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Protein

Proteasome subunit alpha type-1-B

Gene

PAF2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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. May play a role in thiol biosynthesis and arsenic tolerance in association with PAF1/ARS5.1 Publication

Catalytic activityi

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

GO - Molecular functioni

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

GO - Biological processi

  1. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

BioCyciARA:AT1G47250-MONOMER.
ReactomeiREACT_275043. Orc1 removal from chromatin.
REACT_283762. Hedgehog 'on' state.
REACT_295391. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_301780. APC/C:Cdc20 mediated degradation of Securin.
REACT_302317. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_305944. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_309046. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_318090. Separation of Sister Chromatids.
REACT_319658. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_327677. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_336812. ER-Phagosome pathway.
REACT_340730. Autodegradation of the E3 ubiquitin ligase COP1.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-1-B (EC:3.4.25.1)
Alternative name(s):
20S proteasome alpha subunit F-2
Proteasome component 2B
Proteasome subunit alpha type-6
Gene namesi
Name:PAF2
Synonyms:PRC2B, PRS1
Ordered Locus Names:At1g47250
ORF Names:F8G22.3
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G47250.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytosol Source: TAIR
  2. nucleus Source: UniProtKB-SubCell
  3. plasma membrane Source: TAIR
  4. plasmodesma Source: TAIR
  5. proteasome complex Source: TAIR
  6. proteasome core complex, alpha-subunit complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Disruption phenotypei

Do not show arsenic tolerance phenotype.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 277277Proteasome subunit alpha type-1-BPRO_0000124073Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiO23712.
PRIDEiO23712.

Expressioni

Gene expression databases

GenevestigatoriO23712.

Interactioni

Subunit structurei

Component of the 20S core complex of the 26S proteasome. The 26S proteasome is composed of a core protease (CP), known as the 20S proteasome, capped at one or both ends by the 19S regulatory particle (RP/PA700). 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.3 Publications

Protein-protein interaction databases

BioGridi26353. 2 interactions.
IntActiO23712. 1 interaction.
STRINGi3702.AT1G47250.1-P.

Structurei

3D structure databases

ProteinModelPortaliO23712.
SMRiO23712. Positions 4-240.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000091080.
InParanoidiO23712.
KOiK02725.
OMAiDVAPMEI.
PhylomeDBiO23712.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTiSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O23712-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFRNQYDTDV TTWSPTGRLF QVEYAMEAVK QGSAAIGLRS RSHVVLACVN
60 70 80 90 100
KAQSELSSHQ RKIFKVDDHI GVAIAGLTAD GRVLSRYMRS ESINHSFTYE
110 120 130 140 150
SPLPVGRLVV HLADKAQVCT QRSWKRPYGV GLLVGGLDES GAHLYYNCPS
160 170 180 190 200
GNYFEYQAFA IGSRSQAAKT YLERKFESFQ ESSKEDLIKD AIMAIRETLQ
210 220 230 240 250
GETLKSSLCT VSVLGVDEPF HFLDQESIQK VIDTFEKVPE EEEDAGEGEA
260 270
EPEAAPGAAG TGEQGGSGDQ DVAPMEI
Length:277
Mass (Da):30,410
Last modified:May 1, 1999 - v2
Checksum:iC5FBCE302217C521
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF043527 mRNA. Translation: AAC32063.1.
AC079677 Genomic DNA. Translation: AAG52642.1.
CP002684 Genomic DNA. Translation: AEE32143.1.
AY057649 mRNA. Translation: AAL15280.1.
AY141996 mRNA. Translation: AAM98260.1.
Y13182 mRNA. Translation: CAA73625.1.
PIRiT51975.
RefSeqiNP_175158.1. NM_103619.4.
UniGeneiAt.48280.

Genome annotation databases

EnsemblPlantsiAT1G47250.1; AT1G47250.1; AT1G47250.
GeneIDi841128.
KEGGiath:AT1G47250.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF043527 mRNA. Translation: AAC32063.1.
AC079677 Genomic DNA. Translation: AAG52642.1.
CP002684 Genomic DNA. Translation: AEE32143.1.
AY057649 mRNA. Translation: AAL15280.1.
AY141996 mRNA. Translation: AAM98260.1.
Y13182 mRNA. Translation: CAA73625.1.
PIRiT51975.
RefSeqiNP_175158.1. NM_103619.4.
UniGeneiAt.48280.

3D structure databases

ProteinModelPortaliO23712.
SMRiO23712. Positions 4-240.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi26353. 2 interactions.
IntActiO23712. 1 interaction.
STRINGi3702.AT1G47250.1-P.

Proteomic databases

PaxDbiO23712.
PRIDEiO23712.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G47250.1; AT1G47250.1; AT1G47250.
GeneIDi841128.
KEGGiath:AT1G47250.

Organism-specific databases

TAIRiAT1G47250.

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000091080.
InParanoidiO23712.
KOiK02725.
OMAiDVAPMEI.
PhylomeDBiO23712.

Enzyme and pathway databases

BioCyciARA:AT1G47250-MONOMER.
ReactomeiREACT_275043. Orc1 removal from chromatin.
REACT_283762. Hedgehog 'on' state.
REACT_295391. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_301780. APC/C:Cdc20 mediated degradation of Securin.
REACT_302317. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_305944. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_309046. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_318090. Separation of Sister Chromatids.
REACT_319658. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_327677. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_336812. ER-Phagosome pathway.
REACT_340730. Autodegradation of the E3 ubiquitin ligase COP1.

Miscellaneous databases

PROiO23712.

Gene expression databases

GenevestigatoriO23712.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view]
SMARTiSM00948. Proteasome_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular organization of the 20S proteasome gene family from Arabidopsis thaliana."
    Fu H., Doelling J.H., Arendt C.S., Hochstrasser M., Vierstra R.D.
    Genetics 149:677-692(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, NOMENCLATURE.
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "The 20S proteasome gene family in Arabidopsis thaliana."
    Parmentier Y., Bouchez D., Fleck J., Genschik P.
    FEBS Lett. 416:281-285(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-277.
    Strain: cv. Columbia.
  6. "Structure and functional analyses of the 26S proteasome subunits from plants."
    Fu H., Girod P.-A., Doelling J.H., van Nocker S., Hochstrasser M., Finley D., Vierstra R.D.
    Mol. Biol. Rep. 26:137-146(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  7. "Purification of the Arabidopsis 26 S proteasome: biochemical and molecular analyses revealed the presence of multiple isoforms."
    Yang P., Fu H., Walker J., Papa C.M., Smalle J., Ju Y.-M., Vierstra R.D.
    J. Biol. Chem. 279:6401-6413(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "ARS5 is a component of the 26S proteasome complex, and negatively regulates thiol biosynthesis and arsenic tolerance in Arabidopsis."
    Sung D.-Y., Kim T.-H., Komives E.A., Mendoza-Cozatl D.G., Schroeder J.I.
    Plant J. 59:802-812(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  9. "Affinity purification of the Arabidopsis 26 S proteasome reveals a diverse array of plant proteolytic complexes."
    Book A.J., Gladman N.P., Lee S.S., Scalf M., Smith L.M., Vierstra R.D.
    J. Biol. Chem. 285:25554-25569(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S PROTEASOME COMPLEX, SUBUNIT, ACETYLATION AT MET-1.

Entry informationi

Entry nameiPSA1B_ARATH
AccessioniPrimary (citable) accession number: O23712
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: May 1, 1999
Last modified: April 1, 2015
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.