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Protein

Glutathione gamma-glutamylcysteinyltransferase 2

Gene

PCS2

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

Functioni

Involved in the synthesis of phytochelatins (PC) and homophytochelatins (hPC), the heavy-metal-binding peptides of plants.3 Publications

Catalytic activityi

Glutathione + (Glu(-Cys))(n)-Gly = Gly + (Glu(-Cys))(n+1)-Gly.PROSITE-ProRule annotation

Enzyme regulationi

Requires cadmium for activity. Also activated in heterologous system by AsO43- ions, but not by Cu2+, Zn2+, Mn2+ or Ni2+ ions.1 Publication

GO - Molecular functioni

  1. glutathione gamma-glutamylcysteinyltransferase activity Source: TAIR
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. phytochelatin biosynthetic process Source: TAIR
  2. response to metal ion Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Ligandi

Cadmium, Metal-binding

Enzyme and pathway databases

BioCyciARA:AT1G03980-MONOMER.

Protein family/group databases

MEROPSiC83.A01.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione gamma-glutamylcysteinyltransferase 2 (EC:2.3.2.15)
Alternative name(s):
Phytochelatin synthase 2
Short name:
AtPCS2
Gene namesi
Name:PCS2
Ordered Locus Names:At1g03980
ORF Names:F21M11.9
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G03980.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 452452Glutathione gamma-glutamylcysteinyltransferase 2PRO_0000287211Add
BLAST

Proteomic databases

PRIDEiQ9ZWB7.

Expressioni

Tissue specificityi

Expressed in shoots, roots, leaves, stems and flowers.1 Publication

Inductioni

Not induced by cadmium or other heavy metal stress.

Gene expression databases

GenevestigatoriQ9ZWB7.

Interactioni

Protein-protein interaction databases

STRINGi3702.AT1G03980.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ9ZWB7.
SMRiQ9ZWB7. Positions 11-216.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 220220Peptidase C83PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili287 – 31529Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the phytochelatin synthase family.PROSITE-ProRule annotation
Contains 1 peptidase C83 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG76926.
HOGENOMiHOG000241441.
InParanoidiQ9ZWB7.
KOiK05941.
OMAiCEPLEIV.
PhylomeDBiQ9ZWB7.

Family and domain databases

InterProiIPR007719. Phytochelatin_synthase.
IPR015407. Phytochelatin_synthase_C.
[Graphical view]
PfamiPF05023. Phytochelatin. 1 hit.
PF09328. Phytochelatin_C. 2 hits.
[Graphical view]
PROSITEiPS51443. PCS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9ZWB7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSMASLYRRS LSPPAIDFAS FEGKQIFNEA LQKGTMEGFF GLISYFQTQS
60 70 80 90 100
EPAFCGLASL SMVLNSLSID PGRKWKGPWR WFDESMLECC EPLEIVKDKG
110 120 130 140 150
ISFGKVVCLA HSSGAKVEAF RTNQSTIDDF RKYVVKCSTS DNCHMISTYH
160 170 180 190 200
RQVLKQTGTG HFSPIGGYNA ERDMALILDV ARFKYPPHWV PLKLLWDAMD
210 220 230 240 250
SIDQSTGRRR GFMLISRPHR EPGLLYTLSC KDESWISIAK YLKEDVPRLV
260 270 280 290 300
SSQHVDTIER ILYVVFKSLP ANFNQFIKWM AEIRRTEDVN QNLSSEEKSR
310 320 330 340 350
LKLKQELLKQ VQETKLFKHV DKFLSSVYED NLPYVAAKVY CDGDEILSGY
360 370 380 390 400
ESDESCCKET CVKCIKGLGE EKVTVVAYPS GNDVFTALLL ALPPQTWSGI
410 420 430 440 450
KDQSLLQEMK QLISMVSHPT LLQQEVLHLR RQLEMLKRCQ ENKEDEELSA

PA
Length:452
Mass (Da):51,551
Last modified:May 1, 1999 - v1
Checksum:i8E8FD573E9C00A76
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY044049 mRNA. Translation: AAK94671.1.
AC003027 Genomic DNA. Translation: AAD10671.1.
CP002684 Genomic DNA. Translation: AEE27641.1.
BT029214 mRNA. Translation: ABJ17149.1.
PIRiG86170.
RefSeqiNP_171894.1. NM_100279.4.
UniGeneiAt.26664.
At.71149.

Genome annotation databases

EnsemblPlantsiAT1G03980.1; AT1G03980.1; AT1G03980.
GeneIDi839354.
KEGGiath:AT1G03980.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY044049 mRNA. Translation: AAK94671.1.
AC003027 Genomic DNA. Translation: AAD10671.1.
CP002684 Genomic DNA. Translation: AEE27641.1.
BT029214 mRNA. Translation: ABJ17149.1.
PIRiG86170.
RefSeqiNP_171894.1. NM_100279.4.
UniGeneiAt.26664.
At.71149.

3D structure databases

ProteinModelPortaliQ9ZWB7.
SMRiQ9ZWB7. Positions 11-216.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT1G03980.1-P.

Protein family/group databases

MEROPSiC83.A01.

Proteomic databases

PRIDEiQ9ZWB7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G03980.1; AT1G03980.1; AT1G03980.
GeneIDi839354.
KEGGiath:AT1G03980.

Organism-specific databases

TAIRiAT1G03980.

Phylogenomic databases

eggNOGiNOG76926.
HOGENOMiHOG000241441.
InParanoidiQ9ZWB7.
KOiK05941.
OMAiCEPLEIV.
PhylomeDBiQ9ZWB7.

Enzyme and pathway databases

BioCyciARA:AT1G03980-MONOMER.

Gene expression databases

GenevestigatoriQ9ZWB7.

Family and domain databases

InterProiIPR007719. Phytochelatin_synthase.
IPR015407. Phytochelatin_synthase_C.
[Graphical view]
PfamiPF05023. Phytochelatin. 1 hit.
PF09328. Phytochelatin_C. 2 hits.
[Graphical view]
PROSITEiPS51443. PCS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Arabidopsis thaliana expresses a second functional phytochelatin synthase."
    Cazale A.-C., Clemens S.
    FEBS Lett. 507:215-219(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, LACK OF INDUCTION BY CADMIUM, TISSUE SPECIFICITY.
    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. "Arabidopsis ORF clones."
    Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Expression of Arabidopsis phytochelatin synthase 2 is too low to complement an AtPCS1-defective Cad1-3 mutant."
    Lee S., Kang B.S.
    Mol. Cells 19:81-87(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Function of phytochelatin synthase in catabolism of glutathione-conjugates."
    Blum R., Beck A., Korte A., Stengel A., Letzel T., Lendzian K., Grill E.
    Plant J. 49:740-749(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiPCS2_ARATH
AccessioniPrimary (citable) accession number: Q9ZWB7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 1, 1999
Last modified: January 7, 2015
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Expression of PCS2 is too low to complement a PCS1-defective mutant.

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

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 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.