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Protein

Proteasome subunit alpha type-4-like

Gene

Prosalpha3T

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 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. proteasome-mediated ubiquitin-dependent protein catabolic process Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Protein family/group databases

MEROPSiT01.973.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-4-like (EC:3.4.25.1)
Gene namesi
Name:Prosalpha3T
ORF Names:CG1736
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0261395. Prosalpha3T.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. male germ cell nucleus Source: FlyBase
  2. proteasome core complex, alpha-subunit complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 251251Proteasome subunit alpha type-4-likePRO_0000124110Add
BLAST

Proteomic databases

PaxDbiQ9VA12.
PRIDEiQ9VA12.

Expressioni

Tissue specificityi

Testis, prominent after meiosis II. After meiosis, predominantly localized to the haploid spermatid nuclei of the 64-cell cysts, remaining during the elongation and condensation of the spermatid nuclei. In mature, motile sperm, expression is seen exclusively in the sperm head.1 Publication

Gene expression databases

BgeeiQ9VA12.

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

Protein-protein interaction databases

BioGridi68527. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9VA12.
SMRiQ9VA12. Positions 2-239.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074827.
HOGENOMiHOG000263951.
InParanoidiQ9VA12.
KOiK02728.
OMAiCCATGNT.
OrthoDBiEOG7F512J.
PhylomeDBiQ9VA12.

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.

Q9VA12-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARFFDSRTT IFSPEGRLYQ VEYAMEAASQ SGTCVGLLAK NGVLLATERS
60 70 80 90 100
VDKLMDTSIP VPRISWLNEN IACCATGNTA DGNVLVNQLR MIAQQYQFNF
110 120 130 140 150
GEMIPCEQLV TNLCDIKQAY TQYGGKRPFG VSFLYMGWDC RFGFQLYQSD
160 170 180 190 200
PSGNYSGWKA TCIGRKSGAA MEMLQKELFS KGYVSPSVEE AKDVAIKVMG
210 220 230 240 250
MTLGRDSLTP EKLEIAFVQR YGNTTVFHIL EKNEIHRLIE RNNNLKRRVG

S
Length:251
Mass (Da):28,169
Last modified:May 1, 2000 - v1
Checksum:iB1AFF83978DB14D3
GO

Sequence cautioni

The sequence ACD81826.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 752CA → WP in AAN63094. (PubMed:12421421)Curated
Sequence conflicti133 – 1331F → L in AAN63094. (PubMed:12421421)Curated
Sequence conflicti141 – 1422RF → AS in AAN63094. (PubMed:12421421)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAF57116.1.
AY147240 Genomic DNA. Translation: AAN63094.1.
BT032812 mRNA. Translation: ACD81826.1. Different initiation.
RefSeqiNP_651843.1. NM_143586.3.

Genome annotation databases

EnsemblMetazoaiFBtr0085738; FBpp0085100; FBgn0261395.
GeneIDi43679.
KEGGidme:Dmel_CG1736.
UCSCiCG1736-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAF57116.1.
AY147240 Genomic DNA. Translation: AAN63094.1.
BT032812 mRNA. Translation: ACD81826.1. Different initiation.
RefSeqiNP_651843.1. NM_143586.3.

3D structure databases

ProteinModelPortaliQ9VA12.
SMRiQ9VA12. Positions 2-239.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68527. 1 interaction.

Protein family/group databases

MEROPSiT01.973.

Proteomic databases

PaxDbiQ9VA12.
PRIDEiQ9VA12.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0085738; FBpp0085100; FBgn0261395.
GeneIDi43679.
KEGGidme:Dmel_CG1736.
UCSCiCG1736-RA. d. melanogaster.

Organism-specific databases

CTDi43679.
FlyBaseiFBgn0261395. Prosalpha3T.

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074827.
HOGENOMiHOG000263951.
InParanoidiQ9VA12.
KOiK02728.
OMAiCCATGNT.
OrthoDBiEOG7F512J.
PhylomeDBiQ9VA12.

Miscellaneous databases

GenomeRNAii43679.
NextBioi835221.

Gene expression databases

BgeeiQ9VA12.

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. "Expression of proteasome subunit isoforms during spermatogenesis in Drosophila melanogaster."
    Ma J., Katz E., Belote J.M.
    Insect Mol. Biol. 11:627-639(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Testis.
  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. Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.

Entry informationi

Entry nameiPSA4L_DROME
AccessioniPrimary (citable) accession number: Q9VA12
Secondary accession number(s): B3DN24, Q8IS89
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: May 1, 2000
Last modified: February 4, 2015
This is version 110 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, 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.