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Q9SIV2 (PSD2A_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
26S proteasome non-ATPase regulatory subunit 2 homolog A
Alternative name(s):
26S proteasome regulatory subunit RPN1a
Short name=AtRPN1a
26S proteasome regulatory subunit S2 homolog A
Gene names
Name:RPN1A
Ordered Locus Names:At2g20580
ORF Names:F23N11.10
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length891 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins By similarity. Required during embryogenesis (Ref.6). Required for optimal plant growth and stress responses (Ref.7). Required for innate immunity (Ref.10). Ref.6 Ref.7 Ref.10

Subunit structure

Component of the 19S regulatory particule (RP/PA700) base subcomplex 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 RP/PA700 complex is composed of at least 17 different subunits in two subcomplexes, the base and the lid, which form the portions proximal and distal to the 20S proteolytic core, respectively. Ref.1 Ref.9

Subcellular location

Nucleus. Cytoplasm Ref.10.

Tissue specificity

Expressed in stems, leaves, buds, flowers, siliques and developing seeds. Ref.1 Ref.6

Developmental stage

Detected in the floral meristem and primordia of floral organs. During early stages of flower development, expressed in the whole floral meristem, especially in emerging primordia. Later present in developing carpels, particularly in emerging ovule primordia. After fertilization, observed in the embryo and the chalazal endosperm. High levels at the early embryogenesis stages that fade out later. Also present in the developing seed coat, the septum, and the silique wall. In the stamens, detected at high levels in the anthers. Observed in sporogenous cells and then in tetrads of microspores. Ref.6

Induction

By salicylic acid (SA). Ref.10

Disruption phenotype

Embryo lethality due to development arrest at the globular stage with defects in the formation of the embryonic root, the protoderm, and procambium (Ref.6). Increased cell sizes, anthocyanin accumulation, reduced growth rate, reduced fertility, decreased heat shock tolerance, increased oxidative stress tolerance (Ref.7). Mutant displays enhanced susceptibility to the fungal pathogen G. cichoracearum and to virulent and avirulent bacterial Pto DC3000 strains, which indicated defects in basal defense and resistance (R) protein-mediated defense (Ref.10). Ref.6 Ref.7 Ref.10

Sequence similarities

Belongs to the proteasome subunit S2 family.

Contains 7 PC repeats.

Caution

The embryo lethal disruption phenotype (Ref.6) could be confirmed (Ref.7).

Sequence caution

The sequence BAD94334.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 89189126S proteasome non-ATPase regulatory subunit 2 homolog A
PRO_0000399921

Regions

Repeat414 – 44734PC 1
Repeat448 – 48437PC 2
Repeat485 – 51935PC 3
Repeat522 – 55635PC 4
Repeat565 – 59430PC 5
Repeat674 – 70532PC 6
Repeat724 – 73916PC 7

Amino acid modifications

Modified residue2191N-acetylthreonine Ref.9
Cross-link218Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9

Sequences

Sequence LengthMass (Da)Tools
Q9SIV2 [UniParc].

Last modified June 1, 2002. Version 2.
Checksum: 68C0B94F83F21955

FASTA89198,144
        10         20         30         40         50         60 
MAPTQDPNSV GGGAKKDEAT LKVPSKDPKK KDEKKDEDLS EEDLELKQNL ELYVERVQDP 

        70         80         90        100        110        120 
NPELQKAALE SMRQEIRAST SSMTSVPKPL KFLRPHYGTL KAFHETMADS DLKKYLSDIL 

       130        140        150        160        170        180 
SVLALTMSAD GERESLRFRL IGTEGDIGSW GHEYVRNLAG EIAQEYTKRQ SEEASIDDLM 

       190        200        210        220        230        240 
ELVQQIVAFH MKHNAETEAV DLLMDVEDLD LLLEHVDKTN FKRTCNYLTS AARYLPGPDD 

       250        260        270        280        290        300 
MLVLDISYMI YMKFEEYPNA LQIALFLDNT QYVKQVFTSC TDLLKKKQFC YMIARHGITF 

       310        320        330        340        350        360 
ELDDEMVADD DDREALQDIV NNTKLSEGYL TLARDIEVME AKTPEDIYKA HLLDGRASSG 

       370        380        390        400        410        420 
ASVDSARQNL AATFVNAFVN AGFGQDKLMT VPSDSTTGSS GNWLFKNKEH GKTSAAASLG 

       430        440        450        460        470        480 
MIQLWDVDSG LSQLDKYFHS NDNPIIAGAL LGVGIVNCGI KNDCDPALAL LGDYIDKEDS 

       490        500        510        520        530        540 
SVRIGAIMGL GISYAGSQND QIRNKLSPIL NDAKAPLDVI AFASLSLGMI YVGSCNEEVA 

       550        560        570        580        590        600 
QSIIFALMDR SEAELGDALT RFLPLGLGLL YLGKQESVEA TAEVSKTFNE KIRKYCDMTL 

       610        620        630        640        650        660 
LSCAYAGTGN VLKVQDLLAQ CGEHLEKGDI HQGPAVLGLA MVAMSEELGV DMEIRSLERM 

       670        680        690        700        710        720 
LQYGEQNIRR AVPLALGLLC ISNPKVTVMD TLSRLSHDTD SEVAMSAIIS LGLIGAGTNN 

       730        740        750        760        770        780 
ARIAGMLRNL SSYYYKDMSL LFCVRIAQGL VHMGKGLLTL SPFHSERFLL SPTALAGIVT 

       790        800        810        820        830        840 
LLHACLDMKP IILGKYHYVL YFLVLAMQPR MMLTVDENLK PLSVPVRVGQ AVDVVGQAGR 

       850        860        870        880        890 
PKTITGFQTH STPVLLAAGE RAELATDKYI PLSPILEGFI ILKENPDYRE E 

« Hide

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana."
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. expand/collapse author list , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.
Nature 402:761-768(1999) [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. expand/collapse author list , 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]"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. expand/collapse author list , 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 643-891.
Strain: cv. Columbia.
[6]"The RPN1 subunit of the 26S proteasome in Arabidopsis is essential for embryogenesis."
Brukhin V., Gheyselinck J., Gagliardini V., Genschik P., Grossniklaus U.
Plant Cell 17:2723-2737(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[7]"The Arabidopsis 26S proteasome subunit RPN1a is required for optimal plant growth and stress responses."
Wang S., Kurepa J., Smalle J.A.
Plant Cell Physiol. 50:1721-1725(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[8]"Tandem affinity purification and mass spectrometric analysis of ubiquitylated proteins in Arabidopsis."
Saracco S.A., Hansson M., Scalf M., Walker J.M., Smith L.M., Vierstra R.D.
Plant J. 59:344-358(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS].
[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 THR-219, UBIQUITINATION AT LYS-218.
[10]"RPN1a, a 26S proteasome subunit, is required for innate immunity in Arabidopsis."
Yao C., Wu Y., Nie H., Tang D.
Plant J. 71:1015-1028(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INDUCTION BY SALICYLIC ACID.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY230828 mRNA. Translation: AAP86655.1.
AC007048 Genomic DNA. Translation: AAD21708.2.
CP002685 Genomic DNA. Translation: AEC07032.1.
AF360216 mRNA. Translation: AAK25926.1.
AY040061 mRNA. Translation: AAK64119.1.
AK220903 mRNA. Translation: BAD94334.1. Different initiation.
PIRA84591.
RefSeqNP_565477.1. NM_127618.3.
UniGeneAt.22879.

3D structure databases

ProteinModelPortalQ9SIV2.
SMRQ9SIV2. Positions 50-891.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid1933. 28 interactions.
IntActQ9SIV2. 28 interactions.

Proteomic databases

PaxDbQ9SIV2.
PRIDEQ9SIV2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT2G20580.1; AT2G20580.1; AT2G20580.
GeneID816580.
KEGGath:AT2G20580.

Organism-specific databases

TAIRAT2G20580.

Phylogenomic databases

eggNOGCOG5110.
HOGENOMHOG000176022.
InParanoidQ9SIV2.
KOK03028.
OMAIAQGLTH.
PhylomeDBQ9SIV2.

Gene expression databases

GenevestigatorQ9SIV2.

Family and domain databases

Gene3D1.25.10.10. 3 hits.
InterProIPR016643. 26S_Psome_Rpn1.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR002015. Proteasome/cyclosome_rpt.
[Graphical view]
PANTHERPTHR10943:SF1. PTHR10943:SF1. 1 hit.
PfamPF01851. PC_rep. 2 hits.
[Graphical view]
PIRSFPIRSF015965. 26S_Psome_Rpn1. 1 hit.
SUPFAMSSF48371. SSF48371. 4 hits.
ProtoNetSearch...

Other

PROQ9SIV2.

Entry information

Entry namePSD2A_ARATH
AccessionPrimary (citable) accession number: Q9SIV2
Secondary accession number(s): Q56ZR0, Q9C5J1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2010
Last sequence update: June 1, 2002
Last modified: June 11, 2014
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names