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Q9ZWB7 (PCS2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glutathione gamma-glutamylcysteinyltransferase 2

EC=2.3.2.15
Alternative name(s):
Phytochelatin synthase 2
Short name=AtPCS2
Gene names
Name:PCS2
Ordered Locus Names:At1g03980
ORF Names:F21M11.9
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length452 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in the synthesis of phytochelatins (PC) and homophytochelatins (hPC), the heavy-metal-binding peptides of plants. Ref.1 Ref.5 Ref.6

Catalytic activity

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

Enzyme regulation

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

Tissue specificity

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

Induction

Not induced by cadmium or other heavy metal stress. Ref.1

Miscellaneous

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

Sequence similarities

Belongs to the phytochelatin synthase family.

Contains 1 peptidase C83 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 452452Glutathione gamma-glutamylcysteinyltransferase 2
PRO_0000287211

Regions

Domain1 – 220220Peptidase C83
Coiled coil287 – 31529 Potential

Sequences

Sequence LengthMass (Da)Tools
Q9ZWB7 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 8E8FD573E9C00A76

FASTA45251,551
        10         20         30         40         50         60 
MSMASLYRRS LSPPAIDFAS FEGKQIFNEA LQKGTMEGFF GLISYFQTQS EPAFCGLASL 

        70         80         90        100        110        120 
SMVLNSLSID PGRKWKGPWR WFDESMLECC EPLEIVKDKG ISFGKVVCLA HSSGAKVEAF 

       130        140        150        160        170        180 
RTNQSTIDDF RKYVVKCSTS DNCHMISTYH RQVLKQTGTG HFSPIGGYNA ERDMALILDV 

       190        200        210        220        230        240 
ARFKYPPHWV PLKLLWDAMD SIDQSTGRRR GFMLISRPHR EPGLLYTLSC KDESWISIAK 

       250        260        270        280        290        300 
YLKEDVPRLV SSQHVDTIER ILYVVFKSLP ANFNQFIKWM AEIRRTEDVN QNLSSEEKSR 

       310        320        330        340        350        360 
LKLKQELLKQ VQETKLFKHV DKFLSSVYED NLPYVAAKVY CDGDEILSGY ESDESCCKET 

       370        380        390        400        410        420 
CVKCIKGLGE EKVTVVAYPS GNDVFTALLL ALPPQTWSGI KDQSLLQEMK QLISMVSHPT 

       430        440        450 
LLQQEVLHLR RQLEMLKRCQ ENKEDEELSA PA 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY044049 mRNA. Translation: AAK94671.1.
AC003027 Genomic DNA. Translation: AAD10671.1.
CP002684 Genomic DNA. Translation: AEE27641.1.
BT029214 mRNA. Translation: ABJ17149.1.
PIRG86170.
RefSeqNP_171894.1. NM_100279.4.
UniGeneAt.26664.
At.71149.

3D structure databases

ProteinModelPortalQ9ZWB7.
SMRQ9ZWB7. Positions 11-216.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3702.AT1G03980.1-P.

Protein family/group databases

MEROPSC83.A01.

Proteomic databases

PRIDEQ9ZWB7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G03980.1; AT1G03980.1; AT1G03980.
GeneID839354.
KEGGath:AT1G03980.

Organism-specific databases

TAIRAT1G03980.

Phylogenomic databases

eggNOGNOG76926.
HOGENOMHOG000241441.
InParanoidQ9ZWB7.
KOK05941.
OMACEPLEIV.
PhylomeDBQ9ZWB7.

Enzyme and pathway databases

BioCycARA:AT1G03980-MONOMER.

Gene expression databases

GenevestigatorQ9ZWB7.

Family and domain databases

InterProIPR007719. Phytochelatin_synthase.
IPR015407. Phytochelatin_synthase_C.
[Graphical view]
PfamPF05023. Phytochelatin. 1 hit.
PF09328. Phytochelatin_C. 2 hits.
[Graphical view]
PROSITEPS51443. PCS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePCS2_ARATH
AccessionPrimary (citable) accession number: Q9ZWB7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: May 1, 1999
Last modified: May 14, 2014
This is version 76 of the entry and version 1 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

Peptidase families

Classification of peptidase families and list of entries

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names