROME
AccessionPrimary (citable) accession number: Q24178
Secondary accession number(s): Q6QH19, Q8T8U0, Q9VDJ1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: December 8, 2000
Last modified: July 9, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase