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P23638 (PSA3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length258 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PRE8P236394EBI-13967,EBI-13959

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 258258Proteasome subunit alpha type-3
PRO_0000124116

Amino acid modifications

Cross-link199Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.5

Secondary structure

............................................ 258
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23638 [UniParc].

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

FASTA25828,714
        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' 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. expand/collapse author list , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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.
[6]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening."
Sadre-Bazzaz K., Whitby F.G., Robinson H., Formosa T., Hill C.P.
Mol. Cell 37:728-735(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 14-245 IN COMPLEX WITH THE PROTEASOME.
[14]"Near-atomic resolution structural model of the yeast 26S proteasome."
Beck F., Unverdorben P., Bohn S., Schweitzer A., Pfeifer G., Sakata E., Nickell S., Plitzko J.M., Villa E., Baumeister W., Forster F.
Proc. Natl. Acad. Sci. U.S.A. 109:14870-14875(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE 26S PROTEASOME.
+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.
PIRSNBYY3. S12940.
RefSeqNP_011651.3. NM_001181264.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20C/Q1-245[»]
1G0UX-ray2.40B/P1-245[»]
1G65X-ray2.25B/P2-245[»]
1JD2X-ray3.00B/W2-245[»]
1RYPX-ray1.90C/Q2-245[»]
1VSYX-ray3.00C/Q14-245[»]
1Z7QX-ray3.22C/Q1-258[»]
2F16X-ray2.80B/P2-245[»]
2FAKX-ray2.80B/P2-245[»]
2GPLX-ray2.81B/P2-245[»]
2ZCYX-ray2.90B/P1-258[»]
3BDMX-ray2.70B/P1-258[»]
3D29X-ray2.60B/P2-245[»]
3DY3X-ray2.81B/P2-245[»]
3DY4X-ray2.80B/P2-245[»]
3E47X-ray3.00B/P2-245[»]
3GPJX-ray2.70B/P2-245[»]
3GPTX-ray2.41B/P2-245[»]
3GPWX-ray2.50B/P2-245[»]
3HYEX-ray2.50B/P2-245[»]
3L5QX-ray3.00H/T14-245[»]
3MG0X-ray2.68B/P2-245[»]
3MG4X-ray3.11B/P2-245[»]
3MG6X-ray2.60B/P1-245[»]
3MG7X-ray2.78B/P1-245[»]
3MG8X-ray2.59B/P1-245[»]
3NZJX-ray2.40B/P1-258[»]
3NZWX-ray2.50B/P1-258[»]
3NZXX-ray2.70B/P1-258[»]
3OEUX-ray2.60B/P11-245[»]
3OEVX-ray2.85B/P11-245[»]
3OKJX-ray2.70B/P2-245[»]
3SDIX-ray2.65B/P11-245[»]
3SDKX-ray2.70B/P11-245[»]
3SHJX-ray2.80B/P2-245[»]
3TDDX-ray2.70B/P2-245[»]
3UN4X-ray3.40B/P1-258[»]
3UN8X-ray2.70B/P1-258[»]
4CR2electron microscopy7.70C1-258[»]
4CR3electron microscopy9.30C1-258[»]
4CR4electron microscopy8.80C1-258[»]
4EU2X-ray2.51C/Q2-245[»]
4FZCX-ray2.80B/P2-245[»]
4FZGX-ray3.00B/P2-245[»]
4G4SX-ray2.49C1-258[»]
4GK7X-ray2.80B/P2-245[»]
4HNPX-ray2.80B/P2-245[»]
4HRCX-ray2.80B/P2-245[»]
4HRDX-ray2.80B/P2-245[»]
4INRX-ray2.70B/P1-258[»]
4INTX-ray2.90B/P1-258[»]
4INUX-ray3.10B/P1-258[»]
4J70X-ray2.80B/P1-258[»]
4JSQX-ray2.80B/P1-258[»]
4JSUX-ray2.90B/P1-258[»]
4JT0X-ray3.10B/P1-258[»]
4LQIX-ray2.70B/P2-245[»]
4NNNX-ray2.50B/P1-258[»]
4NNWX-ray2.60B/P1-258[»]
4NO1X-ray2.50B/P1-258[»]
4NO6X-ray3.00B/P1-258[»]
4NO8X-ray2.70B/P1-258[»]
4NO9X-ray2.90B/P1-258[»]
ProteinModelPortalP23638.
SMRP23638. Positions 2-245.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33383. 325 interactions.
DIPDIP-2823N.
IntActP23638. 17 interactions.
MINTMINT-484272.
STRING4932.YGR135W.

Protein family/group databases

MEROPST01.973.

Proteomic databases

MaxQBP23638.
PaxDbP23638.
PeptideAtlasP23638.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGR135W; YGR135W; YGR135W.
GeneID853036.
KEGGsce:YGR135W.

Organism-specific databases

CYGDYGR135w.
SGDS000003367. PRE9.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00550000074827.
HOGENOMHOG000091085.
KOK02728.
OMAKQEYKDD.
OrthoDBEOG7SBP0C.

Enzyme and pathway databases

BioCycYEAST:G3O-30841-MONOMER.

Gene expression databases

GenevestigatorP23638.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
InterProIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR016050. Proteasome_bsu_CS.
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

EvolutionaryTraceP23638.
NextBio972935.
PROP23638.

Entry information

Entry namePSA3_YEAST
AccessionPrimary (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: June 11, 2014
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references