PCS1_CAEEL
ID PCS1_CAEEL Reviewed; 426 AA.
AC A5JYS0; A5JYS1; G5ECE4;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Glutathione gamma-glutamylcysteinyltransferase {ECO:0000255|PROSITE-ProRule:PRU00773};
DE EC=2.3.2.15 {ECO:0000269|PubMed:11313333, ECO:0000269|PubMed:20221439};
DE AltName: Full=Phytochelatin synthase {ECO:0000303|PubMed:11313333};
DE Short=PC synthase {ECO:0000303|PubMed:11313333};
GN Name=pcs-1 {ECO:0000303|PubMed:11313333, ECO:0000312|WormBase:F54D5.1a};
GN ORFNames=F54D5.1 {ECO:0000312|WormBase:F54D5.1a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:AAK62992.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM B), FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, AND DISRUPTION PHENOTYPE.
RX PubMed=11313333; DOI=10.1074/jbc.c100152200;
RA Vatamaniuk O.K., Bucher E.A., Ward J.T., Rea P.A.;
RT "A new pathway for heavy metal detoxification in animals. Phytochelatin
RT synthase is required for cadmium tolerance in Caenorhabditis elegans.";
RL J. Biol. Chem. 276:20817-20820(2001).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=20221439; DOI=10.1371/journal.pone.0009564;
RA Schwartz M.S., Benci J.L., Selote D.S., Sharma A.K., Chen A.G., Dang H.,
RA Fares H., Vatamaniuk O.K.;
RT "Detoxification of multiple heavy metals by a half-molecule ABC
RT transporter, HMT-1, and coelomocytes of Caenorhabditis elegans.";
RL PLoS ONE 5:E9564-E9564(2010).
RN [4] {ECO:0000305}
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=24333255; DOI=10.1016/j.cbpc.2013.12.001;
RA Polak N., Read D.S., Jurkschat K., Matzke M., Kelly F.J., Spurgeon D.J.,
RA Stuerzenbaum S.R.;
RT "Metalloproteins and phytochelatin synthase may confer protection against
RT zinc oxide nanoparticle induced toxicity in Caenorhabditis elegans.";
RL Comp. Biochem. Physiol. 160:75-85(2014).
RN [5] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=26907254; DOI=10.3390/ijms17020257;
RA Essig Y.J., Webb S.M., Stuerzenbaum S.R.;
RT "Deletion of Phytochelatin Synthase Modulates the Metal Accumulation
RT Pattern of Cadmium Exposed C. elegans.";
RL Int. J. Mol. Sci. 17:257-257(2016).
CC -!- FUNCTION: Involved in the synthesis of phytochelatins, which are heavy
CC metal binding proteins required for the detoxification of heavy metals
CC such as cadmium, arsenic and copper. {ECO:0000269|PubMed:11313333,
CC ECO:0000269|PubMed:20221439, ECO:0000269|PubMed:26907254}.
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;
CC Evidence={ECO:0000269|PubMed:11313333, ECO:0000269|PubMed:20221439};
CC -!- ACTIVITY REGULATION: Requires cadmium for activity.
CC {ECO:0000305|PubMed:11313333}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:F54D5.1a};
CC IsoId=A5JYS0-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F54D5.1b};
CC IsoId=A5JYS0-2; Sequence=VSP_060555;
CC -!- TISSUE SPECIFICITY: Expressed in hypodermis, pharyngeal grinder,
CC pharyngeal-intestinal valve, body wall and vulval muscles, and
CC coelomocytes (PubMed:20221439). Expressed in posterior pharyngeal cells
CC and anal valve (PubMed:24333255, PubMed:26907254).
CC {ECO:0000269|PubMed:20221439, ECO:0000269|PubMed:24333255,
CC ECO:0000269|PubMed:26907254}.
CC -!- INDUCTION: Induced by zinc oxide nanoparticles in intestinal cells
CC (PubMed:24333255). However, not induced by zinc or cadmium
CC (PubMed:26907254). {ECO:0000269|PubMed:24333255,
CC ECO:0000269|PubMed:26907254}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes hypersensitivity
CC to Cd(2+), specifically causes a reduction in growth, impairs
CC development and reduces fertility. {ECO:0000269|PubMed:11313333}.
CC -!- SIMILARITY: Belongs to the phytochelatin synthase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00773}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK62991.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=AAK62992.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AF299332; AAK62991.1; ALT_SEQ; mRNA.
DR EMBL; AF299333; AAK62992.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BX284602; CAN86618.1; -; Genomic_DNA.
DR EMBL; BX284602; CAN86619.1; -; Genomic_DNA.
DR RefSeq; NP_001122615.1; NM_001129143.3. [A5JYS0-1]
DR RefSeq; NP_001122616.1; NM_001129144.2. [A5JYS0-2]
DR AlphaFoldDB; A5JYS0; -.
DR SMR; A5JYS0; -.
DR STRING; 6239.F54D5.1a; -.
DR MEROPS; C83.003; -.
DR PaxDb; A5JYS0; -.
DR PeptideAtlas; A5JYS0; -.
DR EnsemblMetazoa; F54D5.1a.1; F54D5.1a.1; WBGene00003960. [A5JYS0-1]
DR EnsemblMetazoa; F54D5.1b.1; F54D5.1b.1; WBGene00003960. [A5JYS0-2]
DR GeneID; 174775; -.
DR KEGG; cel:CELE_F54D5.1; -.
DR UCSC; F54D5.1b; c. elegans.
DR CTD; 174775; -.
DR WormBase; F54D5.1a; CE40964; WBGene00003960; pcs-1.
DR WormBase; F54D5.1b; CE40965; WBGene00003960; pcs-1.
DR eggNOG; KOG0632; Eukaryota.
DR GeneTree; ENSGT00390000009204; -.
DR HOGENOM; CLU_046059_1_0_1; -.
DR InParanoid; A5JYS0; -.
DR OMA; CRKFGQC; -.
DR OrthoDB; 1279063at2759; -.
DR PhylomeDB; A5JYS0; -.
DR BRENDA; 2.3.2.15; 1045.
DR PRO; PR:A5JYS0; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00003960; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0016756; F:glutathione gamma-glutamylcysteinyltransferase activity; IDA:WormBase.
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:0071585; P:detoxification of cadmium ion; IMP:UniProtKB.
DR GO; GO:0010273; P:detoxification of copper ion; IMP:WormBase.
DR GO; GO:0050787; P:detoxification of mercury ion; IGI:WormBase.
DR GO; GO:0010312; P:detoxification of zinc ion; IMP:UniProtKB.
DR GO; GO:0046938; P:phytochelatin biosynthetic process; IDA:WormBase.
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 PANTHER; PTHR33447; PTHR33447; 1.
DR Pfam; PF05023; Phytochelatin; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS51443; PCS; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Cadmium; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..426
FT /note="Glutathione gamma-glutamylcysteinyltransferase"
FT /id="PRO_0000449378"
FT DOMAIN 11..232
FT /note="Peptidase C83"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00773"
FT ACT_SITE 65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00773"
FT ACT_SITE 173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00773"
FT ACT_SITE 191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00773"
FT VAR_SEQ 1..8
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060555"
SQ SEQUENCE 426 AA; 48236 MW; E2FFD88F45EB1A40 CRC64;
MSQRRHFKMS VTAKNFYRRP LPETCIEFSS ELGKKLFTEA LVRGSANIYF KLASQFRTQD
EPAYCGLSTL VMVLNALEVD PEKVWKAPWR FYHESMLDCC VPLENIRKSG INLQQFSCLA
KCNRLKSTVS YGDNSPDFLK KFRTSLVNSV RSDDQVLVAS YDRSVLGQTG SGHFSPLAAY
HEDSDQVLIM DVARFKYPPH WVKLETLQKA LCSVDVTTKL PRGLVELELK KGTRPLIMYG
LKAYVNINDS DFATSVISWN QFLLCDPLED DEEEFQLCCR KFGQCFAPHA MCCTQKTFDA
DQKNSCTECS TDQNEACKMI CSEIRRTRFA EVFSSSAVAA LLIAWPFEKG YSERSDRIGN
LAEKYKNEFS AETMNEMNQL TTQIRTLISC SKPPVVININ KPDATSNKCC KNKIGQSCAC
ANDVNL
