ID LGUL_MOUSE Reviewed; 184 AA.
AC Q9CPU0; Q543L3; Q8R3T1;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-APR-2013, entry version 107.
DE RecName: Full=Lactoylglutathione lyase;
DE EC=4.4.1.5;
DE AltName: Full=Aldoketomutase;
DE AltName: Full=Glyoxalase I;
DE Short=Glx I;
DE AltName: Full=Ketone-aldehyde mutase;
DE AltName: Full=Methylglyoxalase;
DE AltName: Full=S-D-lactoylglutathione methylglyoxal lyase;
GN Name=Glo1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Embryo, Kidney, Liver, Medulla oblongata, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6, and Czech II; TISSUE=Brain, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND EXPRESSION IN CD-1 STRAIN.
RX PubMed=15858064; DOI=10.1523/JNEUROSCI.0115-05.2005;
RA Kroemer S.A., Kessler M.S., Milfay D., Birg I.N., Bunck M.,
RA Czibere L., Panhuysen M., Puetz B., Deussing J.M., Holsboer F.,
RA Landgraf R., Turck C.W.;
RT "Identification of glyoxalase-I as a protein marker in a mouse model
RT of extremes in trait anxiety.";
RL J. Neurosci. 25:4375-4384(2005).
CC -!- FUNCTION: Catalyzes the conversion of hemimercaptal, formed from
CC methylglyoxal and glutathione, to S-lactoylglutathione. Involved
CC in the regulation of TNF-induced transcriptional activity of NF-
CC kappa-B (By similarity).
CC -!- CATALYTIC ACTIVITY: (R)-S-lactoylglutathione = glutathione +
CC methylglyoxal.
CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal
CC degradation; (R)-lactate from methylglyoxal: step 1/2.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- PTM: Glutathionylation at Cys-139 inhibits enzyme activity (By
CC similarity).
CC -!- PTM: Phosphorylated at Thr-107 in the presence of CaMK2. However,
CC this is a consensus site for phosphorylation by CK2 so
CC phosphorylation may be mediated by CK2 rather than CaMK2.
CC Phosphorylation is induced by TNF and suppresses the TNF-induced
CC transcriptional activity of NF-kappa-B (By similarity).
CC -!- PTM: Exists in a nitric oxide (NO)-modified form. The exact nature
CC of the modification is unknown, but it suppresses the TNF-induced
CC transcriptional activity of NF-kappa-B (By similarity).
CC -!- MISCELLANEOUS: Expressed at higher levels in CD-1 mice which have
CC been bred for low-anxiety-related behavior than in those which
CC have been bred for high-anxiety-related behavior.
CC -!- SIMILARITY: Belongs to the glyoxalase I family.
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DR EMBL; AK002386; BAB22060.1; -; mRNA.
DR EMBL; AK003567; BAB22863.1; -; mRNA.
DR EMBL; AK005055; BAB23781.1; -; mRNA.
DR EMBL; AK031832; BAC27570.1; -; mRNA.
DR EMBL; AK049703; BAC33882.1; -; mRNA.
DR EMBL; BC024663; AAH24663.1; -; mRNA.
DR EMBL; BC081432; AAH81432.1; -; mRNA.
DR IPI; IPI00321734; -.
DR RefSeq; NP_001107032.1; NM_001113560.1.
DR RefSeq; NP_079650.3; NM_025374.3.
DR UniGene; Mm.261984; -.
DR PDB; 2ZA0; X-ray; 1.70 A; A/B=1-184.
DR PDBsum; 2ZA0; -.
DR ProteinModelPortal; Q9CPU0; -.
DR SMR; Q9CPU0; 4-183.
DR IntAct; Q9CPU0; 1.
DR PhosphoSite; Q9CPU0; -.
DR REPRODUCTION-2DPAGE; IPI00321734; -.
DR REPRODUCTION-2DPAGE; Q9CPU0; -.
DR UCD-2DPAGE; Q9CPU0; -.
DR PaxDb; Q9CPU0; -.
DR PRIDE; Q9CPU0; -.
DR Ensembl; ENSMUST00000024823; ENSMUSP00000024823; ENSMUSG00000024026.
DR Ensembl; ENSMUST00000167624; ENSMUSP00000126586; ENSMUSG00000024026.
DR GeneID; 109801; -.
DR KEGG; mmu:109801; -.
DR CTD; 2739; -.
DR MGI; MGI:95742; Glo1.
DR eggNOG; COG0346; -.
DR GeneTree; ENSGT00390000009312; -.
DR HOGENOM; HOG000232011; -.
DR HOVERGEN; HBG025852; -.
DR InParanoid; Q9CPU0; -.
DR KO; K01759; -.
DR OMA; WALSRKA; -.
DR OrthoDB; EOG4TQMB3; -.
DR UniPathway; UPA00619; UER00675.
DR ChEMBL; CHEMBL2175; -.
DR ChiTaRS; GLO1; mouse.
DR EvolutionaryTrace; Q9CPU0; -.
DR NextBio; 362781; -.
DR ArrayExpress; Q9CPU0; -.
DR Bgee; Q9CPU0; -.
DR CleanEx; MM_GLO1; -.
DR Genevestigator; Q9CPU0; -.
DR GermOnline; ENSMUSG00000024026; Mus musculus.
DR GermOnline; ENSMUSG00000075391; Mus musculus.
DR GO; GO:0004462; F:lactoylglutathione lyase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:Compara.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:Compara.
DR GO; GO:0009438; P:methylglyoxal metabolic process; IEA:Compara.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR InterPro; IPR004361; Glyoxalase_1.
DR InterPro; IPR018146; Glyoxalase_1_CS.
DR Pfam; PF00903; Glyoxalase; 1.
DR TIGRFAMs; TIGR00068; glyox_I; 1.
DR PROSITE; PS00934; GLYOXALASE_I_1; 1.
DR PROSITE; PS00935; GLYOXALASE_I_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Disulfide bond;
KW Glutathionylation; Lyase; Metal-binding; Phosphoprotein;
KW Reference proteome; Zinc.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 184 Lactoylglutathione lyase.
FT /FTId=PRO_0000168078.
FT METAL 34 34 Zinc (By similarity).
FT METAL 100 100 Zinc (By similarity).
FT METAL 127 127 Zinc (By similarity).
FT METAL 173 173 Zinc (By similarity).
FT MOD_RES 2 2 N-acetylalanine (By similarity).
FT MOD_RES 107 107 Phosphothreonine (By similarity).
FT MOD_RES 139 139 S-glutathionyl cysteine (By similarity).
FT MOD_RES 148 148 N6-acetyllysine (By similarity).
FT DISULFID 19 20 By similarity.
FT CONFLICT 92 92 T -> M (in Ref. 2; AAH24663).
FT HELIX 13 18
FT HELIX 25 27
FT STRAND 31 38
FT HELIX 42 51
FT STRAND 56 63
FT HELIX 64 66
FT STRAND 68 75
FT HELIX 78 80
FT HELIX 85 92
FT STRAND 95 104
FT HELIX 107 109
FT STRAND 118 122
FT STRAND 125 131
FT HELIX 135 144
FT STRAND 149 151
FT STRAND 155 158
FT STRAND 162 165
FT STRAND 171 175
FT TURN 177 179
FT HELIX 180 182
SQ SEQUENCE 184 AA; 20810 MW; F6B5667A65454D18 CRC64;
MAEPQPASSG LTDETAFSCC SDPDPSTKDF LLQQTMLRIK DPKKSLDFYT RVLGLTLLQK
LDFPAMKFSL YFLAYEDKND IPKDKSEKTA WTFSRKATLE LTHNWGTEDD ETQSYHNGNS
DPRGFGHIGI AVPDVYSACK RFEELGVKFV KKPDDGKMKG LAFIQDPDGY WIEILNPNKI
ATII
//
