PCS2_ARATH
ID PCS2_ARATH Reviewed; 452 AA.
AC Q9ZWB7;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Glutathione gamma-glutamylcysteinyltransferase 2;
DE EC=2.3.2.15;
DE AltName: Full=Phytochelatin synthase 2;
DE Short=AtPCS2;
GN Name=PCS2; OrderedLocusNames=At1g03980; ORFNames=F21M11.9;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION, LACK OF
RP INDUCTION BY CADMIUM, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=11684101; DOI=10.1016/s0014-5793(01)02976-3;
RA Cazale A.-C., Clemens S.;
RT "Arabidopsis thaliana expresses a second functional phytochelatin
RT synthase.";
RL FEBS Lett. 507:215-219(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=15750344;
RA Lee S., Kang B.S.;
RT "Expression of Arabidopsis phytochelatin synthase 2 is too low to
RT complement an AtPCS1-defective Cad1-3 mutant.";
RL Mol. Cells 19:81-87(2005).
RN [6]
RP FUNCTION.
RX PubMed=17253989; DOI=10.1111/j.1365-313x.2006.02993.x;
RA Blum R., Beck A., Korte A., Stengel A., Letzel T., Lendzian K., Grill E.;
RT "Function of phytochelatin synthase in catabolism of glutathione-
RT conjugates.";
RL Plant J. 49:740-749(2007).
CC -!- FUNCTION: Involved in the synthesis of phytochelatins (PC) and
CC homophytochelatins (hPC), the heavy-metal-binding peptides of plants.
CC {ECO:0000269|PubMed:11684101, ECO:0000269|PubMed:15750344,
CC ECO:0000269|PubMed:17253989}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[Glu(-Cys)](n)-Gly + glutathione + H(+) = [Glu(-Cys)](n+1)-Gly
CC + glycine; Xref=Rhea:RHEA:17917, Rhea:RHEA-COMP:12438, Rhea:RHEA-
CC COMP:12439, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:131728; EC=2.3.2.15; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00773};
CC -!- ACTIVITY REGULATION: Requires cadmium for activity. Also activated in
CC heterologous system by AsO(4)(3-) ions, but not by Cu(2+), Zn(2+),
CC Mn(2+) or Ni(2+) ions. {ECO:0000269|PubMed:11684101}.
CC -!- TISSUE SPECIFICITY: Expressed in shoots, roots, leaves, stems and
CC flowers. {ECO:0000269|PubMed:11684101}.
CC -!- INDUCTION: Not induced by cadmium or other heavy metal stress.
CC -!- MISCELLANEOUS: Expression of PCS2 is too low to complement a PCS1-
CC defective mutant.
CC -!- SIMILARITY: Belongs to the phytochelatin synthase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00773}.
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DR EMBL; AY044049; AAK94671.1; -; mRNA.
DR EMBL; AC003027; AAD10671.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60703.1; -; Genomic_DNA.
DR EMBL; BT029214; ABJ17149.1; -; mRNA.
DR PIR; G86170; G86170.
DR RefSeq; NP_171894.1; NM_100279.5.
DR AlphaFoldDB; Q9ZWB7; -.
DR SMR; Q9ZWB7; -.
DR STRING; 3702.AT1G03980.1; -.
DR MEROPS; C83.004; -.
DR iPTMnet; Q9ZWB7; -.
DR PaxDb; Q9ZWB7; -.
DR PRIDE; Q9ZWB7; -.
DR ProteomicsDB; 236849; -.
DR EnsemblPlants; AT1G03980.3; AT1G03980.3; AT1G03980.
DR GeneID; 839354; -.
DR Gramene; AT1G03980.3; AT1G03980.3; AT1G03980.
DR KEGG; ath:AT1G03980; -.
DR Araport; AT1G03980; -.
DR TAIR; locus:2024172; AT1G03980.
DR eggNOG; KOG0632; Eukaryota.
DR HOGENOM; CLU_046059_0_0_1; -.
DR InParanoid; Q9ZWB7; -.
DR PhylomeDB; Q9ZWB7; -.
DR BioCyc; ARA:AT1G03980-MON; -.
DR PRO; PR:Q9ZWB7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZWB7; baseline and differential.
DR Genevisible; Q9ZWB7; AT.
DR GO; GO:0016756; F:glutathione gamma-glutamylcysteinyltransferase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0098849; P:cellular detoxification of cadmium ion; IBA:GO_Central.
DR GO; GO:0010273; P:detoxification of copper ion; IBA:GO_Central.
DR GO; GO:0046938; P:phytochelatin biosynthetic process; IDA:TAIR.
DR Gene3D; 3.90.70.30; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR040409; PCS-like.
DR InterPro; IPR007719; PCS_N.
DR InterPro; IPR038156; PCS_N_sf.
DR InterPro; IPR015407; Phytochelatin_synthase_C.
DR PANTHER; PTHR33447; PTHR33447; 1.
DR Pfam; PF05023; Phytochelatin; 1.
DR Pfam; PF09328; Phytochelatin_C; 2.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS51443; PCS; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Cadmium; Coiled coil; Metal-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..452
FT /note="Glutathione gamma-glutamylcysteinyltransferase 2"
FT /id="PRO_0000287211"
FT DOMAIN 1..220
FT /note="Peptidase C83"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00773"
FT COILED 287..315
FT /evidence="ECO:0000255"
SQ SEQUENCE 452 AA; 51551 MW; 8E8FD573E9C00A76 CRC64;
MSMASLYRRS LSPPAIDFAS FEGKQIFNEA LQKGTMEGFF GLISYFQTQS EPAFCGLASL
SMVLNSLSID PGRKWKGPWR WFDESMLECC EPLEIVKDKG ISFGKVVCLA HSSGAKVEAF
RTNQSTIDDF RKYVVKCSTS DNCHMISTYH RQVLKQTGTG HFSPIGGYNA ERDMALILDV
ARFKYPPHWV PLKLLWDAMD SIDQSTGRRR GFMLISRPHR EPGLLYTLSC KDESWISIAK
YLKEDVPRLV SSQHVDTIER ILYVVFKSLP ANFNQFIKWM AEIRRTEDVN QNLSSEEKSR
LKLKQELLKQ VQETKLFKHV DKFLSSVYED NLPYVAAKVY CDGDEILSGY ESDESCCKET
CVKCIKGLGE EKVTVVAYPS GNDVFTALLL ALPPQTWSGI KDQSLLQEMK QLISMVSHPT
LLQQEVLHLR RQLEMLKRCQ ENKEDEELSA PA
