GAGT4_ARATH
ID GAGT4_ARATH Reviewed; 191 AA.
AC Q9CAR5;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Putative inactive glutathione hydrolase 4;
DE AltName: Full=Gamma-glutamyltranspeptidase 3;
DE AltName: Full=Putative inactive gamma-glutamyltranspeptidase 4;
GN Name=GGT4; Synonyms=GGT3; OrderedLocusNames=At1g69820; ORFNames=T17F3.15;
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 [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 [2]
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 [3]
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17545509; DOI=10.1104/pp.106.094409;
RA Martin M.N., Saladores P.H., Lambert E., Hudson A.O., Leustek T.;
RT "Localization of members of the gamma-glutamyl transpeptidase family
RT identifies sites of glutathione and glutathione S-conjugate hydrolysis.";
RL Plant Physiol. 144:1715-1732(2007).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=20959624; DOI=10.1093/jxb/erq316;
RA Destro T., Prasad D., Martignago D., Bernet I.L., Trentin A.R., Renu I.K.,
RA Ferretti M., Masi A.;
RT "Compensatory expression and substrate inducibility of gamma-glutamyl
RT transferase GGT2 isoform in Arabidopsis thaliana.";
RL J. Exp. Bot. 62:805-814(2011).
CC -!- TISSUE SPECIFICITY: Expressed at low levels in embryo, roots and
CC leaves. In mature plants, expression is restricted to vascular tissues
CC of roots, leaves, flowers and siliques. {ECO:0000269|PubMed:17545509,
CC ECO:0000269|PubMed:20959624}.
CC -!- DISRUPTION PHENOTYPE: Mutant plants (Ds insertion) display reduced
CC inflorescence height, silique number and seed yield.
CC {ECO:0000269|PubMed:17545509}.
CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene; it is missing regions at
CC the N- and C-terminus compared to its paralogs. {ECO:0000305}.
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DR EMBL; AC010675; AAG52560.1; -; Genomic_DNA.
DR EMBL; CP002684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; D96720; D96720.
DR AlphaFoldDB; Q9CAR5; -.
DR SMR; Q9CAR5; -.
DR STRING; 3702.AT1G69820.1; -.
DR MEROPS; T03.008; -.
DR PaxDb; Q9CAR5; -.
DR PRIDE; Q9CAR5; -.
DR Araport; AT1G69820; -.
DR TAIR; locus:2196769; AT1G69820.
DR eggNOG; KOG2410; Eukaryota.
DR HOGENOM; CLU_014813_1_2_1; -.
DR InParanoid; Q9CAR5; -.
DR PhylomeDB; Q9CAR5; -.
DR BioCyc; ARA:AT1G69820-MON; -.
DR BRENDA; 2.3.2.2; 399.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9CAR5; baseline and differential.
DR Genevisible; Q9CAR5; AT.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0036374; F:glutathione hydrolase activity; IBA:GO_Central.
DR GO; GO:0006751; P:glutathione catabolic process; IBA:GO_Central.
DR Gene3D; 1.10.246.130; -; 1.
DR Gene3D; 3.60.20.40; -; 1.
DR InterPro; IPR043138; GGT_lsub_C.
DR InterPro; IPR000101; GGT_peptidase.
DR InterPro; IPR043137; GGT_ssub.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR PANTHER; PTHR11686; PTHR11686; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
PE 5: Uncertain;
KW Reference proteome.
FT CHAIN 1..191
FT /note="Putative inactive glutathione hydrolase 4"
FT /id="PRO_0000420914"
FT ACT_SITE 54
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 126..127
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 147..148
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
SQ SEQUENCE 191 AA; 20908 MW; ED62B71D2E52AE40 CRC64;
MNLGDPDFVD VSKVISDMLS TNFAQGLKKK INDNKTFDPN YYGGRWDQIN DHGTSHLSII
DSERNVVSLT STINSYFGAL MLSPSTGIVL NNEMDDFSIP MKSSSNLTVP PPAPANFIRP
GKRPLSSMTP TIVLKDGKVK ASVGASGGLY IIAGTTEVFL NYFFLKMDPL SSVLAPRIYH
QLIPNIVSYE N
