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Protein

Proteasome subunit alpha type-7-1B

Gene

Prosalpha4T2

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

Keywordsi

Molecular functionHydrolase, 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-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-2871837 FCERI mediated NF-kB activation
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-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-8939902 Regulation of RUNX2 expression and activity
R-DME-8941858 Regulation of RUNX3 expression and activity
R-DME-8948751 Regulation of PTEN stability and activity
R-DME-9020702 Interleukin-1 signaling
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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0017556 Prosalpha4T2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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 differential
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
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR023332 Proteasome_alpha-type
IPR037560 Proteasome_alpha_7-like
IPR000426 Proteasome_asu_N
IPR001353 Proteasome_sua/b
PANTHERiPTHR11599:SF15 PTHR11599:SF15, 1 hit
PfamiView protein in Pfam
PF00227 Proteasome, 1 hit
PF10584 Proteasome_A_N, 1 hit
SMARTiView protein in SMART
SM00948 Proteasome_A_N, 1 hit
SUPFAMiSSF56235 SSF56235, 1 hit
PROSITEiView protein in PROSITE
PS00388 PROTEASOME_ALPHA_1, 1 hit
PS51475 PROTEASOME_ALPHA_2, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiPSA73_DROME
AccessioniPrimary (citable) accession number: Q27575
Secondary accession number(s): Q6QH11, Q8T3X2, Q9W162
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: December 8, 2000
Last modified: May 23, 2018
This is version 152 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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