P21242 (PSA7_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable proteasome subunit alpha type-7
EC=3.4.25.1

Alternative name(s):
Macropain subunit C1
Multicatalytic endopeptidase complex subunit C1
Proteasome component C1
Proteinase YSCE subunit 1

Gene names

Name:	PRE10
Synonyms:	PRC1, PRS1
Ordered Locus Names:	YOR362C
ORF Names:	O6650

Organism

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

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	288 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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.
Post-translational modification	The alpha and beta forms are probably products of the same gene with different post-translational modifications.
Miscellaneous	Present with 12000 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	Phosphoprotein
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 11545745PubMed 19029916. Source: SGD proteasomal ubiquitin-independent protein catabolic process Inferred from direct assay PubMed 19162040. 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	mRNA binding Inferred from direct assay PubMed 21124907. Source: SGD threonine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PRE1	P22141	3	EBI-13963,EBI-13988
SCL1	P21243	6	EBI-13963,EBI-13975

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.1

Chain

2 – 288

287

Probable proteasome subunit alpha type-7

PRO_0000124102

Amino acid modifications

Modified residue

2

1

Blocked amino end (Thr) Ref.1

Modified residue

278

1

Phosphothreonine Ref.5

Modified residue

279

1

Phosphothreonine Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

288

Helix Strand Turn

Details...

Beta strand

8 – 11

4

Helix

22 – 32

11

Beta strand

37 – 42

6

Beta strand

45 – 53

9

Turn

61 – 63

3

Beta strand

68 – 70

3

Turn

71 – 73

3

Beta strand

74 – 80

7

Helix

82 – 103

22

Helix

109 – 122

14

Turn

123 – 125

3

Beta strand

127 – 129

3

Beta strand

134 – 142

9

Beta strand

145 – 151

7

Turn

153 – 155

3

Beta strand

157 – 166

10

Helix

169 – 182

14

Helix

189 – 203

15

Helix

204 – 207

4

Beta strand

212 – 220

9

Turn

221 – 223

3

Beta strand

227 – 230

4

Helix

234 – 245

12

Sequences

	Sequence		Length	Mass (Da)
	P21242 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 1E51D904CF336747	FASTA	288	31,536
	10 20 30 40 50 60 MTSIGTGYDL SNSVFSPDGR NFQVEYAVKA VENGTTSIGI KCNDGVVFAV EKLITSKLLV 70 80 90 100 110 120 PQKNVKIQVV DRHIGCVYSG LIPDGRHLVN RGREEAASFK KLYKTPIPIP AFADRLGQYV 130 140 150 160 170 180 QAHTLYNSVR PFGVSTIFGG VDKNGAHLYM LEPSGSYWGY KGAATGKGRQ SAKAELEKLV 190 200 210 220 230 240 DHHPEGLSAR EAVKQAAKII YLAHEDNKEK DFELEISWCS LSETNGLHKF VKGDLLQEAI 250 260 270 280 DFAQKEINGD DDEDEDDSDN VMSSDDENAP VATNANATTD QEGDIHLE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Proteasomes are essential for yeast proliferation. cDNA cloning and gene disruption of two major subunits." Fujiwara T., Tanaka K., Orino E., Yoshimura T., Kumatori A., Tamura T., Chung C.H., Nakai T., Yamaguchi K., Shin S., Kakizuka A., Nakanishi S., Ichihara A. J. Biol. Chem. 265:16604-16613(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 106-135; 180-195 AND 200-209, CLEAVAGE OF INITIATOR METHIONINE.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K. Nature 387:98-102(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 multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-278 AND THR-279, 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 5-248 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 1-288 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 1-248 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 5-248 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 5-248 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 5-248 OF COMPLEX WITH THE 20S PROTEASOME AND BORTEZOMIB.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M55436 mRNA. Translation: AAA35227.1.
Z75270 Genomic DNA. Translation: CAA99691.1.
BK006948 Genomic DNA. Translation: DAA11123.1.

PIR

SNBYC1. S11182.

RefSeq

NP_015007.1. NM_001183782.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FNT	X-ray	3.20	G/U	2-288	[»]
1G0U	X-ray	2.40	F/T	1-248	[»]
1G65	X-ray	2.25	F/T	5-248	[»]
1JD2	X-ray	3.00	1/F	5-247	[»]
1RYP	X-ray	1.90	G/U	5-248	[»]
1VSY	X-ray	3.00	G/U	5-248	[»]
1Z7Q	X-ray	3.22	G/U	1-288	[»]
2F16	X-ray	2.80	F/T	5-248	[»]
2FAK	X-ray	2.80	F/T	5-248	[»]
2GPL	X-ray	2.81	F/T	5-248	[»]
2ZCY	X-ray	2.90	F/T	2-288	[»]
3BDM	X-ray	2.70	F/T	2-288	[»]
3D29	X-ray	2.60	F/T	5-248	[»]
3DY3	X-ray	2.81	F/T	5-248	[»]
3DY4	X-ray	2.80	F/T	5-248	[»]
3E47	X-ray	3.00	F/T	5-248	[»]
3GPJ	X-ray	2.70	F/T	5-248	[»]
3GPT	X-ray	2.41	F/T	5-248	[»]
3GPW	X-ray	2.50	F/T	5-248	[»]
3HYE	X-ray	2.50	F/T	5-248	[»]
3L5Q	X-ray	3.00	L/X	5-248	[»]
3MG0	X-ray	2.68	F/T	5-248	[»]
3MG4	X-ray	3.11	F/T	5-248	[»]
3MG6	X-ray	2.60	F/T	1-248	[»]
3MG7	X-ray	2.78	F/T	1-248	[»]
3MG8	X-ray	2.59	F/T	1-248	[»]
3NZJ	X-ray	2.40	F/T	1-288	[»]
3NZW	X-ray	2.50	F/T	1-288	[»]
3NZX	X-ray	2.70	F/T	1-288	[»]
3OEU	X-ray	2.60	F/T	7-248	[»]
3OEV	X-ray	2.85	F/T	7-248	[»]
3OKJ	X-ray	2.70	F/T	5-248	[»]
3SDI	X-ray	2.65	F/T	7-248	[»]
3SDK	X-ray	2.70	F/T	7-248	[»]
3SHJ	X-ray	2.80	F/T	5-248	[»]
3TDD	X-ray	2.70	F/T	5-248	[»]
3UN4	X-ray	3.40	F/T	1-288	[»]
3UN8	X-ray	2.70	F/T	1-288	[»]
4B4T	electron microscopy	7.40	G	1-288	[»]
4FZC	X-ray	2.80	F/T	5-248	[»]
4FZG	X-ray	3.00	F/T	5-248	[»]
4G4S	X-ray	2.49	G	1-288	[»]
4GK7	X-ray	2.80	F/T	5-248	[»]
4INR	X-ray	2.70	F/T	1-288	[»]
4INT	X-ray	2.90	F/T	1-288	[»]
4INU	X-ray	3.10	F/T	1-288	[»]

ProteinModelPortal

P21242.

SMR

P21242. Positions 5-248.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1526N.

IntAct

P21242. 29 interactions.

MINT

MINT-411846.

STRING

4932.YOR362C.

Protein family/group databases

MEROPS

T01.977.

Proteomic databases

PaxDb

P21242.

PeptideAtlas

P21242.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YOR362C; YOR362C; YOR362C.

GeneID

854544.

KEGG

sce:YOR362C.

Organism-specific databases

SGD

S000005889. PRE10.

Phylogenomic databases

eggNOG

COG0638.

GeneTree

ENSGT00550000074912.

HOGENOM

HOG000091086.

KO

K02727.

OMA

NKRIFNI.

OrthoDB

EOG41CB5B.

Enzyme and pathway databases

BioCyc

YEAST:G3O-33832-MONOMER.

Gene expression databases

Genevestigator

P21242.

GermOnline

YOR362C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR000426. Proteasome_asu_N.
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

P21242.

NextBio

976955.

Entry information

Entry name

PSA7_YEAST

Accession

Primary (citable) accession number: P21242
Secondary accession number(s): D6W357

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 151 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program