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Protein

Proteasome subunit alpha type-7-1B

Gene

Prosalpha4T2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

ReactomeiR-DME-1169091. Activation of NF-kappaB in B cells.
R-DME-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-DME-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-DME-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-DME-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-DME-174154. APC/C:Cdc20 mediated degradation of Securin.
R-DME-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-DME-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-DME-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-DME-195253. Degradation of beta-catenin by the destruction complex.
R-DME-202424. Downstream TCR signaling.
R-DME-2467813. Separation of Sister Chromatids.
R-DME-2871837. FCERI mediated NF-kB activation.
R-DME-350562. Regulation of ornithine decarboxylase (ODC).
R-DME-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-DME-4608870. Asymmetric localization of PCP proteins.
R-DME-4641257. Degradation of AXIN.
R-DME-4641258. Degradation of DVL.
R-DME-5358346. Hedgehog ligand biogenesis.
R-DME-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-DME-5607764. CLEC7A (Dectin-1) signaling.
R-DME-5610780. Degradation of GLI1 by the proteasome.
R-DME-5610785. GLI3 is processed to GLI3R by the proteasome.
R-DME-5632684. Hedgehog 'on' state.
R-DME-5658442. Regulation of RAS by GAPs.
R-DME-5676590. NIK-->noncanonical NF-kB signaling.
R-DME-5689603. UCH proteinases.
R-DME-5689880. Ub-specific processing proteases.
R-DME-68949. Orc1 removal from chromatin.
R-DME-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-DME-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-DME-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-DME-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-DME-983168. Antigen processing: Ubiquitination & Proteasome degradation.

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
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0017556. Prosalpha4T2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001241551 – 252Proteasome subunit alpha type-7-1BAdd BLAST252

Proteomic databases

PaxDbiQ27575.
PRIDEiQ27575.

Expressioni

Tissue specificityi

Testis specific.

Gene expression databases

BgeeiFBgn0017556.
ExpressionAtlasiQ27575. baseline.
GenevisibleiQ27575. DM.

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

STRINGi7227.FBpp0072257.

Structurei

3D structure databases

ProteinModelPortaliQ27575.
SMRiQ27575.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0183. Eukaryota.
ENOG410XP21. LUCA.
GeneTreeiENSGT00550000074753.
InParanoidiQ27575.
KOiK02731.
OMAiHIVRTLV.
OrthoDBiEOG091G0GX6.
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)DescriptionActionsGraphical viewLength
Sequence conflicti3 – 4QR → HG in AAC47281 (PubMed:8878681).Curated2
Sequence conflicti188 – 190AAA → RG in AAC47281 (PubMed:8878681).Curated3
Sequence conflicti215K → N in AAL90194 (PubMed:12537569).Curated1
Sequence conflicti243 – 249AEASRRP → PSESA in AAC47281 (PubMed:8878681).Curated7
Sequence conflicti245A → V in AAL90194 (PubMed:12537569).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti45I → L in strain: S-23. 1
Natural varianti191I → V in strain: S-23. 1
Natural varianti213V → E in strain: S-23. 1
Natural varianti241D → A in strain: S-23. 1

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.
FBtr0343481; FBpp0310089; 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.
PIRiS72226.
RefSeqiNP_001286844.1. NM_001299915.1.
NP_611920.1. NM_138076.4.

3D structure databases

ProteinModelPortaliQ27575.
SMRiQ27575.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7227.FBpp0072257.

Proteomic databases

PaxDbiQ27575.
PRIDEiQ27575.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0072350; FBpp0072257; FBgn0017556.
FBtr0343481; FBpp0310089; FBgn0017556.
GeneIDi37910.
KEGGidme:Dmel_CG4569.

Organism-specific databases

CTDi37910.
FlyBaseiFBgn0017556. Prosalpha4T2.

Phylogenomic databases

eggNOGiKOG0183. Eukaryota.
ENOG410XP21. LUCA.
GeneTreeiENSGT00550000074753.
InParanoidiQ27575.
KOiK02731.
OMAiHIVRTLV.
OrthoDBiEOG091G0GX6.
PhylomeDBiQ27575.

Enzyme and pathway databases

ReactomeiR-DME-1169091. Activation of NF-kappaB in B cells.
R-DME-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-DME-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-DME-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-DME-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-DME-174154. APC/C:Cdc20 mediated degradation of Securin.
R-DME-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-DME-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-DME-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-DME-195253. Degradation of beta-catenin by the destruction complex.
R-DME-202424. Downstream TCR signaling.
R-DME-2467813. Separation of Sister Chromatids.
R-DME-2871837. FCERI mediated NF-kB activation.
R-DME-350562. Regulation of ornithine decarboxylase (ODC).
R-DME-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-DME-4608870. Asymmetric localization of PCP proteins.
R-DME-4641257. Degradation of AXIN.
R-DME-4641258. Degradation of DVL.
R-DME-5358346. Hedgehog ligand biogenesis.
R-DME-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-DME-5607764. CLEC7A (Dectin-1) signaling.
R-DME-5610780. Degradation of GLI1 by the proteasome.
R-DME-5610785. GLI3 is processed to GLI3R by the proteasome.
R-DME-5632684. Hedgehog 'on' state.
R-DME-5658442. Regulation of RAS by GAPs.
R-DME-5676590. NIK-->noncanonical NF-kB signaling.
R-DME-5689603. UCH proteinases.
R-DME-5689880. Ub-specific processing proteases.
R-DME-68949. Orc1 removal from chromatin.
R-DME-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-DME-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-DME-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-DME-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-DME-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

GenomeRNAii37910.
PROiQ27575.

Gene expression databases

BgeeiFBgn0017556.
ExpressionAtlasiQ27575. baseline.
GenevisibleiQ27575. DM.

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...

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 30, 2016
This is version 139 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

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 one 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.