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 27-MAR-2024, entry version 177.
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; 48.
DR IntAct; Q9Y315; 15.
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 CPTAC; CPTAC-2724; -.
DR EPD; Q9Y315; -.
DR jPOST; Q9Y315; -.
DR MassIVE; Q9Y315; -.
DR MaxQB; Q9Y315; -.
DR PaxDb; 9606-ENSP00000416583; -.
DR PeptideAtlas; Q9Y315; -.
DR ProteomicsDB; 85959; -.
DR Pumba; Q9Y315; -.
DR Antibodypedia; 55098; 91 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 AGR; HGNC:24269; -.
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; 1330179at2759; -.
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; 11 hits in 1150 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 205 other cell types or 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; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011343; DeoC.
DR InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR NCBIfam; TIGR00126; deoC; 1.
DR PANTHER; PTHR10889; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1.
DR PANTHER; PTHR10889:SF3; DEOXYRIBOSE-PHOSPHATE ALDOLASE; 1.
DR Pfam; PF01791; DeoC; 1.
DR PIRSF; PIRSF001357; DeoC; 1.
DR SMART; SM01133; DeoC; 1.
DR SUPFAM; SSF51569; Aldolase; 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
//
