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Q58DU5

- PSA3_BOVIN

UniProt

Q58DU5 - PSA3_BOVIN

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Protein

Proteasome subunit alpha type-3

Gene

PSMA3

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 3 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 By similarity.By similarity

Catalytic activityi

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

GO - Molecular functioni

  1. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

ReactomeiREACT_203965. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_205339. APC/C:Cdc20 mediated degradation of Securin.
REACT_205897. Activation of NF-kappaB in B cells.
REACT_206368. CDT1 association with the CDC6:ORC:origin complex.
REACT_207857. Asymmetric localization of PCP proteins.
REACT_208116. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_208851. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_208889. degradation of AXIN.
REACT_211738. ER-Phagosome pathway.
REACT_212887. Separation of Sister Chromatids.
REACT_213030. Orc1 removal from chromatin.
REACT_215163. degradation of DVL.
REACT_217860. SCF-beta-TrCP mediated degradation of Emi1.
REACT_218058. Ubiquitin-dependent degradation of Cyclin D1.
REACT_222557. CDK-mediated phosphorylation and removal of Cdc6.
REACT_222622. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_223494. SCF(Skp2)-mediated degradation of p27/p21.
REACT_224434. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_225648. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_226120. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_227515. AUF1 (hnRNP D0) destabilizes mRNA.

Protein family/group databases

MEROPSiT01.977.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-3 (EC:3.4.25.1)
Gene namesi
Name:PSMA3
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 10

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. extracellular vesicular exosome Source: Ensembl
  3. nucleus Source: UniProtKB-KW
  4. proteasome core complex Source: UniProtKB
  5. 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
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 255254Proteasome subunit alpha type-3PRO_0000240275Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei57 – 571N6-acetyllysineBy similarity
Modified residuei206 – 2061N6-acetyllysineBy similarity
Modified residuei230 – 2301N6-acetyllysineBy similarity
Modified residuei243 – 2431PhosphoserineBy similarity
Modified residuei250 – 2501PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiQ58DU5.

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. Interacts with AURKB By similarity.By similarity

Protein-protein interaction databases

IntActiQ58DU5. 1 interaction.
STRINGi9913.ENSBTAP00000003636.

Structurei

Secondary structure

1
255
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi22 – 3211
Beta strandi37 – 415
Beta strandi43 – 5311
Turni61 – 644
Beta strandi67 – 715
Beta strandi74 – 807
Helixi82 – 10322
Helixi109 – 12214
Beta strandi125 – 1295
Beta strandi133 – 14210
Turni143 – 1453
Beta strandi146 – 1527
Beta strandi158 – 16710
Helixi170 – 1778
Helixi182 – 1843
Helixi187 – 20115
Beta strandi204 – 2074
Beta strandi210 – 2167
Turni219 – 2235
Helixi230 – 24415

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IRUX-ray2.75G/U2-255[»]
ProteinModelPortaliQ58DU5.
SMRiQ58DU5. Positions 2-246.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ58DU5.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074912.
HOGENOMiHOG000091086.
HOVERGENiHBG105566.
InParanoidiQ58DU5.
KOiK02727.
OMAiVPDGRHF.
OrthoDBiEOG73JKW6.
TreeFamiTF106208.

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.

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

Q58DU5-1 [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 ELELSWVGEI TNGRHEIVPK DVREEAEKYA KESLKEEDES

DDDNM
Length:255
Mass (Da):28,405
Last modified:January 23, 2007 - v3
Checksum:iF078CC44D597EFA7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BT021502 mRNA. Translation: AAX46349.1.
BC109554 mRNA. Translation: AAI09555.1.
RefSeqiNP_001029407.1. NM_001034235.1.
UniGeneiBt.38213.

Genome annotation databases

EnsembliENSBTAT00000003636; ENSBTAP00000003636; ENSBTAG00000002808.
GeneIDi505176.
KEGGibta:505176.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BT021502 mRNA. Translation: AAX46349.1 .
BC109554 mRNA. Translation: AAI09555.1 .
RefSeqi NP_001029407.1. NM_001034235.1.
UniGenei Bt.38213.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IRU X-ray 2.75 G/U 2-255 [» ]
ProteinModelPortali Q58DU5.
SMRi Q58DU5. Positions 2-246.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q58DU5. 1 interaction.
STRINGi 9913.ENSBTAP00000003636.

Protein family/group databases

MEROPSi T01.977.

Proteomic databases

PRIDEi Q58DU5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000003636 ; ENSBTAP00000003636 ; ENSBTAG00000002808 .
GeneIDi 505176.
KEGGi bta:505176.

Organism-specific databases

CTDi 5684.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00550000074912.
HOGENOMi HOG000091086.
HOVERGENi HBG105566.
InParanoidi Q58DU5.
KOi K02727.
OMAi VPDGRHF.
OrthoDBi EOG73JKW6.
TreeFami TF106208.

Enzyme and pathway databases

Reactomei REACT_203965. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_205339. APC/C:Cdc20 mediated degradation of Securin.
REACT_205897. Activation of NF-kappaB in B cells.
REACT_206368. CDT1 association with the CDC6:ORC:origin complex.
REACT_207857. Asymmetric localization of PCP proteins.
REACT_208116. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_208851. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_208889. degradation of AXIN.
REACT_211738. ER-Phagosome pathway.
REACT_212887. Separation of Sister Chromatids.
REACT_213030. Orc1 removal from chromatin.
REACT_215163. degradation of DVL.
REACT_217860. SCF-beta-TrCP mediated degradation of Emi1.
REACT_218058. Ubiquitin-dependent degradation of Cyclin D1.
REACT_222557. CDK-mediated phosphorylation and removal of Cdc6.
REACT_222622. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_223494. SCF(Skp2)-mediated degradation of p27/p21.
REACT_224434. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_225648. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_226120. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_227515. AUF1 (hnRNP D0) destabilizes mRNA.

Miscellaneous databases

EvolutionaryTracei Q58DU5.
NextBioi 20867018.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view ]
SMARTi SM00948. Proteasome_A_N. 1 hit.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Liver.
  3. "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 nameiPSA3_BOVIN
AccessioniPrimary (citable) accession number: Q58DU5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 78 of the entry and version 3 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