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P30186

- PSA7A_ARATH

UniProt

P30186 - PSA7A_ARATH

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Protein

Proteasome subunit alpha type-7-A

Gene

PAD1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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. Mediates the association of the SCF(TIR1) E3 ubiquitin ligase complex with the proteasome.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:AT3G51260-MONOMER.
ARA:GQT-713-MONOMER.
ReactomeiREACT_106068. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_107429. Orc1 removal from chromatin.
REACT_185297. Separation of Sister Chromatids.
REACT_187712. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_187719. ER-Phagosome pathway.
REACT_187848. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_190947. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_94347. APC/C:Cdc20 mediated degradation of Securin.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-7-A (EC:3.4.25.1)
Alternative name(s):
20S proteasome alpha subunit D-1
Proteasome component 6A
Proteasome subunit alpha type-4
TAS-G64
Gene namesi
Name:PAD1
Synonyms:PRC6A
Ordered Locus Names:At3g51260
ORF Names:F24M12.300
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 3

Organism-specific databases

TAIRiAT3G51260.

Subcellular locationi

Cytoplasm By similarity. Nucleus 1 Publication

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. cytosol Source: TAIR
  3. cytosolic ribosome Source: TAIR
  4. nucleus Source: TAIR
  5. phragmoplast Source: TAIR
  6. proteasome complex Source: TAIR
  7. proteasome core complex, alpha-subunit complex Source: InterPro
  8. spindle Source: TAIR
  9. vacuolar membrane Source: TAIR
  10. vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 250250Proteasome subunit alpha type-7-APRO_0000124159Add
BLAST

Proteomic databases

PaxDbiP30186.
PRIDEiP30186.

Expressioni

Tissue specificityi

Expressed in roots, leaves and flowers.1 Publication

Inductioni

During cell proliferation.1 Publication

Gene expression databases

ExpressionAtlasiP30186. baseline and differential.
GenevestigatoriP30186.

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. Interacts with KIN10 and KIN11 SnRK subunits, and with the SKP1A/ASK1 subunit of the SCF E3 ubiquitin ligase complex.4 Publications

Protein-protein interaction databases

BioGridi9607. 7 interactions.
IntActiP30186. 4 interactions.

Structurei

3D structure databases

ProteinModelPortaliP30186.
SMRiP30186. Positions 4-232.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000091085.
InParanoidiP30186.
KOiK02731.
OMAiPYTQKPA.
PhylomeDBiP30186.

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.

This entry describes 1 isoform i produced by alternative splicing. Align

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: P30186-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MARYDRAITV FSPDGHLFQV EYALEAVRKG NAAVGVRGTD TVVLAVEKKS
60 70 80 90 100
TPKLQDSRSA RKIVSLDNHI ALACAGLKAD ARVLINKARI ECQSHRLTLE
110 120 130 140 150
DPVTVEYITR YIAGLQQKYT QSGGVRPFGL STLIVGFDPY TRIPALYQTD
160 170 180 190 200
PSGTFSAWKA NATGRNSNSI REFLEKNYKE SAGQETVKLA IRALLEVVES
210 220 230 240 250
GGKNIEVAVM TREEGVLKQL EEEEIDIIVA EIEAEKAAAE AAKKGPAKET
Length:250
Mass (Da):27,337
Last modified:April 1, 1993 - v1
Checksum:iE026335F50C74AA3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151G → N in CAA79082. 1 PublicationCurated
Sequence conflicti27 – 271V → L in AAM64989. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66825 mRNA. Translation: CAA47298.1.
AF043522 mRNA. Translation: AAC32058.1.
AL132980 Genomic DNA. Translation: CAB62648.1.
CP002686 Genomic DNA. Translation: AEE78769.1.
AY042820 mRNA. Translation: AAK68760.1.
AY052321 mRNA. Translation: AAK96514.1.
AY061899 mRNA. Translation: AAL31226.1.
AY081448 mRNA. Translation: AAM10010.1.
AY087443 mRNA. Translation: AAM64989.1.
Z17987 mRNA. Translation: CAA79082.1.
PIRiS29240.
RefSeqiNP_190694.1. NM_114985.2. [P30186-1]
UniGeneiAt.19974.
At.67272.

Genome annotation databases

EnsemblPlantsiAT3G51260.1; AT3G51260.1; AT3G51260. [P30186-1]
GeneIDi824289.
KEGGiath:AT3G51260.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66825 mRNA. Translation: CAA47298.1 .
AF043522 mRNA. Translation: AAC32058.1 .
AL132980 Genomic DNA. Translation: CAB62648.1 .
CP002686 Genomic DNA. Translation: AEE78769.1 .
AY042820 mRNA. Translation: AAK68760.1 .
AY052321 mRNA. Translation: AAK96514.1 .
AY061899 mRNA. Translation: AAL31226.1 .
AY081448 mRNA. Translation: AAM10010.1 .
AY087443 mRNA. Translation: AAM64989.1 .
Z17987 mRNA. Translation: CAA79082.1 .
PIRi S29240.
RefSeqi NP_190694.1. NM_114985.2. [P30186-1 ]
UniGenei At.19974.
At.67272.

3D structure databases

ProteinModelPortali P30186.
SMRi P30186. Positions 4-232.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 9607. 7 interactions.
IntActi P30186. 4 interactions.

Proteomic databases

PaxDbi P30186.
PRIDEi P30186.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT3G51260.1 ; AT3G51260.1 ; AT3G51260 . [P30186-1 ]
GeneIDi 824289.
KEGGi ath:AT3G51260.

Organism-specific databases

TAIRi AT3G51260.

Phylogenomic databases

eggNOGi COG0638.
HOGENOMi HOG000091085.
InParanoidi P30186.
KOi K02731.
OMAi PYTQKPA.
PhylomeDBi P30186.

Enzyme and pathway databases

BioCyci ARA:AT3G51260-MONOMER.
ARA:GQT-713-MONOMER.
Reactomei REACT_106068. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_107429. Orc1 removal from chromatin.
REACT_185297. Separation of Sister Chromatids.
REACT_187712. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_187719. ER-Phagosome pathway.
REACT_187848. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_190947. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_94347. APC/C:Cdc20 mediated degradation of Securin.

Gene expression databases

ExpressionAtlasi P30186. baseline and differential.
Genevestigatori P30186.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR000426. Proteasome_asu_N.
IPR023332. Proteasome_suA-type.
IPR001353. Proteasome_sua/b.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
PF10584. Proteasome_A_N. 1 hit.
[Graphical view ]
SMARTi SM00948. Proteasome_A_N. 1 hit.
[Graphical view ]
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00388. PROTEASOME_ALPHA_1. 1 hit.
PS51475. PROTEASOME_ALPHA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequence analysis of a cDNA clone from Arabidopsis thaliana homologous to a proteasome alpha subunit from Drosophila."
    Genschik P., Philipps G., Gigot C., Fleck J.
    FEBS Lett. 309:311-315(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: cv. Columbia.
  2. "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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, NOMENCLATURE.
    Strain: cv. Columbia.
  3. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "The Arabidopsis thaliana transcribed genome: the GDR cDNA program."
    Philipps G., Gigot C.
    Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-86.
    Strain: cv. Columbia.
  8. "Molecular characterization of a beta-type proteasome subunit from Arabidopsis thaliana co-expressed at a high level with an alpha-type proteasome subunit early in the cell cycle."
    Genschik P., Jamet E., Phillips G., Parmentier Y., Gigot C., Fleck J.
    Plant J. 6:537-546(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: cv. Columbia.
    Tissue: Leaf.
  9. "The 20S proteasome gene family in Arabidopsis thaliana."
    Parmentier Y., Bouchez D., Fleck J., Genschik P.
    FEBS Lett. 416:281-285(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  10. "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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  11. "SKP1-SnRK protein kinase interactions mediate proteasomal binding of a plant SCF ubiquitin ligase."
    Farras R., Ferrando A., Jasik J., Kleinow T., Oekresz L., Tiburcio A., Salchert K., del Pozo C., Schell J., Koncz C.
    EMBO J. 20:2742-2756(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KIN10; KIN11 AND SKP1A/ASK1.
  12. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.
  13. "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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S PROTEASOME COMPLEX, SUBUNIT.

Entry informationi

Entry nameiPSA7A_ARATH
AccessioniPrimary (citable) accession number: P30186
Secondary accession number(s): Q41942, Q8LB36
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: October 29, 2014
This is version 126 of the entry and version 1 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