GLYI4_ARATH
ID GLYI4_ARATH Reviewed; 174 AA.
AC Q9XI31;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Glyoxylase I 4 {ECO:0000303|PubMed:30483284, ECO:0000303|PubMed:31652571};
DE Short=AtGLXI-like;4 {ECO:0000303|PubMed:30483284};
DE Short=AtGLYI4 {ECO:0000303|PubMed:21213008};
GN Name=GLYI4 {ECO:0000303|PubMed:21213008, ECO:0000303|PubMed:30483284,
GN ECO:0000303|PubMed:31652571};
GN OrderedLocusNames=At1g15380 {ECO:0000312|Araport:AT1G15380};
GN ORFNames=F9L1.33 {ECO:0000312|EMBL:AAD39666.1};
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INDUCTION BY ABIOTIC STRESSES, TISSUE SPECIFICITY, GENE FAMILY, AND
RP NOMENCLATURE.
RX PubMed=21213008; DOI=10.1007/s10142-010-0203-2;
RA Mustafiz A., Singh A.K., Pareek A., Sopory S.K., Singla-Pareek S.L.;
RT "Genome-wide analysis of rice and Arabidopsis identifies two glyoxalase
RT genes that are highly expressed in abiotic stresses.";
RL Funct. Integr. Genomics 11:293-305(2011).
RN [7]
RP TISSUE SPECIFICITY, INDUCTION BY SALT AND NICKEL IONS, AND GENE FAMILY.
RX PubMed=30483284; DOI=10.3389/fpls.2018.01618;
RA Schmitz J., Rossoni A.W., Maurino V.G.;
RT "Dissecting the physiological function of plant glyoxalase I and glyoxalase
RT I-like proteins.";
RL Front. Plant Sci. 9:1618-1618(2018).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Col-8;
RX PubMed=29852537; DOI=10.1111/pce.13357;
RA Proietti S., Caarls L., Coolen S., Van Pelt J.A., Van Wees S.C.M.,
RA Pieterse C.M.J.;
RT "Genome-wide association study reveals novel players in defense hormone
RT crosstalk in Arabidopsis.";
RL Plant Cell Environ. 41:2342-2356(2018).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INDUCTION BY
RP METHYLGLYOXAL.
RC STRAIN=cv. Col-8;
RX PubMed=31652571; DOI=10.3390/biom9100635;
RA Proietti S., Falconieri G.S., Bertini L., Baccelli I., Paccosi E.,
RA Belardo A., Timperio A.M., Caruso C.;
RT "GLYI4 plays a role in methylglyoxal detoxification and jasmonate-mediated
RT stress responses in Arabidopsis thaliana.";
RL Biomolecules 9:635-635(2019).
CC -!- FUNCTION: Involved in the detoxification and scavenging of
CC methylglyoxal (MG), a cytotoxic aldehyde produced in response to
CC primary metabolism alteration observed during biotic and abiotic
CC stresses (PubMed:31652571). Modulates cross-talk between salicylic acid
CC (SA) and jasmonic acid (JA) signaling pathways during defense responses
CC to pathogens such as Botrytis cinerea (PubMed:29852537).
CC {ECO:0000269|PubMed:29852537, ECO:0000269|PubMed:31652571}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:31652571}.
CC Cytoplasm {ECO:0000269|PubMed:31652571}. Note=Localized at the plasma
CC membrane during methylglyoxal (MG) accumulation, but translocates to
CC the cytoplasm upon jasmonate (MeJA) stimulus.
CC {ECO:0000269|PubMed:31652571}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in roots, and, to a lower extent,
CC in leaves, flowers, seeds and siliques. {ECO:0000269|PubMed:21213008,
CC ECO:0000269|PubMed:30483284}.
CC -!- INDUCTION: Accumulates in response to abiotic stresses such as cold,
CC heat, drought, oxidative stress, genotoxic compounds, wounding, osmotic
CC stress and UV-B (PubMed:21213008). Slightly induced by salt (NaCl) and
CC nickel ions Ni(2+) (PubMed:30483284, PubMed:21213008). Strongly induced
CC by methylglyoxal (MG) (PubMed:31652571). {ECO:0000269|PubMed:21213008,
CC ECO:0000269|PubMed:30483284, ECO:0000269|PubMed:31652571}.
CC -!- DISRUPTION PHENOTYPE: General stress phenotype, characterized by
CC compromised methylglyoxal (MG) scavenging, accumulation of reactive
CC oxygen species (ROS), stomatal closure, and reduced fitness associated
CC with reduced leaf area and dry weight, as well as prolonged flowering
CC time (PubMed:31652571). Increased susceptibility to the pathogenic
CC fungus Plectospherella cucumerina which triggers mainly the jasmonate
CC (JA)-mediated defense signaling pathway (PubMed:31652571). Abnormal
CC cross-talk between salicylic acid (SA) and jasmonic acid (JA) signaling
CC pathways (PubMed:29852537). {ECO:0000269|PubMed:29852537,
CC ECO:0000269|PubMed:31652571}.
CC -!- SIMILARITY: Belongs to the glyoxalase I family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC007591; AAD39666.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29312.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29313.1; -; Genomic_DNA.
DR EMBL; AY072377; AAL62369.1; -; mRNA.
DR EMBL; AY114619; AAM47938.1; -; mRNA.
DR EMBL; AK317354; BAH20026.1; -; mRNA.
DR EMBL; AY088300; AAM65839.1; -; mRNA.
DR PIR; D86288; D86288.
DR RefSeq; NP_001031049.1; NM_001035972.2.
DR RefSeq; NP_563973.1; NM_101407.4.
DR AlphaFoldDB; Q9XI31; -.
DR SMR; Q9XI31; -.
DR STRING; 3702.AT1G15380.1; -.
DR PaxDb; Q9XI31; -.
DR PRIDE; Q9XI31; -.
DR ProteomicsDB; 181572; -.
DR DNASU; 838107; -.
DR EnsemblPlants; AT1G15380.1; AT1G15380.1; AT1G15380.
DR EnsemblPlants; AT1G15380.2; AT1G15380.2; AT1G15380.
DR GeneID; 838107; -.
DR Gramene; AT1G15380.1; AT1G15380.1; AT1G15380.
DR Gramene; AT1G15380.2; AT1G15380.2; AT1G15380.
DR KEGG; ath:AT1G15380; -.
DR Araport; AT1G15380; -.
DR TAIR; locus:2037728; AT1G15380.
DR eggNOG; ENOG502QSP6; Eukaryota.
DR HOGENOM; CLU_046006_12_1_1; -.
DR InParanoid; Q9XI31; -.
DR OMA; MEYVPLN; -.
DR OrthoDB; 1456521at2759; -.
DR PhylomeDB; Q9XI31; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9XI31; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0140041; P:cellular detoxification of methylglyoxal; IMP:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009787; P:regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:2000022; P:regulation of jasmonic acid mediated signaling pathway; IMP:TAIR.
DR GO; GO:2000031; P:regulation of salicylic acid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0009408; P:response to heat; IEP:UniProtKB.
DR GO; GO:0009753; P:response to jasmonic acid; IDA:UniProtKB.
DR GO; GO:0051595; P:response to methylglyoxal; IEP:UniProtKB.
DR GO; GO:0010045; P:response to nickel cation; IEP:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IEP:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IEP:UniProtKB.
DR GO; GO:1902074; P:response to salt; IEP:UniProtKB.
DR GO; GO:0010224; P:response to UV-B; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
DR Gene3D; 3.10.180.10; -; 1.
DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR InterPro; IPR037523; VOC.
DR Pfam; PF00903; Glyoxalase; 1.
DR SUPFAM; SSF54593; SSF54593; 1.
DR PROSITE; PS51819; VOC; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Lyase; Membrane; Plant defense;
KW Reference proteome; Stress response.
FT CHAIN 1..174
FT /note="Glyoxylase I 4"
FT /id="PRO_0000453957"
FT DOMAIN 13..135
FT /note="VOC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT ACT_SITE 131
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
SQ SEQUENCE 174 AA; 19594 MW; 078B0EEBE1801054 CRC64;
MKEDAGNPLH LTSLNHVSVL CRSVDESMNF YQKVLGFIPI RRPESLNFEG AWLFGHGIGI
HLLCAPEPEK LPKKTAINPK DNHISFQCES MGVVEKKLEE MGIDYVRALV EEGGIQVDQL
FFHDPDGFMI EICNCDSLPV VPLVGEMARS CSRVKLHQMV QPQPQTQIHQ VVYP
