Reviewed, UniProtKB/Swiss-Prot P21242 (PSA3_YEAST)

Names and origin

Protein names

Recommended name:
    Proteasome component C1
    EC=3.4.25.1
Alternative name(s):
    Macropain subunit C1
    Proteinase YSCE subunit 1
    Multicatalytic endopeptidase complex subunit C1

Gene names

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

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

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. Ref.3
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
Gene Ontology (GO)
Biological process	ubiquitin-dependent protein catabolic process Traceable author statement. Source: SGD
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell proteasome core complex, alpha-subunit complex Ref.5 Inferred from physical interaction. Source: SGD proteasome storage granule Inferred from direct assay. Source: SGD
Molecular function	protein binding Inferred from physical interaction. Source: IntAct threonine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARO8	P53090	1	EBI-13963,EBI-2042933
ESS1	P22696	1	EBI-13963,EBI-6679
GLN1	P32288	1	EBI-13963,EBI-7665
PRE1	P22141	1	EBI-13963,EBI-13988
PRE8	P23639	1	EBI-13963,EBI-13959
PRE9	P23638	1	EBI-13963,EBI-13967
PUP2	P32379	1	EBI-13963,EBI-13971
RNR2	P09938	1	EBI-13963,EBI-15240
RSP5	P39940	1	EBI-13963,EBI-16219
SCL1	P21243	1	EBI-13963,EBI-13975
SET2	P46995	1	EBI-13963,EBI-16985

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

Proteasome component C1

PRO_0000124102

Amino acid modifications

Modified residue

2

1

Blocked amino end (Thr) Ref.1

Modified residue

278

1

Phosphothreonine Ref.4

Modified residue

279

1

Phosphothreonine Ref.4

Secondary structure

1

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288

Helix Strand Turn

Details...

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

Beta strand

134 – 142

9

Beta strand

145 – 151

7

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)
	P21242-1 [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: 1697860] [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: 9169874] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[4]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-278 AND THR-279, MASS SPECTROMETRY.
[5]	"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: 9087403] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 5-248 OF COMPLEX WITH THE 20S PROTEASOME.
[6]	"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: 11081519] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 1-288 OF COMPLEX WITH THE 20S PROTEASOME AND A 11S REGULATORY COMPLEX.
[7]	"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: 11062564] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-248 OF COMPLEX WITH THE 20S PROTEASOME.
[8]	"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: 16793518] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 5-248 OF COMPLEX WITH THE 20S PROTEASOME AND A TMC-95-BASED INHIBITOR.
[9]	"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: 16608349] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 5-248 OF COMPLEX WITH THE 20S PROTEASOME AND SALINOSPORAMIDE.
[10]	"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: 16531229] [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

EMBLGenBankDDBJ

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

PIR

SNBYC1. S11182.

RefSeq

NP_015007.1.

3D structure databases

PDBPDBe

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	[»]
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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:1526N.

IntAct

P21242. 34 interactions.

STRING

P21242.

Protein family/group databases

MEROPS

T01.977.

Proteomic databases

PeptideAtlas

P21242.

PRIDE

P21242.

Genome annotation databases

Ensembl

YOR362C; YOR362C; YOR362C; Saccharomyces cerevisiae. [Genome view]

GeneID

854544.

GenomeReviews

Gene locus YOR362C in contig Y13140_GR.

KEGG

sce:YOR362C.

NMPDR

fig|4932.3.peg.6126.

Organism-specific databases

CYGD

YOR362c.

SGD

S000005889. PRE10.

Phylogenomic databases

HOGENOM

P21242.

OMA

LSWVGEI.

Enzyme and pathway databases

BRENDA

3.4.25.1. 250.

Gene expression databases

ArrayExpress

P21242.

Genevestigator

P21242.

GermOnline

YOR362C. Saccharomyces cerevisiae.

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...

Other Resources

NextBio

976955.

Entry information

Entry name

PSA3_YEAST

Accession

Primary (citable) accession number: P21242

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)