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Database: UniProt
Entry: Q9CPU0
LinkDB: Q9CPU0
Original site: Q9CPU0 
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   09-JUL-2014, entry version 119.
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).
RN   [4]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-88 AND LYS-148, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
RA   Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH METHYL-GERFELIN,
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, AND
RP   SUBUNIT.
RX   PubMed=18695250; DOI=10.1073/pnas.0712239105;
RA   Kawatani M., Okumura H., Honda K., Kanoh N., Muroi M., Dohmae N.,
RA   Takami M., Kitagawa M., Futamura Y., Imoto M., Osada H.;
RT   "The identification of an osteoclastogenesis inhibitor through the
RT   inhibition of glyoxalase I.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:11691-11696(2008).
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. Required for normal osteoclastogenesis.
CC   -!- CATALYTIC ACTIVITY: (R)-S-lactoylglutathione = glutathione +
CC       methylglyoxal.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit. In the homodimer, two zinc
CC       ions are bound between subunits.
CC   -!- ENZYME REGULATION: Subject to competitive inhibition by methyl-
CC       gerfelin.
CC   -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal
CC       degradation; (R)-lactate from methylglyoxal: step 1/2.
CC   -!- SUBUNIT: Homodimer.
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   CCDS; CCDS28600.1; -.
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   PDB; 4KYH; X-ray; 2.50 A; A/B=1-184.
DR   PDB; 4KYK; X-ray; 2.00 A; A/B=1-184.
DR   PDBsum; 2ZA0; -.
DR   PDBsum; 4KYH; -.
DR   PDBsum; 4KYK; -.
DR   ProteinModelPortal; Q9CPU0; -.
DR   SMR; Q9CPU0; 4-183.
DR   IntAct; Q9CPU0; 5.
DR   MINT; MINT-2513171; -.
DR   ChEMBL; CHEMBL2175; -.
DR   PhosphoSite; Q9CPU0; -.
DR   REPRODUCTION-2DPAGE; IPI00321734; -.
DR   REPRODUCTION-2DPAGE; Q9CPU0; -.
DR   UCD-2DPAGE; Q9CPU0; -.
DR   MaxQB; 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   UCSC; uc012aos.1; mouse.
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; EOG7XPZ6W; -.
DR   PhylomeDB; Q9CPU0; -.
DR   TreeFam; TF105011; -.
DR   UniPathway; UPA00619; UER00675.
DR   ChiTaRS; GLO1; mouse.
DR   EvolutionaryTrace; Q9CPU0; -.
DR   NextBio; 362781; -.
DR   PRO; PR:Q9CPU0; -.
DR   ArrayExpress; Q9CPU0; -.
DR   Bgee; Q9CPU0; -.
DR   CleanEx; MM_GLO1; -.
DR   Genevestigator; Q9CPU0; -.
DR   GO; GO:0004462; F:lactoylglutathione lyase activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:Ensembl.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:Ensembl.
DR   GO; GO:0009438; P:methylglyoxal metabolic process; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0030316; P:osteoclast differentiation; IMP:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:MGI.
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; IPR004361; Glyoxalase_1.
DR   InterPro; IPR018146; Glyoxalase_1_CS.
DR   Pfam; PF00903; Glyoxalase; 1.
DR   SUPFAM; SSF54593; SSF54593; 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   REGION      157    158       Substrate binding.
FT   ACT_SITE    173    173       Proton donor/acceptor (By similarity).
FT   METAL        34     34       Zinc; shared with dimeric partner.
FT   METAL       100    100       Zinc; shared with dimeric partner.
FT   METAL       127    127       Zinc; via tele nitrogen.
FT   METAL       173    173       Zinc.
FT   BINDING      34     34       Substrate; shared with dimeric partner.
FT   BINDING      38     38       Substrate; shared with dimeric partner.
FT   BINDING     104    104       Substrate; shared with dimeric partner.
FT   BINDING     123    123       Substrate (By similarity).
FT   BINDING     127    127       Substrate (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      88     88       N6-succinyllysine.
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; alternate (By
FT                                similarity).
FT   MOD_RES     148    148       N6-succinyllysine; alternate.
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
//
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