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Protein

Probable proteasome subunit alpha type-7

Gene

PRE10

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.

Miscellaneous

Present with 12000 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.PROSITE-ProRule annotation

GO - Molecular functioni

  • mRNA binding Source: SGD
  • threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  • proteasomal ubiquitin-independent protein catabolic process Source: SGD
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: SGD

Keywordsi

Molecular functionHydrolase, Protease, Threonine protease

Enzyme and pathway databases

BioCyciYEAST:G3O-33832-MONOMER
ReactomeiR-SCE-1236978 Cross-presentation of soluble exogenous antigens (endosomes)
R-SCE-174113 SCF-beta-TrCP mediated degradation of Emi1
R-SCE-349425 Autodegradation of the E3 ubiquitin ligase COP1
R-SCE-382556 ABC-family proteins mediated transport
R-SCE-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-SCE-5668541 TNFR2 non-canonical NF-kB pathway
R-SCE-5687128 MAPK6/MAPK4 signaling
R-SCE-5689880 Ub-specific processing proteases
R-SCE-68949 Orc1 removal from chromatin
R-SCE-69017 CDK-mediated phosphorylation and removal of Cdc6
R-SCE-69229 Ubiquitin-dependent degradation of Cyclin D1
R-SCE-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-SCE-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-SCE-983168 Antigen processing: Ubiquitination & Proteasome degradation

Names & Taxonomyi

Protein namesi
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 namesi
Name:PRE10
Synonyms:PRC1, PRS1
Ordered Locus Names:YOR362C
ORF Names:O6650
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR362C
SGDiS000005889 PRE10

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001241022 – 288Probable proteasome subunit alpha type-7Add BLAST287

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonineCombined sources1

Post-translational modificationi

The alpha and beta forms are probably products of the same gene with different post-translational modifications.

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP21242
PaxDbiP21242
PRIDEiP21242

PTM databases

iPTMnetiP21242

Interactioni

Subunit structurei

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.1 Publication

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi34747461 interactors.
DIPiDIP-1526N
IntActiP21242 42 interactors.
MINTiP21242
STRINGi4932.YOR362C

Structurei

Secondary structure

1288
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 10Combined sources3
Beta strandi11 – 13Combined sources3
Beta strandi17 – 19Combined sources3
Helixi22 – 32Combined sources11
Beta strandi37 – 42Combined sources6
Beta strandi45 – 53Combined sources9
Turni61 – 63Combined sources3
Beta strandi68 – 70Combined sources3
Turni71 – 73Combined sources3
Beta strandi74 – 80Combined sources7
Helixi82 – 103Combined sources22
Helixi109 – 122Combined sources14
Turni123 – 125Combined sources3
Beta strandi127 – 129Combined sources3
Beta strandi134 – 142Combined sources9
Beta strandi145 – 151Combined sources7
Turni153 – 155Combined sources3
Beta strandi157 – 166Combined sources10
Helixi169 – 182Combined sources14
Helixi189 – 203Combined sources15
Helixi204 – 207Combined sources4
Beta strandi212 – 220Combined sources9
Turni221 – 223Combined sources3
Beta strandi227 – 230Combined sources4
Helixi234 – 245Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FNTX-ray3.20G/U2-288[»]
1G0UX-ray2.40F/T1-248[»]
1G65X-ray2.25F/T5-248[»]
1JD2X-ray3.001/F5-248[»]
1RYPX-ray1.90G/U5-248[»]
1Z7QX-ray3.22G/U1-288[»]
2F16X-ray2.80F/T5-248[»]
2FAKX-ray2.80F/T5-248[»]
2GPLX-ray2.81F/T5-248[»]
2ZCYX-ray2.90F/T2-288[»]
3BDMX-ray2.70F/T2-288[»]
3D29X-ray2.60F/T5-248[»]
3DY3X-ray2.81F/T5-248[»]
3DY4X-ray2.80F/T5-248[»]
3E47X-ray3.00F/T5-248[»]
3GPJX-ray2.70F/T5-248[»]
3GPTX-ray2.41F/T5-248[»]
3GPWX-ray2.50F/T5-248[»]
3HYEX-ray2.50F/T5-248[»]
3JCOelectron microscopy4.80G/g1-288[»]
3JCPelectron microscopy4.60G/g1-288[»]
3MG0X-ray2.68F/T5-248[»]
3MG4X-ray3.11F/T5-248[»]
3MG6X-ray2.60F/T1-248[»]
3MG7X-ray2.78F/T1-248[»]
3MG8X-ray2.59F/T1-248[»]
3NZJX-ray2.40F/T1-288[»]
3NZWX-ray2.50F/T1-288[»]
3NZXX-ray2.70F/T1-288[»]
3OEUX-ray2.60F/T7-248[»]
3OEVX-ray2.85F/T7-248[»]
3OKJX-ray2.70F/T5-248[»]
3SDIX-ray2.65F/T7-248[»]
3SDKX-ray2.70F/T7-248[»]
3SHJX-ray2.80F/T5-248[»]
3TDDX-ray2.70F/T5-248[»]
3UN4X-ray3.40F/T1-288[»]
3UN8X-ray2.70F/T1-288[»]
3WXRX-ray3.15G/U13-288[»]
4CR2electron microscopy7.70G1-288[»]
4CR3electron microscopy9.30G1-288[»]
4CR4electron microscopy8.80G1-288[»]
4EU2X-ray2.51G/U5-248[»]
4FZCX-ray2.80F/T5-248[»]
4FZGX-ray3.00F/T5-248[»]
4G4SX-ray2.49G1-288[»]
4GK7X-ray2.80F/T5-248[»]
4HNPX-ray2.80F/T5-248[»]
4HRCX-ray2.80F/T5-248[»]
4HRDX-ray2.80F/T5-248[»]
4INRX-ray2.70F/T1-288[»]
4INTX-ray2.90F/T1-288[»]
4INUX-ray3.10F/T1-288[»]
4J70X-ray2.80F/T1-288[»]
4JSQX-ray2.80F/T1-288[»]
4JSUX-ray2.90F/T1-288[»]
4JT0X-ray3.10F/T1-288[»]
4LQIX-ray2.70F/T5-248[»]
4LTCX-ray2.50F/T2-288[»]
4NNNX-ray2.50F/T1-288[»]
4NNWX-ray2.60F/T1-288[»]
4NO1X-ray2.50F/T1-288[»]
4NO6X-ray3.00F/T1-288[»]
4NO8X-ray2.70F/T1-288[»]
4NO9X-ray2.90F/T1-288[»]
4Q1SX-ray2.60F/T1-288[»]
4QBYX-ray3.00F/T1-288[»]
4QLQX-ray2.40F/T1-288[»]
4QLSX-ray2.80F/T1-288[»]
4QLTX-ray2.80F/T1-288[»]
4QLUX-ray2.80F/T1-288[»]
4QLVX-ray2.90F/T1-288[»]
4QUXX-ray3.00F/T1-288[»]
4QUYX-ray2.80F/T1-288[»]
4QV0X-ray3.10F/T1-288[»]
4QV1X-ray2.50F/T1-288[»]
4QV3X-ray3.00F/T1-288[»]
4QV4X-ray2.70F/T1-288[»]
4QV5X-ray2.70F/T1-288[»]
4QV6X-ray2.80F/T1-288[»]
4QV7X-ray2.60F/T1-288[»]
4QV8X-ray2.90F/T1-288[»]
4QV9X-ray2.60F/T1-288[»]
4QVLX-ray2.80F/T1-288[»]
4QVMX-ray2.80F/T1-288[»]
4QVNX-ray2.90F/T1-288[»]
4QVPX-ray2.30F/T1-288[»]
4QVQX-ray2.60F/T1-288[»]
4QVVX-ray2.80F/T1-288[»]
4QVWX-ray3.00F/T1-288[»]
4QVYX-ray2.51F/T1-288[»]
4QW0X-ray2.90F/T1-288[»]
4QW1X-ray2.90F/T1-288[»]
4QW3X-ray2.90F/T1-288[»]
4QW4X-ray2.80F/T1-288[»]
4QW5X-ray3.00F/T1-288[»]
4QW6X-ray2.90F/T1-288[»]
4QW7X-ray2.70F/T1-288[»]
4QWFX-ray3.00F/T1-288[»]
4QWGX-ray2.60F/T1-288[»]
4QWIX-ray2.60F/T1-288[»]
4QWJX-ray2.90F/T1-288[»]
4QWKX-ray2.80F/T1-288[»]
4QWLX-ray2.60F/T1-288[»]
4QWRX-ray2.90F/T1-288[»]
4QWSX-ray3.00F/T1-288[»]
4QWUX-ray3.00F/T1-288[»]
4QWXX-ray2.90F/T1-288[»]
4QXJX-ray2.80F/T1-288[»]
4QZ0X-ray3.00F/T1-288[»]
4QZ1X-ray3.00F/T1-288[»]
4QZ2X-ray2.70F/T1-288[»]
4QZ3X-ray2.80F/T1-288[»]
4QZ4X-ray3.00F/T1-288[»]
4QZ5X-ray2.80F/T1-288[»]
4QZ6X-ray2.90F/T1-288[»]
4QZ7X-ray2.80F/T1-288[»]
4QZWX-ray3.00F/T1-288[»]
4QZXX-ray2.60F/T1-288[»]
4QZZX-ray2.90F/T1-288[»]
4R00X-ray2.80F/T1-288[»]
4R02X-ray2.50F/T1-288[»]
4R17X-ray2.10F/T1-288[»]
4R18X-ray2.40F/T1-288[»]
4RURX-ray2.50F/T1-288[»]
4V7OX-ray3.00AL/AX/BG/BU5-248[»]
4X6ZX-ray2.70G/U1-288[»]
4Y69X-ray2.90F/T1-288[»]
4Y6AX-ray2.60F/T1-288[»]
4Y6VX-ray2.80F/T1-288[»]
4Y6ZX-ray2.70F/T1-288[»]
4Y70X-ray2.40F/T1-288[»]
4Y74X-ray2.70F/T1-288[»]
4Y75X-ray2.80F/T1-288[»]
4Y77X-ray2.50F/T1-288[»]
4Y78X-ray2.80F/T1-288[»]
4Y7WX-ray2.50F/T1-288[»]
4Y7XX-ray2.60F/T1-288[»]
4Y7YX-ray2.40F/T1-288[»]
4Y80X-ray2.50F/T1-288[»]
4Y81X-ray2.80F/T1-288[»]
4Y82X-ray2.80F/T1-288[»]
4Y84X-ray2.70F/T1-288[»]
4Y8GX-ray2.60F/T1-288[»]
4Y8HX-ray2.50F/T1-288[»]
4Y8IX-ray2.60F/T1-288[»]
4Y8JX-ray2.70F/T1-288[»]
4Y8KX-ray2.60F/T1-288[»]
4Y8LX-ray2.40F/T1-288[»]
4Y8MX-ray2.80F/T1-288[»]
4Y8NX-ray2.60F/T1-288[»]
4Y8OX-ray2.70F/T1-288[»]
4Y8PX-ray2.80F/T1-288[»]
4Y8QX-ray2.60F/T1-288[»]
4Y8RX-ray2.70F/T1-288[»]
4Y8SX-ray2.70F/T1-288[»]
4Y8TX-ray2.70F/T1-288[»]
4Y8UX-ray2.90F/T1-288[»]
4Y9YX-ray2.80F/T1-288[»]
4Y9ZX-ray2.80F/T1-288[»]
4YA0X-ray2.80F/T1-288[»]
4YA1X-ray2.90F/T1-288[»]
4YA2X-ray2.70F/T1-288[»]
4YA3X-ray2.70F/T1-288[»]
4YA4X-ray2.90F/T1-288[»]
4YA5X-ray2.50F/T1-288[»]
4YA7X-ray2.70F/T1-288[»]
4YA9X-ray2.70F/T1-288[»]
4Z1LX-ray3.00F/T1-288[»]
5A5Belectron microscopy9.50G1-288[»]
5AHJX-ray2.80F/T1-288[»]
5BOUX-ray2.60F/T1-288[»]
5BXLX-ray2.80F/T1-288[»]
5BXNX-ray2.80F/T1-288[»]
5CGFX-ray2.80F/T1-288[»]
5CGGX-ray2.90F/T1-288[»]
5CGHX-ray2.50F/T1-288[»]
5CGIX-ray2.80F/T1-288[»]
5CZ4X-ray2.30F/T1-288[»]
5CZ5X-ray2.80F/T1-288[»]
5CZ6X-ray2.70F/T1-288[»]
5CZ7X-ray2.50F/T1-288[»]
5CZ8X-ray2.80F/T1-288[»]
5CZ9X-ray2.90F/T1-288[»]
5CZAX-ray2.50F/T1-288[»]
5D0SX-ray2.50F/T1-288[»]
5D0TX-ray2.60F/T1-288[»]
5D0VX-ray2.90F/T1-288[»]
5D0WX-ray2.80F/T1-288[»]
5D0XX-ray2.60F/T1-288[»]
5D0ZX-ray2.90F/T1-288[»]
5DKIX-ray2.80F/T1-288[»]
5DKJX-ray2.80F/T1-288[»]
5FG7X-ray2.70F/T1-288[»]
5FG9X-ray2.60F/T1-288[»]
5FGAX-ray2.70F/T1-288[»]
5FGDX-ray2.80F/T1-288[»]
5FGEX-ray2.60F/T1-288[»]
5FGFX-ray2.60F/T1-288[»]
5FGGX-ray2.70F/T1-288[»]
5FGHX-ray2.80F/T1-288[»]
5FGIX-ray2.90F/T1-288[»]
5FHSX-ray2.70F/T1-288[»]
5JHRX-ray2.90F/T1-288[»]
5JHSX-ray3.00F/T1-288[»]
5L52X-ray2.70F/T1-288[»]
5L54X-ray2.80F/T1-288[»]
5L55X-ray2.90F/T1-288[»]
5L5AX-ray2.40F/T1-288[»]
5L5BX-ray2.80F/T1-288[»]
5L5DX-ray2.80F/T1-288[»]
5L5EX-ray2.90F/T1-288[»]
5L5FX-ray2.50F/T1-288[»]
5L5HX-ray2.60F/T1-288[»]
5L5IX-ray2.90F/T1-288[»]
5L5JX-ray2.90F/T1-288[»]
5L5OX-ray2.60F/T1-288[»]
5L5PX-ray2.80F/T1-288[»]
5L5QX-ray2.80F/T1-288[»]
5L5RX-ray2.90F/T1-288[»]
5L5SX-ray2.60F/T1-288[»]
5L5TX-ray2.90F/T1-288[»]
5L5UX-ray2.60F/T1-288[»]
5L5VX-ray2.70F/T1-288[»]
5L5WX-ray2.80F/T1-288[»]
5L5XX-ray2.90F/T1-288[»]
5L5YX-ray2.70F/T1-288[»]
5L5ZX-ray2.70F/T1-288[»]
5L60X-ray2.70F/T1-288[»]
5L61X-ray2.80F/T1-288[»]
5L62X-ray2.80F/T1-288[»]
5L63X-ray2.70F/T1-288[»]
5L64X-ray2.70F/T1-288[»]
5L65X-ray2.90F/T1-288[»]
5L66X-ray2.80F/T1-288[»]
5L67X-ray2.60F/T1-288[»]
5L68X-ray2.80F/T1-288[»]
5L69X-ray2.70F/T1-288[»]
5L6AX-ray2.80F/T1-288[»]
5L6BX-ray2.60F/T1-288[»]
5L6CX-ray2.60F/T1-288[»]
5LAIX-ray2.50F/T1-288[»]
5LAJX-ray2.90F/T1-288[»]
5LTTX-ray2.70F/T1-288[»]
5M2BX-ray2.70F/T1-288[»]
5MP9electron microscopy4.10G/g1-288[»]
5MPAelectron microscopy4.50G/g1-288[»]
5MPBelectron microscopy7.80G/g1-288[»]
5MPCelectron microscopy7.70G/g1-288[»]
5NIFX-ray3.00G/U1-288[»]
5WVIelectron microscopy6.30G/k1-288[»]
5WVKelectron microscopy4.20G/k1-288[»]
ProteinModelPortaliP21242
SMRiP21242
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21242

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00550000074912
HOGENOMiHOG000091086
InParanoidiP21242
KOiK02727
OMAiFELEMTW
OrthoDBiEOG092C47D8

Family and domain databases

Gene3Di3.60.20.101 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR023332 Proteasome_alpha-type
IPR037555 Proteasome_alpha_3
IPR000426 Proteasome_asu_N
IPR001353 Proteasome_sua/b
PANTHERiPTHR11599:SF10 PTHR11599:SF10, 1 hit
PfamiView protein in Pfam
PF00227 Proteasome, 1 hit
PF10584 Proteasome_A_N, 1 hit
SMARTiView protein in SMART
SM00948 Proteasome_A_N, 1 hit
SUPFAMiSSF56235 SSF56235, 1 hit
PROSITEiView protein in PROSITE
PS00388 PROTEASOME_ALPHA_1, 1 hit
PS51475 PROTEASOME_ALPHA_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21242-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSIGTGYDL SNSVFSPDGR NFQVEYAVKA VENGTTSIGI KCNDGVVFAV
60 70 80 90 100
EKLITSKLLV PQKNVKIQVV DRHIGCVYSG LIPDGRHLVN RGREEAASFK
110 120 130 140 150
KLYKTPIPIP AFADRLGQYV QAHTLYNSVR PFGVSTIFGG VDKNGAHLYM
160 170 180 190 200
LEPSGSYWGY KGAATGKGRQ SAKAELEKLV DHHPEGLSAR EAVKQAAKII
210 220 230 240 250
YLAHEDNKEK DFELEISWCS LSETNGLHKF VKGDLLQEAI DFAQKEINGD
260 270 280
DDEDEDDSDN VMSSDDENAP VATNANATTD QEGDIHLE
Length:288
Mass (Da):31,536
Last modified:January 23, 2007 - v2
Checksum:i1E51D904CF336747
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55436 mRNA Translation: AAA35227.1
Z75270 Genomic DNA Translation: CAA99691.1
BK006948 Genomic DNA Translation: DAA11123.1
PIRiS11182 SNBYC1
RefSeqiNP_015007.1, NM_001183782.1

Genome annotation databases

EnsemblFungiiYOR362C; YOR362C; YOR362C
GeneIDi854544
KEGGisce:YOR362C

Similar proteinsi

Entry informationi

Entry nameiPSA7_YEAST
AccessioniPrimary (citable) accession number: P21242
Secondary accession number(s): D6W357
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 203 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome