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Protein

Proteasome subunit alpha type-1

Gene

PSMA1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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
Biological processImmunity

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-446652. Interleukin-1 signaling.
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-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-8941858. Regulation of RUNX3 expression and activity.
R-BTA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Protein family/group databases

MEROPSiT01.976.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-1 (EC:3.4.25.1By similarity)
Gene namesi
Name:PSMA1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 15

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002740311 – 263Proteasome subunit alpha type-1Add BLAST263

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei110Phosphoserine; alternateBy similarity1
Glycosylationi110O-linked (GlcNAc) serine; alternateBy similarity1
Cross-linki115Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei177PhosphoserineBy similarity1
Cross-linki208Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ3T0X5.
PeptideAtlasiQ3T0X5.
PRIDEiQ3T0X5.

Expressioni

Gene expression databases

BgeeiENSBTAG00000006564.

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). Interacts with NOTCH3 (By similarity).By similarity1 Publication

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000008621.

Structurei

Secondary structure

1263
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni5 – 7Combined sources3
Helixi20 – 31Combined sources12
Beta strandi35 – 39Combined sources5
Beta strandi41 – 49Combined sources9
Beta strandi63 – 67Combined sources5
Beta strandi70 – 76Combined sources7
Helixi78 – 99Combined sources22
Helixi105 – 121Combined sources17
Beta strandi130 – 138Combined sources9
Beta strandi141 – 147Combined sources7
Beta strandi149 – 151Combined sources3
Beta strandi153 – 162Combined sources10
Helixi165 – 179Combined sources15
Helixi184 – 196Combined sources13
Turni207 – 209Combined sources3
Beta strandi210 – 216Combined sources7
Beta strandi219 – 224Combined sources6
Helixi227 – 229Combined sources3
Helixi230 – 233Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IRUX-ray2.75F/T1-263[»]
ProteinModelPortaliQ3T0X5.
SMRiQ3T0X5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ3T0X5.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0863. Eukaryota.
COG0638. LUCA.
GeneTreeiENSGT00550000074855.
HOGENOMiHOG000091080.
HOVERGENiHBG105373.
InParanoidiQ3T0X5.
KOiK02725.
OMAiFMKQQCL.
OrthoDBiEOG091G0DNK.
TreeFamiTF106206.

Family and domain databases

CDDicd03749. proteasome_alpha_type_1. 1 hit.
Gene3Di3.60.20.10. 1 hit.
InterProiView protein in InterPro
IPR029055. Ntn_hydrolases_N.
IPR023332. Proteasome_alpha-type.
IPR035144. Proteasome_alpha1.
IPR000426. Proteasome_asu_N.
IPR001353. Proteasome_sua/b.
PANTHERiPTHR11599:SF93. PTHR11599:SF93. 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.

Q3T0X5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFRNQYDNDV TVWSPQGRIH QIEYAMEAVK QGSATVGLKS KTHAVLVALK
60 70 80 90 100
RAQSELAAHQ KKILHVDNHI GISIAGLTAD ARLLCNFMRQ ECLDSRFVFD
110 120 130 140 150
RPLPVSRLVS LIGSKTQIPT QRYGRRPYGV GLLIAGYDDM GPHIFQTCPS
160 170 180 190 200
ANYFDCRAMS IGARSQSART YLERHMSEFM ECNLNELVKH GLRALRETLP
210 220 230 240 250
AEQDLTTKNV SIGIVGKDLE FTIYDDDDVS PFLEGLEERP QRKAQPTQPA
260
DEPAEKADEP MEH
Length:263
Mass (Da):29,586
Last modified:October 11, 2005 - v1
Checksum:i24142C5BCEFE8DED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC102216 mRNA. Translation: AAI02217.1.
RefSeqiNP_001030387.1. NM_001035310.2.
UniGeneiBt.23202.

Genome annotation databases

EnsembliENSBTAT00000008621; ENSBTAP00000008621; ENSBTAG00000006564.
GeneIDi515503.
KEGGibta:515503.

Similar proteinsi

Entry informationi

Entry nameiPSA1_BOVIN
AccessioniPrimary (citable) accession number: Q3T0X5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: October 11, 2005
Last modified: August 30, 2017
This is version 101 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