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Protein

Cysteine proteinase RD21A

Gene

RD21A

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cysteine protease that plays a role in immunity, senescence, and biotic and abiotic stresses (Probable). Involved in immunity against the necrotrophic fungal pathogen Botrytis cinerea (PubMed:22238602). Involved in elicitor-stimulated programmed cell death (PCD). During infection by the necrotrophic fungal pathogen Botrytis cinerea, functions as PCD-promoting protease that is released from the ER body or vacuole to the cytoplasm (PubMed:23398119). Accumulates in endoplasmic reticulum-derived bodies in epidermal cells and may participate in cell death in stressed or injured cells (PubMed:11577182). Involved in water stress-induced cell death through its protease activity that is released to the cytoplasm after vacuolar collapse (PubMed:26884487). Possesses protease activity in vitro and is involved in cell death in the transmitting tract and septum epidermis during flower development (PubMed:26160583). Possesses peptide ligase activity. Can ligate peptides to unmodified N-termini of acceptor proteins. Probably ligates through a thioester intermediate (PubMed:18660805).1 Publication6 Publications

Enzyme regulationi

Inhibited by the cysteine protease inhibitor E-64.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei161 – 1611PROSITE-ProRule annotation1 Publication
Active sitei297 – 2971PROSITE-ProRule annotation1 Publication
Active sitei317 – 3171PROSITE-ProRule annotation1 Publication

GO - Molecular functioni

  • cysteine-type endopeptidase activity Source: GO_Central
  • cysteine-type peptidase activity Source: TAIR
  • peptidase activity Source: TAIR

GO - Biological processi

  • defense response to fungus Source: TAIR
  • proteolysis Source: TAIR
  • proteolysis involved in cellular protein catabolic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BioCyciARA:AT1G47128-MONOMER.

Protein family/group databases

MEROPSiC01.064.

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine proteinase RD21ACurated (EC:3.4.22.-Curated)
Alternative name(s):
Protein RESPONSIVE TO DEHYDRATION 211 Publication
Short name:
RD211 Publication
Gene namesi
Name:RD21A1 Publication
Ordered Locus Names:At1g47128
ORF Names:F2G19.31
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G47128.

Subcellular locationi

GO - Cellular componenti

  • apoplast Source: TAIR
  • chloroplast Source: TAIR
  • cytoplasmic mRNA processing body Source: TAIR
  • cytoplasmic stress granule Source: TAIR
  • extracellular space Source: GO_Central
  • lysosome Source: GO_Central
  • plasmodesma Source: TAIR
  • vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Vacuole

Pathology & Biotechi

Disruption phenotypei

No visible phenotype under normal growth conditions (PubMed:22238602, PubMed:22396764). Mutant plants show increased susceptibility to infection by the necrotrophic fungal pathogen Botrytis cinerea (PubMed:22238602).2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi161 – 1611C → A: Loss of protease activity. 1 Publication
Mutagenesisi297 – 2971H → A: Loss of protease activity. 1 Publication
Mutagenesisi317 – 3171N → A: Reduces protease activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Propeptidei22 – 136115Activation peptide1 PublicationPRO_0000026457Add
BLAST
Chaini137 – 352216Cysteine proteinase RD21APRO_0000026458Add
BLAST
Propeptidei353 – 462110Removed in mature form1 PublicationPRO_0000046018Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi90 – 901N-linked (GlcNAc...)PROSITE-ProRule annotation
Disulfide bondi158 ↔ 200By similarity
Disulfide bondi192 ↔ 233By similarity
Disulfide bondi291 ↔ 342By similarity
Disulfide bondi375 ↔ 387By similarity
Disulfide bondi381 ↔ 402By similarity
Glycosylationi414 – 4141N-linked (GlcNAc...)PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP43297.
PRIDEiP43297.

Expressioni

Inductioni

By high salt conditions and drought stress.1 Publication

Gene expression databases

GenevisibleiP43297. AT.

Interactioni

Subunit structurei

Interacts with SERPIN1 (PubMed:23398119, PubMed:20181955). Interacts with PRN2 (PubMed:24947605). Interacts with WSCP (PubMed:26160583, PubMed:26016527).5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PDIL1-1Q9XI014EBI-1993101,EBI-449394

Protein-protein interaction databases

BioGridi26347. 11 interactions.
IntActiP43297. 1 interaction.
STRINGi3702.AT1G47128.1.

Structurei

3D structure databases

ProteinModelPortaliP43297.
SMRiP43297. Positions 42-357, 375-422.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
KOG4296. Eukaryota.
COG4870. LUCA.
HOGENOMiHOG000230773.
InParanoidiP43297.
OMAiMSIVVIT.
PhylomeDBiP43297.

Family and domain databases

InterProiIPR000118. Granulin.
IPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF00396. Granulin. 1 hit.
PF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00277. GRAN. 1 hit.
SM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P43297-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGFLKPTMAI LFLAMVAVSS AVDMSIISYD EKHGVSTTGG RSEAEVMSIY
60 70 80 90 100
EAWLVKHGKA QSQNSLVEKD RRFEIFKDNL RFVDEHNEKN LSYRLGLTRF
110 120 130 140 150
ADLTNDEYRS KYLGAKMEKK GERRTSLRYE ARVGDELPES IDWRKKGAVA
160 170 180 190 200
EVKDQGGCGS CWAFSTIGAV EGINQIVTGD LITLSEQELV DCDTSYNEGC
210 220 230 240 250
NGGLMDYAFE FIIKNGGIDT DKDYPYKGVD GTCDQIRKNA KVVTIDSYED
260 270 280 290 300
VPTYSEESLK KAVAHQPISI AIEAGGRAFQ LYDSGIFDGS CGTQLDHGVV
310 320 330 340 350
AVGYGTENGK DYWIVRNSWG KSWGESGYLR MARNIASSSG KCGIAIEPSY
360 370 380 390 400
PIKNGENPPN PGPSPPSPIK PPTQCDSYYT CPESNTCCCL FEYGKYCFAW
410 420 430 440 450
GCCPLEAATC CDDNYSCCPH EYPVCDLDQG TCLLSKNSPF SVKALKRKPA
460
TPFWSQGRKN IA
Length:462
Mass (Da):50,966
Last modified:November 1, 1995 - v1
Checksum:i4C59955CCB95AA58
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13043 Genomic DNA. Translation: BAA02374.1.
AC083835 Genomic DNA. Translation: AAG50628.1.
CP002684 Genomic DNA. Translation: AEE32135.1.
AY072130 mRNA. Translation: AAL59952.1.
AY133781 mRNA. Translation: AAM91715.1.
PIRiJN0719.
RefSeqiNP_564497.1. NM_103612.2.
UniGeneiAt.43549.
At.47599.
At.71705.

Genome annotation databases

EnsemblPlantsiAT1G47128.1; AT1G47128.1; AT1G47128.
GeneIDi841122.
GrameneiAT1G47128.1; AT1G47128.1; AT1G47128.
KEGGiath:AT1G47128.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13043 Genomic DNA. Translation: BAA02374.1.
AC083835 Genomic DNA. Translation: AAG50628.1.
CP002684 Genomic DNA. Translation: AEE32135.1.
AY072130 mRNA. Translation: AAL59952.1.
AY133781 mRNA. Translation: AAM91715.1.
PIRiJN0719.
RefSeqiNP_564497.1. NM_103612.2.
UniGeneiAt.43549.
At.47599.
At.71705.

3D structure databases

ProteinModelPortaliP43297.
SMRiP43297. Positions 42-357, 375-422.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi26347. 11 interactions.
IntActiP43297. 1 interaction.
STRINGi3702.AT1G47128.1.

Protein family/group databases

MEROPSiC01.064.

Proteomic databases

PaxDbiP43297.
PRIDEiP43297.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G47128.1; AT1G47128.1; AT1G47128.
GeneIDi841122.
GrameneiAT1G47128.1; AT1G47128.1; AT1G47128.
KEGGiath:AT1G47128.

Organism-specific databases

TAIRiAT1G47128.

Phylogenomic databases

eggNOGiKOG1543. Eukaryota.
KOG4296. Eukaryota.
COG4870. LUCA.
HOGENOMiHOG000230773.
InParanoidiP43297.
OMAiMSIVVIT.
PhylomeDBiP43297.

Enzyme and pathway databases

BioCyciARA:AT1G47128-MONOMER.

Miscellaneous databases

PROiP43297.

Gene expression databases

GenevisibleiP43297. AT.

Family and domain databases

InterProiIPR000118. Granulin.
IPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERiPTHR12411. PTHR12411. 1 hit.
PfamiPF00396. Granulin. 1 hit.
PF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00277. GRAN. 1 hit.
SM00848. Inhibitor_I29. 1 hit.
SM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEiPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and expression of two genes that encode distinct drought-inducible cysteine proteinases in Arabidopsis thaliana."
    Koizumi M., Yamaguchi-Shinozaki K., Tsuji H., Shinozaki K.
    Gene 129:175-182(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
    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. "A proteinase-storing body that prepares for cell death or stresses in the epidermal cells of Arabidopsis."
    Hayashi Y., Yamada K., Shimada T., Matsushima R., Nishizawa N.K., Nishimura M., Hara-Nishimura I.
    Plant Cell Physiol. 42:894-899(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. "A slow maturation of a cysteine protease with a granulin domain in the vacuoles of senescing Arabidopsis leaves."
    Yamada K., Matsushima R., Nishimura M., Hara-Nishimura I.
    Plant Physiol. 127:1626-1634(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  7. "Beta-lactone probes identify a papain-like peptide ligase in Arabidopsis thaliana."
    Wang Z., Gu C., Colby T., Shindo T., Balamurugan R., Waldmann H., Kaiser M., van der Hoorn R.A.
    Nat. Chem. Biol. 4:557-563(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION.
  8. "Arabidopsis AtSerpin1, crystal structure and in vivo interaction with its target protease RESPONSIVE TO DESICCATION-21 (RD21)."
    Lampl N., Budai-Hadrian O., Davydov O., Joss T.V., Harrop S.J., Curmi P.M., Roberts T.H., Fluhr R.
    J. Biol. Chem. 285:13550-13560(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SERPIN1.
  9. "A role in immunity for Arabidopsis cysteine protease RD21, the ortholog of the tomato immune protease C14."
    Shindo T., Misas-Villamil J.C., Hoerger A.C., Song J., van der Hoorn R.A.
    PLoS ONE 7:E29317-E29317(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  10. "Post-translational regulation and trafficking of the granulin-containing protease RD21 of Arabidopsis thaliana."
    Gu C., Shabab M., Strasser R., Wolters P.J., Shindo T., Niemer M., Kaschani F., Mach L., van der Hoorn R.A.
    PLoS ONE 7:E32422-E32422(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, ACTIVE SITE, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, MUTAGENESIS OF CYS-161; HIS-297 AND ASN-317, DISRUPTION PHENOTYPE.
  11. "Set-point control of RD21 protease activity by AtSerpin1 controls cell death in Arabidopsis."
    Lampl N., Alkan N., Davydov O., Fluhr R.
    Plant J. 74:498-510(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SERPIN1, SUBCELLULAR LOCATION.
  12. "PIRIN2 stabilizes cysteine protease XCP2 and increases susceptibility to the vascular pathogen Ralstonia solanacearum in Arabidopsis."
    Zhang B., Tremousaygue D., Denance N., van Esse H.P., Hoerger A.C., Dabos P., Goffner D., Thomma B.P., van der Hoorn R.A., Tuominen H.
    Plant J. 79:1009-1019(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRN2.
  13. "A Kunitz-type protease inhibitor regulates programmed cell death during flower development in Arabidopsis thaliana."
    Boex-Fontvieille E., Rustgi S., Reinbothe S., Reinbothe C.
    J. Exp. Bot. 66:6119-6135(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH WSCP.
  14. "Water-soluble chlorophyll protein is involved in herbivore resistance activation during greening of Arabidopsis thaliana."
    Boex-Fontvieille E., Rustgi S., von Wettstein D., Reinbothe S., Reinbothe C.
    Proc. Natl. Acad. Sci. U.S.A. 112:7303-7308(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WSCP.
  15. "Singlet oxygen induced membrane disruption and serpin-protease balance in vacuolar driven cell death in Arabidopsis thaliana."
    Koh E., Carmieli R., Mor A., Fluhr R.
    Plant Physiol. 0:0-0(2016) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiRD21A_ARATH
AccessioniPrimary (citable) accession number: P43297
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 8, 2016
This is version 128 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

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 one 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.