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Protein

Cysteine proteinase RD19a

Gene

RD19A

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei159 – 1591By similarity
Active sitei302 – 3021By similarity
Active sitei329 – 3291By similarity

GO - Molecular functioni

GO - Biological processi

  • defense response to bacterium Source: TAIR
  • proteolysis involved in cellular protein catabolic process Source: GO_Central
  • response to osmotic stress Source: TAIR
  • response to salt stress Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Enzyme and pathway databases

BioCyciARA:AT4G39090-MONOMER.
ReactomeiR-ATH-2132295. MHC class II antigen presentation.

Protein family/group databases

MEROPSiC01.022.

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine proteinase RD19a (EC:3.4.22.-)
Short name:
RD19
Gene namesi
Name:RD19A
Ordered Locus Names:At4g39090
ORF Names:F19H22.190
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G39090.

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: GO_Central
  • lysosome Source: GO_Central
  • nucleus Source: TAIR
  • vacuole Source: TAIR
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Propeptidei24 – 134111Activation peptideSequence analysisPRO_0000026455Add
BLAST
Chaini135 – 368234Cysteine proteinase RD19aPRO_0000026456Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi156 ↔ 206By similarity
Disulfide bondi194 ↔ 240By similarity
Glycosylationi253 – 2531N-linked (GlcNAc...)Sequence analysis
Disulfide bondi296 ↔ 350By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP43296.
PRIDEiP43296.

Expressioni

Inductioni

By high salt conditions.

Gene expression databases

ExpressionAtlasiP43296. baseline and differential.
GenevisibleiP43296. AT.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT4G39090.1.

Structurei

3D structure databases

ProteinModelPortaliP43296.
SMRiP43296. Positions 48-362.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C1 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1542. Eukaryota.
COG4870. LUCA.
HOGENOMiHOG000230774.
InParanoidiP43296.
KOiK01373.
OMAiLPINAFR.
PhylomeDBiP43296.

Family and domain databases

InterProiIPR025661. 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.
PfamiPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00848. 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.

P43296-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDRLKLYFSV FVLSFFIVSV SSSDVNDGDD LVIRQVVGGA EPQVLTSEDH
60 70 80 90 100
FSLFKRKFGK VYASNEEHDY RFSVFKANLR RARRHQKLDP SATHGVTQFS
110 120 130 140 150
DLTRSEFRKK HLGVRSGFKL PKDANKAPIL PTENLPEDFD WRDHGAVTPV
160 170 180 190 200
KNQGSCGSCW SFSATGALEG ANFLATGKLV SLSEQQLVDC DHECDPEEAD
210 220 230 240 250
SCDSGCNGGL MNSAFEYTLK TGGLMKEEDY PYTGKDGKTC KLDKSKIVAS
260 270 280 290 300
VSNFSVISID EEQIAANLVK NGPLAVAINA GYMQTYIGGV SCPYICTRRL
310 320 330 340 350
NHGVLLVGYG AAGYAPARFK EKPYWIIKNS WGETWGENGF YKICKGRNIC
360
GVDSMVSTVA ATVSTTAH
Length:368
Mass (Da):40,419
Last modified:November 1, 1995 - v1
Checksum:i9D64CF35E07F519D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13042 Genomic DNA. Translation: BAA02373.1.
AL035679 Genomic DNA. Translation: CAB38829.1.
AL161594 Genomic DNA. Translation: CAB80572.1.
CP002687 Genomic DNA. Translation: AEE87016.1.
AY080598 mRNA. Translation: AAL85009.1.
AY133844 mRNA. Translation: AAM91778.1.
PIRiJN0718.
RefSeqiNP_568052.1. NM_120069.4.
UniGeneiAt.2850.
At.74924.

Genome annotation databases

EnsemblPlantsiAT4G39090.1; AT4G39090.1; AT4G39090.
GeneIDi830064.
GrameneiAT4G39090.1; AT4G39090.1; AT4G39090.
KEGGiath:AT4G39090.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13042 Genomic DNA. Translation: BAA02373.1.
AL035679 Genomic DNA. Translation: CAB38829.1.
AL161594 Genomic DNA. Translation: CAB80572.1.
CP002687 Genomic DNA. Translation: AEE87016.1.
AY080598 mRNA. Translation: AAL85009.1.
AY133844 mRNA. Translation: AAM91778.1.
PIRiJN0718.
RefSeqiNP_568052.1. NM_120069.4.
UniGeneiAt.2850.
At.74924.

3D structure databases

ProteinModelPortaliP43296.
SMRiP43296. Positions 48-362.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT4G39090.1.

Protein family/group databases

MEROPSiC01.022.

Proteomic databases

PaxDbiP43296.
PRIDEiP43296.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G39090.1; AT4G39090.1; AT4G39090.
GeneIDi830064.
GrameneiAT4G39090.1; AT4G39090.1; AT4G39090.
KEGGiath:AT4G39090.

Organism-specific databases

TAIRiAT4G39090.

Phylogenomic databases

eggNOGiKOG1542. Eukaryota.
COG4870. LUCA.
HOGENOMiHOG000230774.
InParanoidiP43296.
KOiK01373.
OMAiLPINAFR.
PhylomeDBiP43296.

Enzyme and pathway databases

BioCyciARA:AT4G39090-MONOMER.
ReactomeiR-ATH-2132295. MHC class II antigen presentation.

Miscellaneous databases

PROiP43296.

Gene expression databases

ExpressionAtlasiP43296. baseline and differential.
GenevisibleiP43296. AT.

Family and domain databases

InterProiIPR025661. 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.
PfamiPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSiPR00705. PAPAIN.
SMARTiSM00848. 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].
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(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.
    , 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.

Entry informationi

Entry nameiRD19A_ARATH
AccessioniPrimary (citable) accession number: P43296
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 17, 2016
This is version 119 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.