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Protein

Proteasome subunit alpha type-3

Gene

Psma3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Binds to the C-terminus of CDKN1A and thereby mediates its degradation. Negatively regulates the membrane trafficking of the cell-surface thromboxane A2 receptor (TBXA2R) isoform 2.By similarity

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-RNO-1169091 Activation of NF-kappaB in B cells
R-RNO-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-RNO-1236978 Cross-presentation of soluble exogenous antigens (endosomes)
R-RNO-174084 Autodegradation of Cdh1 by Cdh1:APC/C
R-RNO-174113 SCF-beta-TrCP mediated degradation of Emi1
R-RNO-174154 APC/C:Cdc20 mediated degradation of Securin
R-RNO-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-RNO-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-RNO-187577 SCF(Skp2)-mediated degradation of p27/p21
R-RNO-195253 Degradation of beta-catenin by the destruction complex
R-RNO-202424 Downstream TCR signaling
R-RNO-2467813 Separation of Sister Chromatids
R-RNO-2871837 FCERI mediated NF-kB activation
R-RNO-349425 Autodegradation of the E3 ubiquitin ligase COP1
R-RNO-350562 Regulation of ornithine decarboxylase (ODC)
R-RNO-382556 ABC-family proteins mediated transport
R-RNO-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-RNO-4608870 Asymmetric localization of PCP proteins
R-RNO-4641257 Degradation of AXIN
R-RNO-4641258 Degradation of DVL
R-RNO-5358346 Hedgehog ligand biogenesis
R-RNO-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-RNO-5607764 CLEC7A (Dectin-1) signaling
R-RNO-5610780 Degradation of GLI1 by the proteasome
R-RNO-5610785 GLI3 is processed to GLI3R by the proteasome
R-RNO-5632684 Hedgehog 'on' state
R-RNO-5658442 Regulation of RAS by GAPs
R-RNO-5668541 TNFR2 non-canonical NF-kB pathway
R-RNO-5676590 NIK-->noncanonical NF-kB signaling
R-RNO-5687128 MAPK6/MAPK4 signaling
R-RNO-5689603 UCH proteinases
R-RNO-5689880 Ub-specific processing proteases
R-RNO-68827 CDT1 association with the CDC6:ORC:origin complex
R-RNO-68949 Orc1 removal from chromatin
R-RNO-69017 CDK-mediated phosphorylation and removal of Cdc6
R-RNO-69229 Ubiquitin-dependent degradation of Cyclin D1
R-RNO-69481 G2/M Checkpoints
R-RNO-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-RNO-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-RNO-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-RNO-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-RNO-8939902 Regulation of RUNX2 expression and activity
R-RNO-8941858 Regulation of RUNX3 expression and activity
R-RNO-8948751 Regulation of PTEN stability and activity
R-RNO-9020702 Interleukin-1 signaling
R-RNO-983168 Antigen processing: Ubiquitination & Proteasome degradation

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-3 (EC:3.4.25.1By similarity)
Alternative name(s):
Macropain subunit C8
Multicatalytic endopeptidase complex subunit C8
Proteasome component C8
Proteasome subunit K
Gene namesi
Name:Psma3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi61844 Psma3

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
Initiator methionineiRemoved1 Publication
ChainiPRO_00001240932 – 255Proteasome subunit alpha type-3Add BLAST254

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine1 Publication1
Modified residuei57N6-acetyllysineBy similarity1
Modified residuei206N6-acetyllysineBy similarity1
Modified residuei230N6-acetyllysineBy similarity1
Modified residuei243PhosphoserineCombined sources1
Modified residuei250PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP18422
PRIDEiP18422

2D gel databases

World-2DPAGEi0004:P18422

PTM databases

iPTMnetiP18422
PhosphoSitePlusiP18422

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSRNOG00000007851
GenevisibleiP18422 RN

Interactioni

Subunit structurei

The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is a barrel-shaped complex made of 28 subunits that are arranged in four stacked rings. The two outer rings are each formed by seven alpha subunits, and the two inner rings are formed by seven beta subunits. The proteolytic activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7. Interacts with AURKB. Interacts with CDKN1A. Interacts with MDM2 and RB1. Interacts with the C-terminus of TBXA2R isoform 2. Interacts with DNAJB2.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi248291, 2 interactors
268414, 1 interactor
STRINGi10116.ENSRNOP00000010753

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6EPCelectron microscopy12.30G1-255[»]
6EPDelectron microscopy15.40G1-255[»]
6EPEelectron microscopy12.80G1-255[»]
6EPFelectron microscopy11.80G1-255[»]
ProteinModelPortaliP18422
SMRiP18422
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0184 Eukaryota
ENOG410XP01 LUCA
GeneTreeiENSGT00550000074912
HOGENOMiHOG000091086
HOVERGENiHBG105566
InParanoidiP18422
KOiK02727
OMAiFELEMTW
OrthoDBiEOG091G0GQL
PhylomeDBiP18422
TreeFamiTF106208

Family and domain databases

Gene3Di3.60.20.10, 1 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR023332 Proteasome_alpha-type
IPR037555 Proteasome_alpha_3
IPR000426 Proteasome_asu_N
IPR001353 Proteasome_sua/b
PANTHERiPTHR11599:SF10 PTHR11599:SF10, 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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P18422-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSIGTGYDL SASTFSPDGR VFQVEYAMKA VENSSTAIGI RCKDGVVFGV
60 70 80 90 100
EKLVLSKLYE EGSNKRLFNV DRHVGMAVAG LLADARSLAD IAREEASNFR
110 120 130 140 150
SNFGYNIPLK HLADRVAMYV HAYTLYSAVR PFGCSFMLGS YSVNDGAQLY
160 170 180 190 200
MIDPSGVSYG YWGCAIGKAR QAAKTEIEKL QMKEMTCRDV VKEVAKIIYI
210 220 230 240 250
VHDEVKDKAF ELELSWVGEL TKGRHEIVPK DVREEAEKYA KESLKEEDES

DDDNM
Length:255
Mass (Da):28,419
Last modified:January 23, 2007 - v3
Checksum:iF07FCB33A2E79FA7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55985 mRNA Translation: CAA39457.1
D90258 mRNA Translation: BAA14302.1
M58593 mRNA Translation: AAA40840.1
BC081817 mRNA Translation: AAH81817.1
PIRiS14004 SNRTC8
RefSeqiNP_001004094.1, NM_001004094.1
NP_058976.1, NM_017280.2
UniGeneiRn.129822
Rn.3997

Genome annotation databases

EnsembliENSRNOT00000010753; ENSRNOP00000010753; ENSRNOG00000007851
GeneIDi29670
408248
KEGGirno:29670
rno:408248
UCSCiRGD:61844 rat

Similar proteinsi

Entry informationi

Entry nameiPSA3_RAT
AccessioniPrimary (citable) accession number: P18422
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 160 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

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