Reviewed, UniProtKB/Swiss-Prot Q42134 (PSA5B_ARATH)

Names and origin

Protein names

Recommended name:
    Proteasome subunit alpha type-5-B
    EC=3.4.25.1
Alternative name(s):
    20S proteasome alpha subunit E-2
    Proteasome component Z

Gene names

Name:	PAE2
Synonyms:	PRCZ
Ordered Locus Names:	At3g14290
ORF Names:	MLN21.8

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	237 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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	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. Ref.5
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Sequence similarities	Belongs to the peptidase T1A family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus Proteasome
Molecular function	Hydrolase Protease Threonine protease
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytosolic ribosome Inferred from direct assay. Source: TAIR nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell proteasome core complex Inferred from electronic annotation. Source: InterPro
Molecular function	threonine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 237	237	Proteasome subunit alpha type-5-B		PRO_0000124125

Sequences

	Sequence		Length	Mass (Da)
	Q42134-1 [UniParc]. Last modified May 1, 1999. Version 2. Checksum: B178A3A0DDA12680	FASTA	237	25,977
	10 20 30 40 50 60 MFLTRTEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGV KTKEGVVLAV EKRITSPLLE 70 80 90 100 110 120 PSSVEKIMEI DDHIGCAMSG LIADARTLVE HARVETQNHR FSYGEPMTVE STTQALCDLA 130 140 150 160 170 180 LRFGEGEEES MSRPFGVSLL IAGHDENGPS LYYTDPSGTF WQCNAKAIGS GSEGADSSLQ 190 200 210 220 230 EQFNKDITLQ EAETIAVSIL KQVMEEKVTP NNVDIAKVAP AYHLYTPQEV EAVISRL

References

	« Hide 'large scale' referencesShow '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: 9611183] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], NOMENCLATURE. Strain: cv. Columbia.
[2]	"Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones." Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S. DNA Res. 7:131-135(2000) [PubMed: 10819329] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"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. , 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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Further progress towards a catalogue of all Arabidopsis genes: analysis of a set of 5000 non-redundant ESTs." Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C., Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R., Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J. , Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D., Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P., Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H. Plant J. 9:101-124(1996) [PubMed: 8580968] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 181-237. Strain: cv. Columbia. Tissue: Seedling.
[5]	"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: 14623884] [Abstract] Cited for: SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF043525 mRNA. Translation: AAC32061.1. AB022220 Genomic DNA. Translation: BAB01035.1. AF370245 mRNA. Translation: AAK44060.1. AY062970 mRNA. Translation: AAL33816.1. Z26556 mRNA. Translation: CAA81327.1.
IPI	IPI00548261.
PIR	T51973.
RefSeq	NP_188046.1.
UniGene	At.21306
3D structure databases
HSSP	HSSP built from PDB template 1RYP based on UniProtKB P32379.
ModBase	Search...
Protein-protein interaction databases
STRING	Q42134.
Protein family/group databases
MEROPS	T01.975.
Proteomic databases
PRIDE	Q42134.
Genome annotation databases
GeneID	820649.
GenomeReviews	Gene locus AT3G14290 in contig BA000014_GR.
KEGG	ath:AT3G14290.
NMPDR	fig|3702.1.peg.13562.
Organism-specific databases
TAIR	At3g14290.
Phylogenomic databases
OMA	LIADSRT.
Enzyme and pathway databases
BRENDA	3.4.25.1. 302.
Gene expression databases
ArrayExpress	Q42134.
Genevestigator	Q42134.
GermOnline	AT3G14290. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR000426. Proteasome_asu_CS. IPR001353. Proteasome_sua/b. [Graphical view]
Pfam	PF00227. Proteasome. 1 hit. PF10584. Proteasome_A_N. 1 hit. [Graphical view]
PROSITE	PS00388. PROTEASOME_A. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PSA5B_ARATH

Accession

Primary (citable) accession number: Q42134

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 8, 2000
Last sequence update:	May 1, 1999
Last modified:	November 3, 2009
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)