Skip Header

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

O81149

- PSA5A_ARATH

UniProt

O81149 - PSA5A_ARATH

(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 alpha type-5-A

Gene

PAE1

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.

Catalytic activityi

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

GO - Molecular functioni

  1. ribonuclease activity Source: TAIR
  2. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. response to cadmium ion Source: TAIR
  2. RNA phosphodiester bond hydrolysis Source: GOC
  3. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

BioCyciARA:AT1G53850-MONOMER.
ARA:GQT-2342-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_240263. Ubiquitin-dependent degradation of Cyclin D1.
REACT_241531. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_244054. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_252436. CDK-mediated phosphorylation and removal of Cdc6.
REACT_94347. APC/C:Cdc20 mediated degradation of Securin.

Protein family/group databases

MEROPSiT01.975.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit alpha type-5-A (EC:3.4.25.1)
Alternative name(s):
20S proteasome alpha subunit E-1
Gene namesi
Name:PAE1
Ordered Locus Names:At1g53850
ORF Names:T18A20.8
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G53850.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: TAIR
  2. cytosol Source: TAIR
  3. cytosolic ribosome Source: TAIR
  4. nucleus Source: TAIR
  5. plasma membrane Source: TAIR
  6. proteasome complex Source: TAIR
  7. proteasome core complex, alpha-subunit complex Source: InterPro
  8. vacuolar membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 237237Proteasome subunit alpha type-5-APRO_0000124124Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Cross-linki66 – 66Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiO81149.
PRIDEiO81149.

Expressioni

Gene expression databases

GenevestigatoriO81149.

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

IntActiO81149. 2 interactions.
STRINGi3702.AT1G53850.1-P.

Structurei

3D structure databases

ProteinModelPortaliO81149.
SMRiO81149. Positions 8-234.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1A family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000091085.
InParanoidiO81149.
KOiK02729.
OMAiHYDEGMD.
PhylomeDBiO81149.

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.

O81149-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFLTRTEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGV KTKEGVVLAV
60 70 80 90 100
EKRITSPLLE PSSVEKIMEI DDHIGCAMSG LIADARTLVE HARVETQNHR
110 120 130 140 150
FSYGEPMTVE STTQALCDLA LRFGEGEEES MSRPFGVSLL IAGHDENGPS
160 170 180 190 200
LYYTDPSGTF WQCNAKAIGS GSEGADSSLQ EQFNKDLSLQ EAETIAVSIL
210 220 230
KQVMEEKVTP NNVDIAKVAP AYHLYTPQEV EAVIARL
Length:237
Mass (Da):25,947
Last modified:November 1, 1998 - v1
Checksum:iB17DED1D6E2C9680
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti121 – 1211L → F in BAD94476. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF043524 mRNA. Translation: AAC32060.1.
AC009324 Genomic DNA. Translation: AAF02858.1.
CP002684 Genomic DNA. Translation: AEE33009.1.
CP002684 Genomic DNA. Translation: AEE33010.1.
AY072371 mRNA. Translation: AAL62363.1.
AY114616 mRNA. Translation: AAM47935.1.
AY086045 mRNA. Translation: AAM63255.1.
AK220949 mRNA. Translation: BAD94476.1.
PIRiT51972.
RefSeqiNP_001077717.1. NM_001084248.1.
NP_175788.1. NM_104262.2.
UniGeneiAt.23242.

Genome annotation databases

EnsemblPlantsiAT1G53850.1; AT1G53850.1; AT1G53850.
AT1G53850.2; AT1G53850.2; AT1G53850.
GeneIDi841822.
KEGGiath:AT1G53850.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF043524 mRNA. Translation: AAC32060.1 .
AC009324 Genomic DNA. Translation: AAF02858.1 .
CP002684 Genomic DNA. Translation: AEE33009.1 .
CP002684 Genomic DNA. Translation: AEE33010.1 .
AY072371 mRNA. Translation: AAL62363.1 .
AY114616 mRNA. Translation: AAM47935.1 .
AY086045 mRNA. Translation: AAM63255.1 .
AK220949 mRNA. Translation: BAD94476.1 .
PIRi T51972.
RefSeqi NP_001077717.1. NM_001084248.1.
NP_175788.1. NM_104262.2.
UniGenei At.23242.

3D structure databases

ProteinModelPortali O81149.
SMRi O81149. Positions 8-234.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O81149. 2 interactions.
STRINGi 3702.AT1G53850.1-P.

Protein family/group databases

MEROPSi T01.975.

Proteomic databases

PaxDbi O81149.
PRIDEi O81149.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G53850.1 ; AT1G53850.1 ; AT1G53850 .
AT1G53850.2 ; AT1G53850.2 ; AT1G53850 .
GeneIDi 841822.
KEGGi ath:AT1G53850.

Organism-specific databases

TAIRi AT1G53850.

Phylogenomic databases

eggNOGi COG0638.
HOGENOMi HOG000091085.
InParanoidi O81149.
KOi K02729.
OMAi HYDEGMD.
PhylomeDBi O81149.

Enzyme and pathway databases

BioCyci ARA:AT1G53850-MONOMER.
ARA:GQT-2342-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_240263. Ubiquitin-dependent degradation of Cyclin D1.
REACT_241531. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_244054. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_252436. CDK-mediated phosphorylation and removal of Cdc6.
REACT_94347. APC/C:Cdc20 mediated degradation of Securin.

Gene expression databases

Genevestigatori O81149.

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. "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.
  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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "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].
  6. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 121-237.
    Strain: cv. Columbia.
  7. "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.
  8. "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.
  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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, CHARACTERIZATION OF THE 26S PROTEASOME COMPLEX, SUBUNIT, ACETYLATION AT MET-1, UBIQUITINATION AT LYS-66.

Entry informationi

Entry nameiPSA5A_ARATH
AccessioniPrimary (citable) accession number: O81149
Secondary accession number(s): Q56ZL5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: November 1, 1998
Last modified: November 26, 2014
This is version 116 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