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A2YVR7

- PSA2_ORYSI

UniProt

A2YVR7 - PSA2_ORYSI

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Protein
Proteasome subunit alpha type-2
Gene
PAB1, OsI_028410
Organism
Oryza sativa subsp. indica (Rice)
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.

GO - Molecular functioni

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

GO - Biological processi

  1. defense response to bacterium Source: EnsemblPlants/Gramene
  2. response to zinc ion Source: EnsemblPlants/Gramene
  3. 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-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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza

Organism-specific databases

GrameneiA2YVR7.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytosolic ribosome Source: EnsemblPlants/Gramene
  2. nucleus Source: UniProtKB-SubCell
  3. 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 – 235235Proteasome subunit alpha type-2
PRO_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.

Protein-protein interaction databases

STRINGi39947.LOC_Os03g26970.1.

Structurei

3D structure databases

ProteinModelPortaliA2YVR7.
SMRiA2YVR7. Positions 6-234.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000091085.

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

MGDSQYSFSL TTFSPSGKLV QIEHALTAVG SGQTSLGIKA ANGVVIATEK    50
KLPSILVDET SVQKIQSLTP NIGVVYSGMG PDFRVLVRKS RKQAQQYYRL 100
YKETIPVTQL VRETAAVMQE FTQSGGVRPF GVSLLIAGYD DNGPQLYQVD 150
PSGSYFSWKA SAMGKNVSNA KTFLEKRYTE DMELDDAIHT AILTLKEGYE 200
GQISANNIEI GIIRSDREFK VLSPAEIKDF LEEVE 235
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.

Sequence conflict

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF022735 mRNA. Translation: AAB82138.1. Frameshift.
CM000133 Genomic DNA. No translation available.
PIRiT02089.
UniGeneiOs.7900.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF022735 mRNA. Translation: AAB82138.1 . Frameshift.
CM000133 Genomic DNA. No translation available.
PIRi T02089.
UniGenei Os.7900.

3D structure databases

ProteinModelPortali A2YVR7.
SMRi A2YVR7. Positions 6-234.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 39947.LOC_Os03g26970.1.

Proteomic databases

PRIDEi A2YVR7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

Gramenei A2YVR7.

Phylogenomic databases

eggNOGi COG0638.
HOGENOMi HOG000091085.

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. "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 11, 2014
This is version 43 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant 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

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