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O23712 (PSA1B_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 118. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proteasome subunit alpha type-1-B

EC=3.4.25.1
Alternative name(s):
20S proteasome alpha subunit F-2
Proteasome component 2B
Proteasome subunit alpha type-6
Gene names
Name:PAF2
Synonyms:PRC2B, PRS1
Ordered Locus Names:At1g47250
ORF Names:F8G22.3
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length277 AA.
Sequence statusComplete.
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. May play a role in thiol biosynthesis and arsenic tolerance in association with PAF1/ARS5. Ref.8

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.6 Ref.7 Ref.9

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Disruption phenotype

Do not show arsenic tolerance phenotype. Ref.8

Sequence similarities

Belongs to the peptidase T1A family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 277277Proteasome subunit alpha type-1-B
PRO_0000124073

Amino acid modifications

Modified residue11N-acetylmethionine Ref.9

Sequences

Sequence LengthMass (Da)Tools
O23712 [UniParc].

Last modified May 1, 1999. Version 2.
Checksum: C5FBCE302217C521

FASTA27730,410
        10         20         30         40         50         60 
MFRNQYDTDV TTWSPTGRLF QVEYAMEAVK QGSAAIGLRS RSHVVLACVN KAQSELSSHQ 

        70         80         90        100        110        120 
RKIFKVDDHI GVAIAGLTAD GRVLSRYMRS ESINHSFTYE SPLPVGRLVV HLADKAQVCT 

       130        140        150        160        170        180 
QRSWKRPYGV GLLVGGLDES GAHLYYNCPS GNYFEYQAFA IGSRSQAAKT YLERKFESFQ 

       190        200        210        220        230        240 
ESSKEDLIKD AIMAIRETLQ GETLKSSLCT VSVLGVDEPF HFLDQESIQK VIDTFEKVPE 

       250        260        270 
EEEDAGEGEA EPEAAPGAAG TGEQGGSGDQ DVAPMEI 

« Hide

References

« Hide 'large scale' references
[1]"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], GENE FAMILY, NOMENCLATURE.
Strain: cv. Columbia.
[2]"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.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"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].
Strain: cv. Columbia.
[5]"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] OF 11-277.
Strain: cv. Columbia.
[6]"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.
[7]"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.
[8]"ARS5 is a component of the 26S proteasome complex, and negatively regulates thiol biosynthesis and arsenic tolerance in Arabidopsis."
Sung D.-Y., Kim T.-H., Komives E.A., Mendoza-Cozatl D.G., Schroeder J.I.
Plant J. 59:802-812(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[9]"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, ACETYLATION AT MET-1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF043527 mRNA. Translation: AAC32063.1.
AC079677 Genomic DNA. Translation: AAG52642.1.
CP002684 Genomic DNA. Translation: AEE32143.1.
AY057649 mRNA. Translation: AAL15280.1.
AY141996 mRNA. Translation: AAM98260.1.
Y13182 mRNA. Translation: CAA73625.1.
PIRT51975.
RefSeqNP_175158.1. NM_103619.4.
UniGeneAt.48280.

3D structure databases

ProteinModelPortalO23712.
SMRO23712. Positions 4-240.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid26353. 2 interactions.
IntActO23712. 1 interaction.
STRING3702.AT1G47250.1-P.

Protein family/group databases

MEROPST01.976.

Proteomic databases

PaxDbO23712.
PRIDEO23712.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G47250.1; AT1G47250.1; AT1G47250.
GeneID841128.
KEGGath:AT1G47250.

Organism-specific databases

TAIRAT1G47250.

Phylogenomic databases

eggNOGCOG0638.
HOGENOMHOG000091080.
InParanoidO23712.
KOK02725.
OMADVAPMEI.
PhylomeDBO23712.

Enzyme and pathway databases

BioCycARA:AT1G47250-MONOMER.

Gene expression databases

GenevestigatorO23712.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
InterProIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMSSF56235. SSF56235. 1 hit.
PROSITEPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROO23712.

Entry information

Entry namePSA1B_ARATH
AccessionPrimary (citable) accession number: O23712
Entry history
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: May 1, 1999
Last modified: June 11, 2014
This is version 118 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