ID   GLOD4_HUMAN             Reviewed;         313 AA.
AC   Q9HC38; D3DTG9; D3DTH1; Q96B89; Q9H3J8; Q9HC37; Q9NVN1;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=Glyoxalase domain-containing protein 4;
GN   Name=GLOD4; Synonyms=C17orf25; ORFNames=CGI-150, My027;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RX   PubMed=11642406; DOI=10.1038/sj.cr.7290088;
RA   Qin W.X., Wan D.F., Sun F.Y., Zhang P.P., Han L.W., Huang Y., Jiang H.Q.,
RA   Zhao X.T., He M., Ye Y., Cong W.M., Wu M.C., Zhang L.S., Yang N.W.,
RA   Gu J.R.;
RT   "Cloning and characterization of a novel gene (C17orf25) from the deletion
RT   region on chromosome 17p13.3 in hepatocellular carcinoma.";
RL   Cell Res. 11:209-216(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Fetal brain;
RA   Mao Y.M., Xie Y., Ying K.;
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ILE-282.
RC   TISSUE=Brain;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 6-12; 97-116; 156-177; 188-198; 240-252 AND 289-305,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Fetal brain cortex;
RA   Lubec G., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [7]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH NUDT9.
RX   PubMed=12897971;
RA   Zhang H.-T., Yan Z.-Q., Hu X.-B., Yang S.-L., Gong Y.;
RT   "Interaction of C17orf25 with ADP-ribose pyrophosphatase NUDT9 detected via
RT   yeast two-hybrid method.";
RL   Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 35:747-751(2003).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
CC   -!- SUBUNIT: Interacts with NUDT9. {ECO:0000269|PubMed:12897971}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000305|PubMed:12897971}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9HC38-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9HC38-2; Sequence=VSP_023646;
CC       Name=3;
CC         IsoId=Q9HC38-3; Sequence=VSP_023646, VSP_023647, VSP_023648;
CC   -!- TISSUE SPECIFICITY: Expressed in heart, brain, liver, kidney, pancreas
CC       and placenta. Not expressed in skeletal muscle and lung.
CC       {ECO:0000269|PubMed:11642406}.
CC   -!- MISCELLANEOUS: Expression is decreased in hepatocellular carcinoma
CC       samples as compared to adjacent non-cancerous liver tissues from the
CC       same patients. Transfection in hepatocellular carcinoma cells and
CC       overexpression can inhibit the cell growth.
CC   -!- SIMILARITY: Belongs to the glyoxalase I family. {ECO:0000305}.
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DR   EMBL; AF177342; AAG17986.1; -; mRNA.
DR   EMBL; AF177343; AAG17987.1; -; mRNA.
DR   EMBL; AF061730; AAG43141.1; -; mRNA.
DR   EMBL; AK001488; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; CH471108; EAW90645.1; -; Genomic_DNA.
DR   EMBL; CH471108; EAW90646.1; -; Genomic_DNA.
DR   EMBL; CH471108; EAW90647.1; -; Genomic_DNA.
DR   EMBL; CH471108; EAW90649.1; -; Genomic_DNA.
DR   EMBL; CH471108; EAW90650.1; -; Genomic_DNA.
DR   EMBL; BC008605; AAH08605.1; -; mRNA.
DR   EMBL; BC015848; AAH15848.1; -; mRNA.
DR   CCDS; CCDS32520.1; -. [Q9HC38-2]
DR   CCDS; CCDS92216.1; -. [Q9HC38-1]
DR   RefSeq; NP_057164.3; NM_016080.3. [Q9HC38-2]
DR   PDB; 3ZI1; X-ray; 1.90 A; A=1-287.
DR   PDBsum; 3ZI1; -.
DR   AlphaFoldDB; Q9HC38; -.
DR   SMR; Q9HC38; -.
DR   BioGRID; 119237; 81.
DR   IntAct; Q9HC38; 12.
DR   MINT; Q9HC38; -.
DR   STRING; 9606.ENSP00000301329; -.
DR   ChEMBL; CHEMBL4295951; -.
DR   GlyGen; Q9HC38; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9HC38; -.
DR   MetOSite; Q9HC38; -.
DR   PhosphoSitePlus; Q9HC38; -.
DR   SwissPalm; Q9HC38; -.
DR   BioMuta; GLOD4; -.
DR   DMDM; 74718831; -.
DR   REPRODUCTION-2DPAGE; IPI00792035; -.
DR   EPD; Q9HC38; -.
DR   jPOST; Q9HC38; -.
DR   MassIVE; Q9HC38; -.
DR   MaxQB; Q9HC38; -.
DR   PeptideAtlas; Q9HC38; -.
DR   ProteomicsDB; 81633; -. [Q9HC38-1]
DR   ProteomicsDB; 81634; -. [Q9HC38-2]
DR   ProteomicsDB; 81635; -. [Q9HC38-3]
DR   Pumba; Q9HC38; -.
DR   TopDownProteomics; Q9HC38-2; -. [Q9HC38-2]
DR   Antibodypedia; 10285; 130 antibodies from 25 providers.
DR   DNASU; 51031; -.
DR   Ensembl; ENST00000301328.9; ENSP00000301328.5; ENSG00000167699.14. [Q9HC38-1]
DR   Ensembl; ENST00000301329.11; ENSP00000301329.6; ENSG00000167699.14. [Q9HC38-2]
DR   GeneID; 51031; -.
DR   KEGG; hsa:51031; -.
DR   MANE-Select; ENST00000301329.11; ENSP00000301329.6; NM_016080.4; NP_057164.3. [Q9HC38-2]
DR   UCSC; uc002fru.4; human. [Q9HC38-1]
DR   AGR; HGNC:14111; -.
DR   CTD; 51031; -.
DR   DisGeNET; 51031; -.
DR   GeneCards; GLOD4; -.
DR   HGNC; HGNC:14111; GLOD4.
DR   HPA; ENSG00000167699; Low tissue specificity.
DR   MIM; 620650; gene.
DR   neXtProt; NX_Q9HC38; -.
DR   OpenTargets; ENSG00000167699; -.
DR   PharmGKB; PA162389795; -.
DR   VEuPathDB; HostDB:ENSG00000167699; -.
DR   GeneTree; ENSGT00390000012340; -.
DR   HOGENOM; CLU_044479_0_0_1; -.
DR   InParanoid; Q9HC38; -.
DR   OMA; GCEAACN; -.
DR   OrthoDB; 103756at2759; -.
DR   PhylomeDB; Q9HC38; -.
DR   TreeFam; TF105801; -.
DR   PathwayCommons; Q9HC38; -.
DR   SignaLink; Q9HC38; -.
DR   BioGRID-ORCS; 51031; 15 hits in 1158 CRISPR screens.
DR   ChiTaRS; GLOD4; human.
DR   GeneWiki; GLOD4; -.
DR   GenomeRNAi; 51031; -.
DR   Pharos; Q9HC38; Tbio.
DR   PRO; PR:Q9HC38; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q9HC38; Protein.
DR   Bgee; ENSG00000167699; Expressed in buccal mucosa cell and 204 other cell types or tissues.
DR   ExpressionAtlas; Q9HC38; baseline and differential.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR   CDD; cd16357; GLOD4_C; 1.
DR   Gene3D; 3.10.180.10; 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1; 2.
DR   InterPro; IPR043193; GLOD4.
DR   InterPro; IPR043194; GLOD4_C.
DR   InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR   InterPro; IPR037523; VOC.
DR   PANTHER; PTHR46466; GLYOXALASE DOMAIN-CONTAINING PROTEIN 4; 1.
DR   PANTHER; PTHR46466:SF1; GLYOXALASE DOMAIN-CONTAINING PROTEIN 4; 1.
DR   Pfam; PF21701; GLOD4_C; 1.
DR   Pfam; PF21207; GLOD4_N; 1.
DR   SUPFAM; SSF54593; Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase; 2.
DR   PROSITE; PS51819; VOC; 2.
DR   Genevisible; Q9HC38; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Direct protein sequencing;
KW   Mitochondrion; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..313
FT                   /note="Glyoxalase domain-containing protein 4"
FT                   /id="PRO_0000280391"
FT   DOMAIN          5..145
FT                   /note="VOC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   DOMAIN          152..273
FT                   /note="VOC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT   MOD_RES         146
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CPV4"
FT   MOD_RES         288
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CPV4"
FT   VAR_SEQ         32..62
FT                   /note="ESCSVARLECSGAISAHCSDYTRITEDSFSK -> LRHEEFEEGCKAACNG
FT                   (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:11642406,
FT                   ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|Ref.2"
FT                   /id="VSP_023646"
FT   VAR_SEQ         197..203
FT                   /note="CKLELQG -> VSNLGEE (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_023647"
FT   VAR_SEQ         204..313
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_023648"
FT   VARIANT         282
FT                   /note="M -> I (in dbSNP:rs17851349)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_031128"
FT   CONFLICT        295
FT                   /note="A -> S (in Ref. 1; AAG17987)"
FT                   /evidence="ECO:0000305"
FT   STRAND          5..12
FT                   /evidence="ECO:0007829|PDB:3ZI1"
FT   HELIX           16..25
FT                   /evidence="ECO:0007829|PDB:3ZI1"
FT   STRAND          30..37
FT                   /evidence="ECO:0007829|PDB:3ZI1"
FT   STRAND          68..76
FT                   /evidence="ECO:0007829|PDB:3ZI1"
FT   TURN            78..80
FT                   /evidence="ECO:0007829|PDB:3ZI1"
FT   STRAND          83..89
FT                   /evidence="ECO:0007829|PDB:3ZI1"
FT   STRAND          99..107
FT                   /evidence="ECO:0007829|PDB:3ZI1"
FT   HELIX           109..118
FT                   /evidence="ECO:0007829|PDB:3ZI1"
FT   STRAND          123..126
FT                   /evidence="ECO:0007829|PDB:3ZI1"
FT   STRAND          129..133
FT                   /evidence="ECO:0007829|PDB:3ZI1"
FT   STRAND          139..145
FT                   /evidence="ECO:0007829|PDB:3ZI1"
FT   STRAND          152..161
FT                   /evidence="ECO:0007829|PDB:3ZI1"
FT   HELIX           163..172
FT                   /evidence="ECO:0007829|PDB:3ZI1"
FT   STRAND          177..182
FT                   /evidence="ECO:0007829|PDB:3ZI1"
FT   TURN            183..186
FT                   /evidence="ECO:0007829|PDB:3ZI1"
FT   STRAND          187..193
FT                   /evidence="ECO:0007829|PDB:3ZI1"
FT   STRAND          198..203
FT                   /evidence="ECO:0007829|PDB:3ZI1"
FT   STRAND          216..221
FT                   /evidence="ECO:0007829|PDB:3ZI1"
FT   HELIX           223..225
FT                   /evidence="ECO:0007829|PDB:3ZI1"
FT   HELIX           226..235
FT                   /evidence="ECO:0007829|PDB:3ZI1"
FT   STRAND          239..247
FT                   /evidence="ECO:0007829|PDB:3ZI1"
FT   STRAND          255..261
FT                   /evidence="ECO:0007829|PDB:3ZI1"
FT   STRAND          267..272
FT                   /evidence="ECO:0007829|PDB:3ZI1"
FT   HELIX           273..279
FT                   /evidence="ECO:0007829|PDB:3ZI1"
SQ   SEQUENCE   313 AA;  34793 MW;  43DB04159153F07C CRC64;
     MAARRALHFV FKVGNRFQTA RFYRDVLGMK VESCSVARLE CSGAISAHCS DYTRITEDSF
     SKPYDGKWSK TMVGFGPEDD HFVAELTYNY GVGDYKLGND FMGITLASSQ AVSNARKLEW
     PLTEVAEGVF ETEAPGGYKF YLQNRSLPQS DPVLKVTLAV SDLQKSLNYW CNLLGMKIYE
     KDEEKQRALL GYADNQCKLE LQGVKGGVDH AAAFGRIAFS CPQKELPDLE DLMKRENQKI
     LTPLVSLDTP GKATVQVVIL ADPDGHEICF VGDEAFRELS KMDPEGSKLL DDAMAADKSD
     EWFAKHNKPK ASG
//