Proteasome subunit alpha type-3 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P23638 (PSA3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 139. History...

Clusters with 100%, 90%, 50% identity |

Documents (5) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Proteasome subunit alpha type-3
EC=3.4.25.1

Alternative name(s):
Macropain subunit Y13
Multicatalytic endopeptidase complex subunit Y13
Proteasome component Y13
Proteinase YSCE subunit 13

Gene names

Name:	PRE9
Synonyms:	PRS5
Ordered Locus Names:	YGR135W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	258 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that 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. It 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.
Subcellular location	Cytoplasm. Nucleus.
Miscellaneous	Present with 17100 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the peptidase T1A family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus Proteasome
Molecular function	Hydrolase Protease Threonine protease
PTM	Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay PubMed 11545745 PubMed 19029916. Source: SGD proteasomal ubiquitin-independent protein catabolic process Inferred from direct assay PubMed 19162040. Source: SGD proteasome core complex assembly Inferred from mutant phenotype PubMed 14739934. Source: SGD
Cellular_component	nuclear outer membrane-endoplasmic reticulum membrane network Inferred by curator Ref.6. Source: SGD nucleus Inferred by curator Ref.6. Source: SGD proteasome core complex, alpha-subunit complex Inferred from direct assay Ref.6. Source: SGD proteasome storage granule Inferred from direct assay PubMed 18504300. Source: SGD
Molecular_function	threonine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PRE8	P23639	4	EBI-13967,EBI-13959

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 258

258

Proteasome subunit alpha type-3

PRO_0000124116

Amino acid modifications

Cross-link

199

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.5

Secondary structure

258

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P23638 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: B43BB05233A01A9E
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FASTA

258

28,714

        10         20         30         40         50         60 
MGSRRYDSRT TIFSPEGRLY QVEYALESIS HAGTAIGIMA SDGIVLAAER KVTSTLLEQD 

        70         80         90        100        110        120 
TSTEKLYKLN DKIAVAVAGL TADAEILINT ARIHAQNYLK TYNEDIPVEI LVRRLSDIKQ 

       130        140        150        160        170        180 
GYTQHGGLRP FGVSFIYAGY DDRYGYQLYT SNPSGNYTGW KAISVGANTS AAQTLLQMDY 

       190        200        210        220        230        240 
KDDMKVDDAI ELALKTLSKT TDSSALTYDR LEFATIRKGA NDGEVYQKIF KPQEIKDILV 

       250 
KTGITKKDED EEADEDMK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and functional analysis of three subunits of yeast proteasome." Emori Y., Tsukahara T., Kawasaki H., Ishiura S., Sugita H., Suzuki K. Mol. Cell. Biol. 11:344-353(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 73-92; 120-139 AND 200-236. Strain: ATCC 26786 / X2180-1A.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. Kleine K. Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]	"A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery." Hitchcock A.L., Auld K., Gygi S.P., Silver P.A. Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-199, MASS SPECTROMETRY.
[6]	"Structure of 20S proteasome from yeast at 2.4-A resolution." Groll M., Ditzel L., Loewe J., Stock D., Bochtler M., Bartunik H.D., Huber R. Nature 386:463-471(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-245 OF COMPLEX WITH THE 20S PROTEASOME.
[7]	"Structural basis for the activation of 20S proteasomes by 11S regulators." Whitby F.G., Masters E.I., Kramer L., Knowlton J.R., Yao Y., Wang C.C., Hill C.P. Nature 408:115-120(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 1-245 OF COMPLEX WITH THE 20S PROTEASOME AND A 11S REGULATORY COMPLEX.
[8]	"A gated channel into the proteasome core particle." Groll M., Bajorek M., Koehler A., Moroder L., Rubin D.M., Huber R., Glickman M.H., Finley D. Nat. Struct. Biol. 7:1062-1067(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-245 OF COMPLEX WITH THE 20S PROTEASOME.
[9]	"TMC-95-based inhibitor design provides evidence for the catalytic versatility of the proteasome." Groll M., Goetz M., Kaiser M., Weyher E., Moroder L. Chem. Biol. 13:607-614(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 2-245 OF COMPLEX WITH THE 20S PROTEASOME AND A TMC-95-BASED INHIBITOR.
[10]	"Crystal structures of salinosporamide A (NPI-0052) and B (NPI-0047) in complex with the 20S proteasome reveal important consequences of beta-lactone ring opening and a mechanism for irreversible binding." Groll M., Huber R., Potts B.C.M. J. Am. Chem. Soc. 128:5136-5141(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-245 OF COMPLEX WITH THE 20S PROTEASOME AND SALINOSPORAMIDE.
[11]	"Crystal structure of the boronic acid-based proteasome inhibitor bortezomib in complex with the yeast 20S proteasome." Groll M., Berkers C.R., Ploegh H.L., Ovaa H. Structure 14:451-456(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-245 OF COMPLEX WITH THE 20S PROTEASOME AND BORTEZOMIB.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M63851 Genomic DNA. Translation: AAA34907.1.
X56730 Genomic DNA. Translation: CAA40054.1.
Z72920 Genomic DNA. Translation: CAA97148.1.
BK006941 Genomic DNA. Translation: DAA08228.1.

PIR

SNBYY3. S12940.

RefSeq

NP_011651.3. NM_001181264.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FNT	X-ray	3.20	C/Q	1-245	[»]
1G0U	X-ray	2.40	B/P	1-245	[»]
1G65	X-ray	2.25	B/P	2-245	[»]
1JD2	X-ray	3.00	B/W	2-245	[»]
1RYP	X-ray	1.90	C/Q	2-245	[»]
1VSY	X-ray	3.00	C/Q	14-245	[»]
1Z7Q	X-ray	3.22	C/Q	1-258	[»]
2F16	X-ray	2.80	B/P	2-245	[»]
2FAK	X-ray	2.80	B/P	2-245	[»]
2GPL	X-ray	2.81	B/P	2-245	[»]
2ZCY	X-ray	2.90	B/P	1-258	[»]
3BDM	X-ray	2.70	B/P	1-258	[»]
3D29	X-ray	2.60	B/P	2-245	[»]
3DY3	X-ray	2.81	B/P	2-245	[»]
3DY4	X-ray	2.80	B/P	2-245	[»]
3E47	X-ray	3.00	B/P	2-245	[»]
3GPJ	X-ray	2.70	B/P	2-245	[»]
3GPT	X-ray	2.41	B/P	2-245	[»]
3GPW	X-ray	2.50	B/P	2-245	[»]
3HYE	X-ray	2.50	B/P	2-245	[»]
3L5Q	X-ray	3.00	H/T	14-245	[»]
3MG0	X-ray	2.68	B/P	2-245	[»]
3MG4	X-ray	3.11	B/P	2-245	[»]
3MG6	X-ray	2.60	B/P	1-245	[»]
3MG7	X-ray	2.78	B/P	1-245	[»]
3MG8	X-ray	2.59	B/P	1-245	[»]
3NZJ	X-ray	2.40	B/P	1-258	[»]
3NZW	X-ray	2.50	B/P	1-258	[»]
3NZX	X-ray	2.70	B/P	1-258	[»]
3OEU	X-ray	2.60	B/P	11-245	[»]
3OEV	X-ray	2.85	B/P	11-245	[»]
3OKJ	X-ray	2.70	B/P	2-245	[»]
3SDI	X-ray	2.65	B/P	11-245	[»]
3SDK	X-ray	2.70	B/P	11-245	[»]
3SHJ	X-ray	2.80	B/P	2-245	[»]
3TDD	X-ray	2.70	B/P	2-245	[»]
3UN4	X-ray	3.40	B/P	1-258	[»]
3UN8	X-ray	2.70	B/P	1-258	[»]
4B4T	electron microscopy	7.40	C	1-258	[»]
4FZC	X-ray	2.80	B/P	2-245	[»]
4FZG	X-ray	3.00	B/P	2-245	[»]
4G4S	X-ray	2.49	C	1-258	[»]
4GK7	X-ray	2.80	B/P	2-245	[»]
4INR	X-ray	2.70	B/P	1-258	[»]
4INT	X-ray	2.90	B/P	1-258	[»]
4INU	X-ray	3.10	B/P	1-258	[»]

ProteinModelPortal

P23638.

SMR

P23638. Positions 2-245.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2823N.

IntAct

P23638. 14 interactions.

MINT

MINT-484272.

STRING

4932.YGR135W.

Protein family/group databases

MEROPS

T01.973.

Proteomic databases

PaxDb

P23638.

PeptideAtlas

P23638.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YGR135W; YGR135W; YGR135W.

GeneID

853036.

KEGG

sce:YGR135W.
sce:YGR143W.

Organism-specific databases

CYGD

YGR135w.

SGD

S000003367. PRE9.

Phylogenomic databases

eggNOG

COG0638.

GeneTree

ENSGT00550000074827.

HOGENOM

HOG000091085.

K02728.

OMA

LVSHLCD.

OrthoDB

EOG47Q1G3.

Gene expression databases

Genevestigator

P23638.

GermOnline

YGR135W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR000426. Proteasome_asu_N.
IPR016050. Proteasome_bsu_CS.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]

Pfam

PF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]

SMART

SM00948. Proteasome_A_N. 1 hit.
[Graphical view]

PROSITE

PS00388. PROTEASOME_A_1. 1 hit.
PS51475. PROTEASOME_A_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P23638.

NextBio

972935.

Entry information

Entry name

PSA3_YEAST

Accession

Primary (citable) accession number: P23638
Secondary accession number(s): D6VUR7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	May 1, 2013
This is version 139 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents