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Q3ZCK9

- PSA4_BOVIN

UniProt

Q3ZCK9 - PSA4_BOVIN

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Protein

Proteasome subunit alpha type-4

Gene

PSMA4

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

MEROPSiT01.973.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-4 (EC:3.4.25.1)
Gene namesi
Name:PSMA4
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 21

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity. CytoplasmP-body By similarity
Note: Colocalizes with TRIM5 in the cytoplasmic bodies.By similarity

GO - Cellular componenti

  1. cytoplasmic mRNA processing body Source: UniProtKB
  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
Chaini1 – 261261Proteasome subunit alpha type-4PRO_0000274032Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131PhosphoserineBy similarity
Modified residuei75 – 751PhosphoserineBy similarity
Modified residuei127 – 1271N6-acetyllysineBy similarity
Modified residuei176 – 1761N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiQ3ZCK9.

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.ENSBTAP00000019203.

Structurei

Secondary structure

1
261
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni3 – 53
Helixi19 – 2810
Beta strandi34 – 385
Beta strandi40 – 478
Beta strandi63 – 675
Beta strandi69 – 7810
Helixi80 – 10122
Helixi107 – 12014
Turni121 – 1233
Beta strandi124 – 1263
Beta strandi132 – 1409
Turni141 – 1433
Beta strandi144 – 1518
Turni152 – 1543
Beta strandi155 – 1584
Beta strandi160 – 1656
Turni166 – 1694
Helixi170 – 1789
Helixi186 – 19914
Beta strandi200 – 2023
Beta strandi212 – 2176
Beta strandi220 – 2223
Beta strandi224 – 2274
Helixi230 – 24112
Turni245 – 2473

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IRUX-ray2.75C/Q1-261[»]
ProteinModelPortaliQ3ZCK9.
SMRiQ3ZCK9. Positions 2-237.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ3ZCK9.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074827.
HOGENOMiHOG000091085.
HOVERGENiHBG003005.
InParanoidiQ3ZCK9.
KOiK02728.
OMAiKQEYKDD.
OrthoDBiEOG7F512J.
TreeFamiTF106209.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR016050. Proteasome_bsu_CS.
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.

Q3ZCK9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSRRYDSRTT IFSPEGRLYQ VEYAMEAIGH AGTCLGILAN DGVLLAAERR
60 70 80 90 100
NIHKLLDEVF FSEKIYKLNE DMACSVAGIT SDANVLTNEL RLIAQRYLLQ
110 120 130 140 150
YQEPIPCEQL VTALCDIKQA YTQFGGKRPF GVSLLYIGWD KHYGFQLYQS
160 170 180 190 200
DPSGNYGGWK ATCIGNNSAA AVSMLKQDYK EGEMTLKSAL ALAIKVLNKT
210 220 230 240 250
MDVSKLSAEK VEIATLTREN GKTVIRVLKQ KEVEQLIKKH EEEEAKAERE
260
KKEKEQKEKD K
Length:261
Mass (Da):29,484
Last modified:September 27, 2005 - v1
Checksum:i7867422B1B31F3B9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC102102 mRNA. Translation: AAI02103.1.
RefSeqiNP_001029553.1. NM_001034381.2.
UniGeneiBt.49419.

Genome annotation databases

EnsembliENSBTAT00000019203; ENSBTAP00000019203; ENSBTAG00000014440.
GeneIDi510423.
KEGGibta:510423.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC102102 mRNA. Translation: AAI02103.1 .
RefSeqi NP_001029553.1. NM_001034381.2.
UniGenei Bt.49419.

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 C/Q 1-261 [» ]
ProteinModelPortali Q3ZCK9.
SMRi Q3ZCK9. Positions 2-237.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9913.ENSBTAP00000019203.

Protein family/group databases

MEROPSi T01.973.

Proteomic databases

PRIDEi Q3ZCK9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSBTAT00000019203 ; ENSBTAP00000019203 ; ENSBTAG00000014440 .
GeneIDi 510423.
KEGGi bta:510423.

Organism-specific databases

CTDi 5685.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00550000074827.
HOGENOMi HOG000091085.
HOVERGENi HBG003005.
InParanoidi Q3ZCK9.
KOi K02728.
OMAi KQEYKDD.
OrthoDBi EOG7F512J.
TreeFami TF106209.

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 Q3ZCK9.
NextBioi 20869437.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR016050. Proteasome_bsu_CS.
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. 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 20S PROTEASOME.

Entry informationi

Entry nameiPSA4_BOVIN
AccessioniPrimary (citable) accession number: Q3ZCK9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: September 27, 2005
Last modified: October 29, 2014
This is version 81 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