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GLOD4_CAEEL
ID   GLOD4_CAEEL             Reviewed;         281 AA.
AC   Q09253;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Glyoxalase 1;
DE            Short=CeGly;
DE   AltName: Full=Glyoxalase domain-containing protein 4;
GN   Name=glod-4; Synonyms=tag-73; ORFNames=C16C10.10;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
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   [2]
RP   TISSUE SPECIFICITY.
RX   PubMed=17850180; DOI=10.1371/journal.pbio.0050237;
RA   Hunt-Newbury R., Viveiros R., Johnsen R., Mah A., Anastas D., Fang L.,
RA   Halfnight E., Lee D., Lin J., Lorch A., McKay S., Okada H.M., Pan J.,
RA   Schulz A.K., Tu D., Wong K., Zhao Z., Alexeyenko A., Burglin T.,
RA   Sonnhammer E., Schnabel R., Jones S.J., Marra M.A., Baillie D.L.,
RA   Moerman D.G.;
RT   "High-throughput in vivo analysis of gene expression in Caenorhabditis
RT   elegans.";
RL   PLoS Biol. 5:E237-E237(2007).
RN   [3]
RP   FUNCTION.
RX   PubMed=18221415; DOI=10.1111/j.1474-9726.2008.00371.x;
RA   Morcos M., Du X., Pfisterer F., Hutter H., Sayed A.A.R., Thornalley P.,
RA   Ahmed N., Baynes J., Thorpe S., Kukudov G., Schlotterer A., Bozorgmehr F.,
RA   El Baki R.A., Stern D., Moehrlen F., Ibrahim Y., Oikonomou D., Hamann A.,
RA   Becker C., Zeier M., Schwenger V., Miftari N., Humpert P., Hammes H.-P.,
RA   Buechler M., Bierhaus A., Brownlee M., Nawroth P.P.;
RT   "Glyoxalase-1 prevents mitochondrial protein modification and enhances
RT   lifespan in Caenorhabditis elegans.";
RL   Aging Cell 7:260-269(2008).
CC   -!- FUNCTION: Thought to act as a glyoxalase. May remove methylglyoxal from
CC       mitochondrial proteins. Has roles in reducing oxidative stress and
CC       increasing lifespan. {ECO:0000269|PubMed:18221415}.
CC   -!- TISSUE SPECIFICITY: Expressed in the following tissues in both larvae
CC       and adults: pharynx, pharyngeal-intestinal valve, intestine, anal
CC       sphincter, vulval muscle, seam cells and the nervous system.
CC       {ECO:0000269|PubMed:17850180}.
CC   -!- DEVELOPMENTAL STAGE: Expression increases from day 1 to day 12 but
CC       activity decreased 10-fold during this period indicating that post
CC       translational modification is operational.
CC   -!- SIMILARITY: Belongs to the glyoxalase I family. {ECO:0000305}.
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DR   EMBL; Z46787; CAA86748.1; -; Genomic_DNA.
DR   PIR; T19331; T19331.
DR   RefSeq; NP_497827.1; NM_065426.1.
DR   AlphaFoldDB; Q09253; -.
DR   SMR; Q09253; -.
DR   BioGRID; 40767; 8.
DR   STRING; 6239.C16C10.10; -.
DR   EPD; Q09253; -.
DR   PaxDb; Q09253; -.
DR   PeptideAtlas; Q09253; -.
DR   EnsemblMetazoa; C16C10.10.1; C16C10.10.1; WBGene00006448.
DR   GeneID; 175530; -.
DR   KEGG; cel:CELE_C16C10.10; -.
DR   CTD; 175530; -.
DR   WormBase; C16C10.10; CE01490; WBGene00006448; glod-4.
DR   eggNOG; KOG2943; Eukaryota.
DR   GeneTree; ENSGT00390000012340; -.
DR   HOGENOM; CLU_044479_0_0_1; -.
DR   InParanoid; Q09253; -.
DR   OMA; GCEAACN; -.
DR   OrthoDB; 824414at2759; -.
DR   PhylomeDB; Q09253; -.
DR   PRO; PR:Q09253; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00006448; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0008340; P:determination of adult lifespan; IMP:UniProtKB.
DR   GO; GO:0009438; P:methylglyoxal metabolic process; IMP:UniProtKB.
DR   CDD; cd16357; GLOD4_C; 1.
DR   Gene3D; 3.10.180.10; -; 2.
DR   InterPro; IPR043193; GLOD4.
DR   InterPro; IPR043194; GLOD4_C.
DR   InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR   InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR   InterPro; IPR037523; VOC.
DR   PANTHER; PTHR46466; PTHR46466; 1.
DR   Pfam; PF00903; Glyoxalase; 1.
DR   SUPFAM; SSF54593; SSF54593; 2.
DR   PROSITE; PS51819; VOC; 2.
PE   2: Evidence at transcript level;
KW   Reference proteome; Repeat.
FT   CHAIN           1..281
FT                   /note="Glyoxalase 1"
FT                   /id="PRO_0000065184"
FT   DOMAIN          4..127
FT                   /note="VOC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   DOMAIN          132..251
FT                   /note="VOC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
SQ   SEQUENCE   281 AA;  32093 MW;  D32D2A9573EA517B CRC64;
     MTARALHYVF KVANRAKTID FFTNVLNMKV LRHEEFEKGC EATCNGPYNG RWSKTMIGYG
     SEDEHFVLEI TYNYPIHKYE LGNDYRAIVI DSDQLFEKVE KINHRKSGCG RLAVKDPDGH
     EFKIGKADQS PKVLRVQVNV GDLEKSKKYW NETLGMPIVE EKSSRIRMSY GDGQCELEIV
     KSQDKIDRKT GFGRIAFSYP EDKLESLQDK IKSANGTIIN ELTTLETPGK ADVQVVILAD
     PDEHEICFVG DEGFRALSKI DDKAESELKE QIKKDDSEKW I
 
 
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