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DEOC_HUMAN
ID   DEOC_HUMAN              Reviewed;         318 AA.
AC   Q9Y315; Q53HN9; Q6PHW2;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-2002, sequence version 2.
DT   03-AUG-2022, entry version 169.
DE   RecName: Full=Deoxyribose-phosphate aldolase;
DE            Short=DERA;
DE            EC=4.1.2.4 {ECO:0000269|PubMed:25229427};
DE   AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase;
DE   AltName: Full=Phosphodeoxyriboaldolase;
DE            Short=Deoxyriboaldolase;
GN   Name=DERA; ORFNames=CGI-26;
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 [LARGE SCALE MRNA].
RX   PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA   Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT   "Identification of novel human genes evolutionarily conserved in
RT   Caenorhabditis elegans by comparative proteomics.";
RL   Genome Res. 10:703-713(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Adipose tissue;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skin;
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   [4]
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   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, INTERACTION WITH YBX1, TISSUE
RP   SPECIFICITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-218 AND LYS-254.
RX   PubMed=25229427; DOI=10.1016/j.bbamcr.2014.09.007;
RA   Salleron L., Magistrelli G., Mary C., Fischer N., Bairoch A., Lane L.;
RT   "DERA is the human deoxyribose phosphate aldolase and is involved in stress
RT   response.";
RL   Biochim. Biophys. Acta 1843:2913-2925(2014).
RN   [6]
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).
CC   -!- FUNCTION: Catalyzes a reversible aldol reaction between acetaldehyde
CC       and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-
CC       phosphate. Participates in stress granule (SG) assembly. May allow ATP
CC       production from extracellular deoxyinosine in conditions of energy
CC       deprivation. {ECO:0000269|PubMed:25229427}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-deoxy-D-ribose 5-phosphate = acetaldehyde + D-glyceraldehyde
CC         3-phosphate; Xref=Rhea:RHEA:12821, ChEBI:CHEBI:15343,
CC         ChEBI:CHEBI:59776, ChEBI:CHEBI:62877; EC=4.1.2.4;
CC         Evidence={ECO:0000269|PubMed:25229427};
CC   -!- PATHWAY: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate
CC       degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-
CC       deoxy-alpha-D-ribose 1-phosphate: step 2/2.
CC   -!- SUBUNIT: Interacts with YBX1. {ECO:0000269|PubMed:25229427}.
CC   -!- INTERACTION:
CC       Q9Y315; Q8IZ83: ALDH16A1; NbExp=6; IntAct=EBI-1048152, EBI-1044483;
CC       Q9Y315; Q03933: HSF2; NbExp=3; IntAct=EBI-1048152, EBI-2556750;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25229427}.
CC       Cytoplasmic granule {ECO:0000269|PubMed:25229427}. Nucleus
CC       {ECO:0000269|PubMed:25229427}. Note=Recruited to stress granules but
CC       not to processing bodies upon arsenite or clotrimazole treatment or
CC       energy deprivation. {ECO:0000269|PubMed:25229427}.
CC   -!- TISSUE SPECIFICITY: Mainly expressed in liver, lung and colon.
CC       {ECO:0000269|PubMed:25229427}.
CC   -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 2
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD27735.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAH56234.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAD96261.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF132960; AAD27735.1; ALT_INIT; mRNA.
DR   EMBL; AK222541; BAD96261.1; ALT_INIT; mRNA.
DR   EMBL; BC056234; AAH56234.1; ALT_INIT; mRNA.
DR   CCDS; CCDS44838.1; -.
DR   RefSeq; NP_057038.2; NM_015954.3.
DR   AlphaFoldDB; Q9Y315; -.
DR   SMR; Q9Y315; -.
DR   BioGRID; 119262; 38.
DR   IntAct; Q9Y315; 12.
DR   MINT; Q9Y315; -.
DR   STRING; 9606.ENSP00000416583; -.
DR   ChEMBL; CHEMBL4295988; -.
DR   iPTMnet; Q9Y315; -.
DR   MetOSite; Q9Y315; -.
DR   PhosphoSitePlus; Q9Y315; -.
DR   BioMuta; DERA; -.
DR   DMDM; 24636817; -.
DR   EPD; Q9Y315; -.
DR   jPOST; Q9Y315; -.
DR   MassIVE; Q9Y315; -.
DR   MaxQB; Q9Y315; -.
DR   PaxDb; Q9Y315; -.
DR   PeptideAtlas; Q9Y315; -.
DR   PRIDE; Q9Y315; -.
DR   ProteomicsDB; 85959; -.
DR   Antibodypedia; 55098; 76 antibodies from 16 providers.
DR   DNASU; 51071; -.
DR   Ensembl; ENST00000428559.7; ENSP00000416583.2; ENSG00000023697.13.
DR   GeneID; 51071; -.
DR   KEGG; hsa:51071; -.
DR   MANE-Select; ENST00000428559.7; ENSP00000416583.2; NM_015954.4; NP_057038.2.
DR   UCSC; uc001rde.4; human.
DR   CTD; 51071; -.
DR   DisGeNET; 51071; -.
DR   GeneCards; DERA; -.
DR   HGNC; HGNC:24269; DERA.
DR   HPA; ENSG00000023697; Tissue enhanced (liver).
DR   MIM; 619668; gene.
DR   neXtProt; NX_Q9Y315; -.
DR   OpenTargets; ENSG00000023697; -.
DR   PharmGKB; PA134943367; -.
DR   VEuPathDB; HostDB:ENSG00000023697; -.
DR   eggNOG; KOG3981; Eukaryota.
DR   GeneTree; ENSGT00390000007878; -.
DR   HOGENOM; CLU_053595_3_0_1; -.
DR   InParanoid; Q9Y315; -.
DR   OMA; RYSGPDY; -.
DR   OrthoDB; 1349979at2759; -.
DR   PhylomeDB; Q9Y315; -.
DR   TreeFam; TF314251; -.
DR   BRENDA; 4.1.2.4; 2681.
DR   PathwayCommons; Q9Y315; -.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   Reactome; R-HSA-71336; Pentose phosphate pathway.
DR   SABIO-RK; Q9Y315; -.
DR   SignaLink; Q9Y315; -.
DR   SIGNOR; Q9Y315; -.
DR   UniPathway; UPA00002; UER00468.
DR   BioGRID-ORCS; 51071; 9 hits in 1072 CRISPR screens.
DR   ChiTaRS; DERA; human.
DR   GenomeRNAi; 51071; -.
DR   Pharos; Q9Y315; Tbio.
DR   PRO; PR:Q9Y315; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q9Y315; protein.
DR   Bgee; ENSG00000023697; Expressed in secondary oocyte and 203 other tissues.
DR   ExpressionAtlas; Q9Y315; baseline and differential.
DR   Genevisible; Q9Y315; HS.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR   GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; IDA:UniProtKB.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IBA:GO_Central.
DR   GO; GO:0046121; P:deoxyribonucleoside catabolic process; IDA:UniProtKB.
DR   GO; GO:0009264; P:deoxyribonucleotide catabolic process; IBA:GO_Central.
DR   GO; GO:0046386; P:deoxyribose phosphate catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006098; P:pentose-phosphate shunt; TAS:Reactome.
DR   CDD; cd00959; DeoC; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011343; DeoC.
DR   InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR   PANTHER; PTHR10889; PTHR10889; 1.
DR   Pfam; PF01791; DeoC; 1.
DR   PIRSF; PIRSF001357; DeoC; 1.
DR   SMART; SM01133; DeoC; 1.
DR   TIGRFAMs; TIGR00126; deoC; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Lyase; Nucleus; Reference proteome; Schiff base.
FT   CHAIN           1..318
FT                   /note="Deoxyribose-phosphate aldolase"
FT                   /id="PRO_0000057310"
FT   ACT_SITE        155
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6L0"
FT   ACT_SITE        218
FT                   /note="Schiff-base intermediate with acetaldehyde"
FT                   /evidence="ECO:0000269|PubMed:25229427"
FT   ACT_SITE        254
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000269|PubMed:25229427"
FT   MUTAGEN         218
FT                   /note="K->A: Abolishes deoxyribose-phosphate aldolase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:25229427"
FT   MUTAGEN         254
FT                   /note="K->A: Abolishes deoxyribose-phosphate aldolase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:25229427"
FT   CONFLICT        159
FT                   /note="N -> S (in Ref. 2; BAD96261)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        234
FT                   /note="I -> T (in Ref. 2; BAD96261)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        240
FT                   /note="I -> T (in Ref. 2; BAD96261)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   318 AA;  35231 MW;  E9576567D0E5CBDE CRC64;
     MSAHNRGTEL DLSWISKIQV NHPAVLRRAE QIQARRTVKK EWQAAWLLKA VTFIDLTTLS
     GDDTSSNIQR LCYKAKYPIR EDLLKALNMH DKGITTAAVC VYPARVCDAV KALKAAGCNI
     PVASVAAGFP AGQTHLKTRL EEIRLAVEDG ATEIDVVINR SLVLTGQWEA LYDEIRQFRK
     ACGEAHLKTI LATGELGTLT NVYKASMIAM MAGSDFIKTS TGKETVNATF PVAIVMLRAI
     RDFFWKTGNK IGFKPAGGIR SAKDSLAWLS LVKEELGDEW LKPELFRIGA STLLSDIERQ
     IYHHVTGRYA AYHDLPMS
 
 
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