Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O24361

- PSB5_SPIOL

UniProt

O24361 - PSB5_SPIOL

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Proteasome subunit beta type-5

Gene
N/A
Organism
Spinacia oleracea (Spinach)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

The proteasome is a multicatalytic proteinase complex which 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. The proteasome has an ATP-dependent proteolytic activity.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei56 – 561NucleophileBy similarity

GO - Molecular functioni

  1. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. proteolysis involved in cellular protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Protein family/group databases

MEROPSiT01.A10.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-5 (EC:3.4.25.1)
Alternative name(s):
20S proteasome subunit E
Proteasome epsilon chain
OrganismiSpinacia oleracea (Spinach)
Taxonomic identifieri3562 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

Subcellular locationi

Cytoplasm PROSITE-ProRule annotation. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
  3. proteasome core complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 5555Removed in mature formSequence AnalysisPRO_0000026607Add
BLAST
Chaini56 – 272217Proteasome subunit beta type-5PRO_0000026608Add
BLAST

Keywords - PTMi

Zymogen

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.

Structurei

3D structure databases

ProteinModelPortaliO24361.
SMRiO24361. Positions 56-254.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O24361-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKLDTSGLES TAPIFRRSDF VFDGLQMTPS FDLPNPTDFD GFQKEAVQMV
60 70 80 90 100
KPAKGTTTLA FIFKHGVMVA ADSRASMGGY ISSQSVKKII EINPYMLGTM
110 120 130 140 150
AGGAADCQFW HRNLGIKCRL HELANKRRIS VTGASKLLAN ILYNYRGMGL
160 170 180 190 200
SVGTMIAGWD ETGPGLYYVD SEGGRLKGMR FSVGSGSPYA YGVLDNGYKY
210 220 230 240 250
DMTVEEASEL ARRAIYHATY RDGASGGVVS VYHVGPDGWK KVTGDDVGDL
260 270
HFQYYPVVPA TVEQEMVEVV GA
Length:272
Mass (Da):29,620
Last modified:January 1, 1998 - v1
Checksum:i4D800127F7CEFC3A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D78172 mRNA. Translation: BAA21650.1.
PIRiT09132.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D78172 mRNA. Translation: BAA21650.1 .
PIRi T09132.

3D structure databases

ProteinModelPortali O24361.
SMRi O24361. Positions 56-254.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi T01.A10.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
[Graphical view ]
PRINTSi PR00141. PROTEASOME.
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Characterization of 26S proteasome alpha- and beta-type and ATPase subunits from spinach and their expression during early stages of seedling development."
    Ito N., Tomizawa K., Tanaka K., Matsui M., Kendrick R.E., Sato T., Nakagawa H.
    Plant Mol. Biol. 34:307-316(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiPSB5_SPIOL
AccessioniPrimary (citable) accession number: O24361
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: October 29, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3