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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

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. Mediates the lipopolysaccharide-induced signal macrophage proteasome. Might be involved in the anti-inflammatory response of macrophages during the interaction with C.albicans heat-inactivated cells (By similarity).By similarity

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.PROSITE-ProRule annotation

GO - Molecular functioni

  1. lipopolysaccharide binding Source: Ensembl
  2. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. immune system process Source: UniProtKB-KW
  2. negative regulation of inflammatory response to antigenic stimulus Source: Ensembl
  3. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Keywords - Biological processi

Immunity

Enzyme and pathway databases

ReactomeiREACT_274004. degradation of DVL.
REACT_276477. ER-Phagosome pathway.
REACT_280521. Activation of NF-kappaB in B cells.
REACT_282220. Asymmetric localization of PCP proteins.
REACT_284817. Hh ligand biogenesis disease.
REACT_290505. SCF(Skp2)-mediated degradation of p27/p21.
REACT_291730. Separation of Sister Chromatids.
REACT_293325. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_295102. CDT1 association with the CDC6:ORC:origin complex.
REACT_297209. Degradation of beta-catenin by the destruction complex.
REACT_302851. CDK-mediated phosphorylation and removal of Cdc6.
REACT_304977. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_306095. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_307496. Hedgehog ligand biogenesis.
REACT_308391. Ubiquitin-dependent degradation of Cyclin D1.
REACT_311810. Hedgehog 'on' state.
REACT_314321. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_321728. Regulation of ornithine decarboxylase (ODC).
REACT_326365. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_327729. Degradation of GLI2 by the proteasome.
REACT_328795. Orc1 removal from chromatin.
REACT_328929. SCF-beta-TrCP mediated degradation of Emi1.
REACT_329551. degradation of AXIN.
REACT_329646. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_330101. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_333090. GLI3 is processed to GLI3R by the proteasome.
REACT_335347. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_337384. Degradation of GLI1 by the proteasome.
REACT_338497. APC/C:Cdc20 mediated degradation of Securin.
REACT_350460. Regulation of activated PAK-2p34 by proteasome mediated degradation.

Protein family/group databases

MEROPSiT01.976.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-1 (EC:3.4.25.1)
Gene namesi
Name:PSMA1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Chromosome 15

Subcellular locationi

  1. Cytoplasm By similarity
  2. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
  3. proteasome core complex Source: UniProtKB
  4. proteasome core complex, alpha-subunit complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 263263Proteasome subunit alpha type-1PRO_0000274031Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Glycosylationi110 – 1101O-linked (GlcNAc)By similarity
Cross-linki115 – 115Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki208 – 208Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiQ3T0X5.
PRIDEiQ3T0X5.

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.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000008621.

Structurei

Secondary structure

1
263
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni5 – 73Combined sources
Helixi20 – 3112Combined sources
Beta strandi35 – 395Combined sources
Beta strandi41 – 499Combined sources
Beta strandi63 – 675Combined sources
Beta strandi70 – 767Combined sources
Helixi78 – 9922Combined sources
Helixi105 – 12117Combined sources
Beta strandi130 – 1389Combined sources
Beta strandi141 – 1477Combined sources
Beta strandi149 – 1513Combined sources
Beta strandi153 – 16210Combined sources
Helixi165 – 17915Combined sources
Helixi184 – 19613Combined sources
Turni207 – 2093Combined sources
Beta strandi210 – 2167Combined sources
Beta strandi219 – 2246Combined sources
Helixi227 – 2293Combined sources
Helixi230 – 2334Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IRUX-ray2.75F/T1-263[»]
SMRiQ3T0X5. Positions 4-241.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ3T0X5.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074855.
HOGENOMiHOG000091080.
HOVERGENiHBG105373.
InParanoidiQ3T0X5.
KOiK02725.
OMAiFMKQQCL.
OrthoDBiEOG7WQ7T1.
TreeFamiTF106206.

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.

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.

Cross-referencesi

Sequence databases

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IRUX-ray2.75F/T1-263[»]
SMRiQ3T0X5. Positions 4-241.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000008621.

Protein family/group databases

MEROPSiT01.976.

Proteomic databases

PaxDbiQ3T0X5.
PRIDEiQ3T0X5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5682.

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074855.
HOGENOMiHOG000091080.
HOVERGENiHBG105373.
InParanoidiQ3T0X5.
KOiK02725.
OMAiFMKQQCL.
OrthoDBiEOG7WQ7T1.
TreeFamiTF106206.

Enzyme and pathway databases

ReactomeiREACT_274004. degradation of DVL.
REACT_276477. ER-Phagosome pathway.
REACT_280521. Activation of NF-kappaB in B cells.
REACT_282220. Asymmetric localization of PCP proteins.
REACT_284817. Hh ligand biogenesis disease.
REACT_290505. SCF(Skp2)-mediated degradation of p27/p21.
REACT_291730. Separation of Sister Chromatids.
REACT_293325. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_295102. CDT1 association with the CDC6:ORC:origin complex.
REACT_297209. Degradation of beta-catenin by the destruction complex.
REACT_302851. CDK-mediated phosphorylation and removal of Cdc6.
REACT_304977. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_306095. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_307496. Hedgehog ligand biogenesis.
REACT_308391. Ubiquitin-dependent degradation of Cyclin D1.
REACT_311810. Hedgehog 'on' state.
REACT_314321. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_321728. Regulation of ornithine decarboxylase (ODC).
REACT_326365. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_327729. Degradation of GLI2 by the proteasome.
REACT_328795. Orc1 removal from chromatin.
REACT_328929. SCF-beta-TrCP mediated degradation of Emi1.
REACT_329551. degradation of AXIN.
REACT_329646. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_330101. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_333090. GLI3 is processed to GLI3R by the proteasome.
REACT_335347. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_337384. Degradation of GLI1 by the proteasome.
REACT_338497. APC/C:Cdc20 mediated degradation of Securin.
REACT_350460. Regulation of activated PAK-2p34 by proteasome mediated degradation.

Miscellaneous databases

EvolutionaryTraceiQ3T0X5.
NextBioi20871856.

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...

Publicationsi

« Hide 'large scale' publications
  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Ileum.
  2. "The structure of the mammalian 20S proteasome at 2.75 A resolution."
    Unno M., Mizushima T., Morimoto Y., Tomisugi Y., Tanaka K., Yasuoka N., Tsukihara T.
    Structure 10:609-618(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF COMPLEX WITH THE 20S PROTEASOME.

Entry informationi

Entry nameiPSA1_BOVIN
AccessioniPrimary (citable) accession number: Q3T0X5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: October 11, 2005
Last modified: April 1, 2015
This is version 82 of the entry and version 1 of the sequence. [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

External Data

Dasty 3

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 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.