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Protein

Proteasome subunit alpha type-2

Gene

PAB1

Organism
Oryza sativa subsp. indica (Rice)
Status
Reviewed-Annotation score: 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-2 (EC:3.4.25.1)
Alternative name(s):
20S proteasome alpha subunit B
20S proteasome subunit alpha-2
Gene namesi
Name:PAB1
ORF Names:OsI_028410
OrganismiOryza sativa subsp. indica (Rice)
Taxonomic identifieri39946 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladeOryzoideaeOryzeaeOryzinaeOryza
ProteomesiUP000007015 Componenti: Chromosome 8

Organism-specific databases

GrameneiA2YVR7.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 235235Proteasome subunit alpha type-2PRO_0000301662Add
BLAST

Proteomic databases

PRIDEiA2YVR7.

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

STRINGi39946.BGIOSGA026895-PA.

Structurei

3D structure databases

ProteinModelPortaliA2YVR7.
SMRiA2YVR7. Positions 6-234.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000091085.
OMAiNKVEMIT.

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.

A2YVR7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGDSQYSFSL TTFSPSGKLV QIEHALTAVG SGQTSLGIKA ANGVVIATEK
60 70 80 90 100
KLPSILVDET SVQKIQSLTP NIGVVYSGMG PDFRVLVRKS RKQAQQYYRL
110 120 130 140 150
YKETIPVTQL VRETAAVMQE FTQSGGVRPF GVSLLIAGYD DNGPQLYQVD
160 170 180 190 200
PSGSYFSWKA SAMGKNVSNA KTFLEKRYTE DMELDDAIHT AILTLKEGYE
210 220 230
GQISANNIEI GIIRSDREFK VLSPAEIKDF LEEVE
Length:235
Mass (Da):25,844
Last modified:September 11, 2007 - v2
Checksum:iD98998C0BC6CD676
GO

Sequence cautioni

The sequence AAB82138.1 differs from that shown. Reason: Frameshift at position 229. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231E → N in AAB82138 (Ref. 1) Curated
Sequence conflicti45 – 462VI → FV in AAB82138 (Ref. 1) Curated
Sequence conflicti72 – 721I → V in AAB82138 (Ref. 1) Curated
Sequence conflicti91 – 911R → P in AAB82138 (Ref. 1) Curated
Sequence conflicti97 – 982YY → CC in AAB82138 (Ref. 1) Curated
Sequence conflicti105 – 1051I → M in AAB82138 (Ref. 1) Curated
Sequence conflicti178 – 1781Y → H in AAB82138 (Ref. 1) Curated
Sequence conflicti191 – 1911A → G in AAB82138 (Ref. 1) Curated
Sequence conflicti194 – 1941T → I in AAB82138 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF022735 mRNA. Translation: AAB82138.1. Frameshift.
CM000133 Genomic DNA. No translation available.
PIRiT02089.
UniGeneiOs.7900.

Genome annotation databases

EnsemblPlantsiBGIOSGA026895-TA; BGIOSGA026895-PA; BGIOSGA026895.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF022735 mRNA. Translation: AAB82138.1. Frameshift.
CM000133 Genomic DNA. No translation available.
PIRiT02089.
UniGeneiOs.7900.

3D structure databases

ProteinModelPortaliA2YVR7.
SMRiA2YVR7. Positions 6-234.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi39946.BGIOSGA026895-PA.

Proteomic databases

PRIDEiA2YVR7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiBGIOSGA026895-TA; BGIOSGA026895-PA; BGIOSGA026895.

Organism-specific databases

GrameneiA2YVR7.

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000091085.
OMAiNKVEMIT.

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. "Isolation and characterization of proteasome from rice."
    Lee M.C., Kim C.S., Eun M.Y.
    Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Milyang 23.
    Tissue: Seed.
  2. "The genomes of Oryza sativa: a history of duplications."
    Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.
    , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.
    PLoS Biol. 3:266-281(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. 93-11.

Entry informationi

Entry nameiPSA2_ORYSI
AccessioniPrimary (citable) accession number: A2YVR7
Secondary accession number(s): O22539, Q6AVF6, Q9LSU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: June 24, 2015
This is version 48 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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

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.