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Protein

Proteasome subunit alpha type-5

Gene

PSMA5

Organism
Bos taurus (Bovine)
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).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-BTA-1169091 Activation of NF-kappaB in B cells
R-BTA-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-BTA-1236978 Cross-presentation of soluble exogenous antigens (endosomes)
R-BTA-174084 Autodegradation of Cdh1 by Cdh1:APC/C
R-BTA-174113 SCF-beta-TrCP mediated degradation of Emi1
R-BTA-174154 APC/C:Cdc20 mediated degradation of Securin
R-BTA-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-BTA-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-BTA-187577 SCF(Skp2)-mediated degradation of p27/p21
R-BTA-195253 Degradation of beta-catenin by the destruction complex
R-BTA-202424 Downstream TCR signaling
R-BTA-2467813 Separation of Sister Chromatids
R-BTA-2871837 FCERI mediated NF-kB activation
R-BTA-349425 Autodegradation of the E3 ubiquitin ligase COP1
R-BTA-350562 Regulation of ornithine decarboxylase (ODC)
R-BTA-382556 ABC-family proteins mediated transport
R-BTA-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-BTA-4608870 Asymmetric localization of PCP proteins
R-BTA-4641257 Degradation of AXIN
R-BTA-4641258 Degradation of DVL
R-BTA-5358346 Hedgehog ligand biogenesis
R-BTA-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-BTA-5607764 CLEC7A (Dectin-1) signaling
R-BTA-5610780 Degradation of GLI1 by the proteasome
R-BTA-5610785 GLI3 is processed to GLI3R by the proteasome
R-BTA-5632684 Hedgehog 'on' state
R-BTA-5658442 Regulation of RAS by GAPs
R-BTA-5668541 TNFR2 non-canonical NF-kB pathway
R-BTA-5676590 NIK-->noncanonical NF-kB signaling
R-BTA-5687128 MAPK6/MAPK4 signaling
R-BTA-5689603 UCH proteinases
R-BTA-5689880 Ub-specific processing proteases
R-BTA-6798695 Neutrophil degranulation
R-BTA-68827 CDT1 association with the CDC6:ORC:origin complex
R-BTA-68949 Orc1 removal from chromatin
R-BTA-69017 CDK-mediated phosphorylation and removal of Cdc6
R-BTA-69229 Ubiquitin-dependent degradation of Cyclin D1
R-BTA-69481 G2/M Checkpoints
R-BTA-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-BTA-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-BTA-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-BTA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-BTA-8939902 Regulation of RUNX2 expression and activity
R-BTA-8941858 Regulation of RUNX3 expression and activity
R-BTA-8948751 Regulation of PTEN stability and activity
R-BTA-9020702 Interleukin-1 signaling
R-BTA-983168 Antigen processing: Ubiquitination & Proteasome degradation

Protein family/group databases

MEROPSiT01.975

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-5 (EC:3.4.25.1By similarity)
Gene namesi
Name:PSMA5
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 3

Organism-specific databases

VGNCiVGNC:33440 PSMA5

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_00002740331 – 241Proteasome subunit alpha type-5Add BLAST241

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei16PhosphoserineBy similarity1
Modified residuei55PhosphothreonineBy similarity1
Modified residuei56PhosphoserineBy similarity1
Modified residuei63PhosphoserineBy similarity1
Glycosylationi198O-linked (GlcNAc) serineBy similarity1

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ5E987
PeptideAtlasiQ5E987
PRIDEiQ5E987

Expressioni

Gene expression databases

BgeeiENSBTAG00000020641

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 (PubMed:12015144). PSMA5 interacts directly with the PSMG1-PSMG2 heterodimer which promotes 20S proteasome assembly (By similarity).By similarity1 Publication

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000027507

Structurei

Secondary structure

1241
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi22 – 31Combined sources10
Beta strandi37 – 42Combined sources6
Beta strandi45 – 51Combined sources7
Beta strandi66 – 71Combined sources6
Beta strandi74 – 80Combined sources7
Helixi82 – 103Combined sources22
Helixi109 – 117Combined sources9
Turni118 – 121Combined sources4
Beta strandi133 – 135Combined sources3
Beta strandi139 – 147Combined sources9
Beta strandi150 – 156Combined sources7
Beta strandi162 – 171Combined sources10
Helixi174 – 184Combined sources11
Helixi191 – 205Combined sources15
Beta strandi214 – 220Combined sources7
Beta strandi222 – 224Combined sources3
Helixi231 – 238Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IRUX-ray2.75E/S1-241[»]
ProteinModelPortaliQ5E987
SMRiQ5E987
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5E987

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0176 Eukaryota
COG0638 LUCA
GeneTreeiENSGT00550000074958
HOGENOMiHOG000091085
HOVERGENiHBG003005
InParanoidiQ5E987
KOiK02729
OMAiFQVEYAR
OrthoDBiEOG091G0GX6
TreeFamiTF106211

Family and domain databases

CDDicd03753 proteasome_alpha_type_5, 1 hit
Gene3Di3.60.20.10, 1 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR023332 Proteasome_alpha-type
IPR033812 Proteasome_alpha_type_5
IPR000426 Proteasome_asu_N
IPR001353 Proteasome_sua/b
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.

Q5E987-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFLTRSEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGI QTSEGVCLAV
60 70 80 90 100
EKRITSPLME PSSIEKIVEI DAHIGCAMSG LIADAKTLID KARVETQNHW
110 120 130 140 150
FTYNETMTVE SVTQAVSNLA LQFGEEDADP GAMSRPFGVA LLFGGVDEKG
160 170 180 190 200
PQLFHMDPSG TFVQCDARAI GSASEGAQSS LQEVYHKSMT LKEAIKSSLI
210 220 230 240
ILKQVMEEKL NATNIELATV QPGQNFHMFT KEELEEVIKD I
Length:241
Mass (Da):26,411
Last modified:March 15, 2005 - v1
Checksum:i5610CDA00469120A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021033 mRNA Translation: AAX09050.1
BC102343 mRNA Translation: AAI02344.1
RefSeqiNP_001015566.1, NM_001015566.1
UniGeneiBt.47769

Genome annotation databases

EnsembliENSBTAT00000027507; ENSBTAP00000027507; ENSBTAG00000020641
GeneIDi510155
KEGGibta:510155

Similar proteinsi

Entry informationi

Entry nameiPSA5_BOVIN
AccessioniPrimary (citable) accession number: Q5E987
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: March 15, 2005
Last modified: May 23, 2018
This is version 112 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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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