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Q9PVY6

- PSA7A_XENLA

UniProt

Q9PVY6 - PSA7A_XENLA

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Protein

Proteasome subunit alpha type-7-A

Gene

psma7-a

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 3 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

  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

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-7-A (EC:3.4.25.1)
Alternative name(s):
Proteasome subunit alpha 4-A
Gene namesi
Name:psma7-a
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-974602. psma7.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
  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 – 248248Proteasome subunit alpha type-7-APRO_0000124147Add
BLAST

Post-translational modificationi

Phosphorylated in G2 phase.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ9PVY6.

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

BioGridi98959. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9PVY6.
SMRiQ9PVY6. Positions 2-232.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG003005.
KOiK02731.

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.

Q9PVY6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSYDRAITVF SPDGHLFQVE YAQEAVKKGS TAVGVRGKEI VVLGVEKKSV
60 70 80 90 100
AKLQDERTVR KICALDENVF MAFAGLTADA RIVINRARVE CQSHRLTVED
110 120 130 140 150
PVTVEYITRY IASLKQRYTQ SNGRRPFGIS ALIVGFDFDG TPRLYQTDPS
160 170 180 190 200
GTYHAWKANA IGRGAKSVRE FLEKHYTDEA IETDDLTIKL VIKALLEVVQ
210 220 230 240
SGGKNIELAV MRRDQPLKIL NPEEIERYVA EIEKEKEENE KKKQKKTT
Length:248
Mass (Da):28,036
Last modified:May 1, 2000 - v1
Checksum:iB62213FED11C3A60
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB004782 mRNA. Translation: BAA86962.1.
BC084072 mRNA. Translation: AAH84072.1.
RefSeqiNP_001081054.1. NM_001087585.1.
UniGeneiXl.921.

Genome annotation databases

GeneIDi394357.
KEGGixla:394357.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB004782 mRNA. Translation: BAA86962.1 .
BC084072 mRNA. Translation: AAH84072.1 .
RefSeqi NP_001081054.1. NM_001087585.1.
UniGenei Xl.921.

3D structure databases

ProteinModelPortali Q9PVY6.
SMRi Q9PVY6. Positions 2-232.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 98959. 1 interaction.

Proteomic databases

PRIDEi Q9PVY6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 394357.
KEGGi xla:394357.

Organism-specific databases

CTDi 394357.
Xenbasei XB-GENE-974602. psma7.

Phylogenomic databases

HOVERGENi HBG003005.
KOi K02731.

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. "Identification of the Xenopus 20S proteasome alpha 4 subunit which is modified in the meiotic cell cycle."
    Tokumoto M., Horiguchi R., Nagahama Y., Tokumoto T.
    Gene 239:301-308(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Ovary.
  2. NIH - Xenopus Gene Collection (XGC) project
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo.

Entry informationi

Entry nameiPSA7A_XENLA
AccessioniPrimary (citable) accession number: Q9PVY6
Secondary accession number(s): Q5XHI5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3