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Protein

Proteasome subunit alpha type-4

Gene

psmA4

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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.

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

ReactomeiREACT_274720. Orc1 removal from chromatin.
REACT_295029. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_297739. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_297926. Hedgehog 'on' state.
REACT_314379. ER-Phagosome pathway.
REACT_317678. APC/C:Cdc20 mediated degradation of Securin.
REACT_319046. Separation of Sister Chromatids.
REACT_324488. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_336966. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_344410. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_350432. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_351052. Autodegradation of Cdh1 by Cdh1:APC/C.

Protein family/group databases

MEROPSiT01.973.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-4 (EC:3.4.25.1)
Alternative name(s):
Proteasome component DD4
Gene namesi
Name:psmA4
Synonyms:prdD
ORF Names:DDB_G0280969
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
ProteomesiUP000002195 Componentsi: Chromosome 3, Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0280969. psmA4.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: dictyBase
  • nucleus Source: dictyBase
  • proteasome core complex Source: GO_Central
  • 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 – 250250Proteasome subunit alpha type-4PRO_0000124108Add
BLAST

Proteomic databases

PRIDEiP34119.

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 (By similarity).By similarity

Protein-protein interaction databases

STRINGi44689.DDB0214953.

Structurei

3D structure databases

ProteinModelPortaliP34119.
SMRiP34119. Positions 2-241.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
InParanoidiP34119.
KOiK02728.
OMAiLVSHLCD.
PhylomeDBiP34119.

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.

P34119-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARRYDQRTT IFSPEGRVYQ VEYAMTAIRH AGATVGILAK DGIVLAAEKK
60 70 80 90 100
TTAKLLDSST SISEKMFKID EHVVCAVAGI TSDANILINY ARLSSQRFFY
110 120 130 140 150
QYQEPMPVEQ LVSQICDTKQ GYTQYGGLRP FGVSFLYAGW DRHYGFQLYQ
160 170 180 190 200
SDPSGNFAGW KATSIGGENS QVAQSVLRSN YKPDISLKEA LQLALKVLTK
210 220 230 240 250
TMDRSNINSE KLEFSYFTKQ GDNVVYHIFT AAELDAFIKE TDLEQETEDN
Length:250
Mass (Da):28,101
Last modified:February 1, 1994 - v1
Checksum:i39387786A34999DC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L22212 mRNA. Translation: AAA33233.1.
AAFI02000040 Genomic DNA. Translation: EAL66781.1.
RefSeqiXP_640858.1. XM_635766.1.

Genome annotation databases

EnsemblProtistsiDDB0214953; DDB0214953; DDB_G0280969.
GeneIDi8622914.
KEGGiddi:DDB_G0280969.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L22212 mRNA. Translation: AAA33233.1.
AAFI02000040 Genomic DNA. Translation: EAL66781.1.
RefSeqiXP_640858.1. XM_635766.1.

3D structure databases

ProteinModelPortaliP34119.
SMRiP34119. Positions 2-241.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi44689.DDB0214953.

Protein family/group databases

MEROPSiT01.973.

Proteomic databases

PRIDEiP34119.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiDDB0214953; DDB0214953; DDB_G0280969.
GeneIDi8622914.
KEGGiddi:DDB_G0280969.

Organism-specific databases

dictyBaseiDDB_G0280969. psmA4.

Phylogenomic databases

eggNOGiCOG0638.
InParanoidiP34119.
KOiK02728.
OMAiLVSHLCD.
PhylomeDBiP34119.

Enzyme and pathway databases

ReactomeiREACT_274720. Orc1 removal from chromatin.
REACT_295029. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_297739. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_297926. Hedgehog 'on' state.
REACT_314379. ER-Phagosome pathway.
REACT_317678. APC/C:Cdc20 mediated degradation of Securin.
REACT_319046. Separation of Sister Chromatids.
REACT_324488. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_336966. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_344410. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_350432. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_351052. Autodegradation of Cdh1 by Cdh1:APC/C.

Miscellaneous databases

PROiP34119.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Proteasomes from Dictyostelium discoideum: characterization of structure and function."
    Schauer T.M., Nesper M., Kehl M., Lottspeich F., Mueller-Taubenberger A., Gerisch G., Baumeister W.
    J. Struct. Biol. 111:135-147(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: AX2.
  2. "The genome of the social amoeba Dictyostelium discoideum."
    Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
    , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
    Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: AX4.

Entry informationi

Entry nameiPSA4_DICDI
AccessioniPrimary (citable) accession number: P34119
Secondary accession number(s): Q54UB8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: July 22, 2015
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Dictyostelium discoideum
    Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
  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.