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Q9XI05 (PSB3A_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proteasome subunit beta type-3-A

EC=3.4.25.1
Alternative name(s):
20S proteasome beta subunit C-1
Proteasome component T
Gene names
Name:PBC1
Synonyms:PRCT
Ordered Locus Names:At1g21720
ORF Names:F8K7.15
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length204 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

Cleavage of peptide bonds with very broad specificity.

Subunit structure

Component of the 20S core complex of the 26S proteasome. The 26S proteasome is composed of a core protease (CP), known as the 20S proteasome, capped at one or both ends by the 19S regulatory particle (RP/PA700). 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. Ref.8 Ref.9 Ref.10

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Sequence similarities

Belongs to the peptidase T1B family.

Sequence caution

The sequence AAC32068.1 differs from that shown. Reason: Frameshift at position 41.

The sequence CAA73616.1 differs from that shown. Reason: Frameshift at position 41.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9XI05-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9XI05-2)

The sequence of this isoform differs from the canonical sequence as follows:
     2-2: S → Q
Note: May be due to intron retention. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Probable
Chain2 – 204203Proteasome subunit beta type-3-A
PRO_0000148065

Natural variations

Alternative sequence21S → Q in isoform 2.
VSP_016143

Experimental info

Sequence conflict81G → V in AAM62756. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 9, 2010. Version 2.
Checksum: B52E22CDB3EDA467

FASTA20422,798
        10         20         30         40         50         60 
MSIFEYNGSA VVAMVGKNCF AIASDRRLGV QLQTIATDFQ RISKIHDRVF IGLSGLATDV 

        70         80         90        100        110        120 
QTLYQRLVFR HKLYQLREER DMKPETFASL VSAILYEKRF GPYLCQPVIA GLGDDDKPFI 

       130        140        150        160        170        180 
CTMDSIGAKE LAKDFVVSGT ASESLYGACE AMYKPDMEAE ELFETISQAL LSSVDRDCLS 

       190        200 
GWGGHVYIVT PTEIKERILK GRMD 

« Hide

Isoform 2 [UniParc].

Checksum: E1CD9513D8D2F3B9
Show »

FASTA20422,839

References

« Hide 'large scale' references
[1]"The 20S proteasome gene family in Arabidopsis thaliana."
Parmentier Y., Bouchez D., Fleck J., Genschik P.
FEBS Lett. 416:281-285(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: cv. Columbia.
[2]"Molecular organization of the 20S proteasome gene family from Arabidopsis thaliana."
Fu H., Doelling J.H., Arendt C.S., Hochstrasser M., Vierstra R.D.
Genetics 149:677-692(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), GENE FAMILY, NOMENCLATURE.
Strain: cv. Columbia.
[3]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[5]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: cv. Columbia.
[6]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: cv. Columbia.
[7]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[8]"Structure and functional analyses of the 26S proteasome subunits from plants."
Fu H., Girod P.-A., Doelling J.H., van Nocker S., Hochstrasser M., Finley D., Vierstra R.D.
Mol. Biol. Rep. 26:137-146(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[9]"Purification of the Arabidopsis 26 S proteasome: biochemical and molecular analyses revealed the presence of multiple isoforms."
Yang P., Fu H., Walker J., Papa C.M., Smalle J., Ju Y.-M., Vierstra R.D.
J. Biol. Chem. 279:6401-6413(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"Affinity purification of the Arabidopsis 26 S proteasome reveals a diverse array of plant proteolytic complexes."
Book A.J., Gladman N.P., Lee S.S., Scalf M., Smith L.M., Vierstra R.D.
J. Biol. Chem. 285:25554-25569(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S PROTEASOME COMPLEX, SUBUNIT, CLEAVAGE OF INITIATOR METHIONINE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y13173 mRNA. Translation: CAA73616.1. Frameshift.
AF043532 mRNA. Translation: AAC32068.1. Frameshift.
AC007727 Genomic DNA. Translation: AAD41426.1.
CP002684 Genomic DNA. Translation: AEE30146.1.
AY065070 mRNA. Translation: AAL38246.1.
AY114628 mRNA. Translation: AAM47947.1.
AF344327 mRNA. Translation: AAK06878.1.
AK226397 mRNA. Translation: BAE98543.1.
AY085532 mRNA. Translation: AAM62756.1.
PIRF86350.
RefSeqNP_564149.1. NM_102021.2. [Q9XI05-1]
UniGeneAt.11467.

3D structure databases

ProteinModelPortalQ9XI05.
SMRQ9XI05. Positions 2-204.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid24015. 1 interaction.

Proteomic databases

PaxDbQ9XI05.
PRIDEQ9XI05.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G21720.1; AT1G21720.1; AT1G21720. [Q9XI05-1]
GeneID838776.
KEGGath:AT1G21720.

Organism-specific databases

TAIRAT1G21720.

Phylogenomic databases

eggNOGCOG0638.
HOGENOMHOG000090523.
InParanoidQ9XI05.
KOK02735.
OMAMDLIGCP.
PhylomeDBQ9XI05.

Enzyme and pathway databases

BioCycARA:AT1G21720-MONOMER.

Gene expression databases

GenevestigatorQ9XI05.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
InterProIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
[Graphical view]
SUPFAMSSF56235. SSF56235. 1 hit.
PROSITEPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePSB3A_ARATH
AccessionPrimary (citable) accession number: Q9XI05
Secondary accession number(s): O23707 expand/collapse secondary AC list , Q0WWF5, Q8LEA7, Q8VZC4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: February 9, 2010
Last modified: June 11, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names