DEOC_MOUSE
ID DEOC_MOUSE Reviewed; 318 AA.
AC Q91YP3; Q3UD33; Q9CZI8;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Deoxyribose-phosphate aldolase;
DE Short=DERA;
DE EC=4.1.2.4 {ECO:0000250|UniProtKB:Q9Y315};
DE AltName: Full=2-deoxy-D-ribose 5-phosphate aldolase;
DE AltName: Full=Phosphodeoxyriboaldolase;
DE Short=Deoxyriboaldolase;
GN Name=Dera;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Heart, Liver, and Placenta;
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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000250|UniProtKB:Q9Y315}.
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:0000250|UniProtKB:Q9Y315};
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:0000250|UniProtKB:Q9Y315}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y315}.
CC Cytoplasmic granule {ECO:0000250|UniProtKB:Q9Y315}. Nucleus
CC {ECO:0000250|UniProtKB:Q9Y315}. Note=Recruited to stress granules but
CC not to processing bodies upon arsenite or clotrimazole treatment or
CC energy deprivation. {ECO:0000250|UniProtKB:Q9Y315}.
CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. DeoC type 2
CC subfamily. {ECO:0000305}.
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DR EMBL; AK083298; BAC38850.1; -; mRNA.
DR EMBL; AK145820; BAE26672.1; -; mRNA.
DR EMBL; AK150273; BAE29429.1; -; mRNA.
DR EMBL; AK150712; BAE29790.1; -; mRNA.
DR EMBL; AK152462; BAE31239.1; -; mRNA.
DR EMBL; AK169418; BAE41164.1; -; mRNA.
DR EMBL; BC016218; AAH16218.1; -; mRNA.
DR CCDS; CCDS20666.1; -.
DR RefSeq; NP_766321.1; NM_172733.1.
DR AlphaFoldDB; Q91YP3; -.
DR SMR; Q91YP3; -.
DR BioGRID; 231264; 1.
DR STRING; 10090.ENSMUSP00000084959; -.
DR iPTMnet; Q91YP3; -.
DR PhosphoSitePlus; Q91YP3; -.
DR SwissPalm; Q91YP3; -.
DR EPD; Q91YP3; -.
DR jPOST; Q91YP3; -.
DR MaxQB; Q91YP3; -.
DR PaxDb; Q91YP3; -.
DR PeptideAtlas; Q91YP3; -.
DR PRIDE; Q91YP3; -.
DR ProteomicsDB; 279341; -.
DR Antibodypedia; 55098; 76 antibodies from 16 providers.
DR DNASU; 232449; -.
DR Ensembl; ENSMUST00000087675; ENSMUSP00000084959; ENSMUSG00000030225.
DR GeneID; 232449; -.
DR KEGG; mmu:232449; -.
DR UCSC; uc009enh.1; mouse.
DR CTD; 51071; -.
DR MGI; MGI:1913762; Dera.
DR VEuPathDB; HostDB:ENSMUSG00000030225; -.
DR eggNOG; KOG3981; Eukaryota.
DR GeneTree; ENSGT00390000007878; -.
DR HOGENOM; CLU_053595_3_0_1; -.
DR InParanoid; Q91YP3; -.
DR OMA; LTGQWEX; -.
DR OrthoDB; 1349979at2759; -.
DR PhylomeDB; Q91YP3; -.
DR TreeFam; TF314251; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-71336; Pentose phosphate pathway.
DR UniPathway; UPA00002; UER00468.
DR BioGRID-ORCS; 232449; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Dera; mouse.
DR PRO; PR:Q91YP3; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q91YP3; protein.
DR Bgee; ENSMUSG00000030225; Expressed in dorsal pancreas and 200 other tissues.
DR ExpressionAtlas; Q91YP3; baseline and differential.
DR Genevisible; Q91YP3; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0004139; F:deoxyribose-phosphate aldolase activity; ISO:MGI.
DR GO; GO:0016052; P:carbohydrate catabolic process; IBA:GO_Central.
DR GO; GO:0046121; P:deoxyribonucleoside catabolic process; ISO:MGI.
DR GO; GO:0009264; P:deoxyribonucleotide catabolic process; IBA:GO_Central.
DR GO; GO:0046386; P:deoxyribose phosphate catabolic process; IEA:UniProtKB-UniPathway.
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_0000057311"
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:0000250|UniProtKB:Q9Y315"
FT ACT_SITE 254
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9Y315"
SQ SEQUENCE 318 AA; 34975 MW; 1C7DE27CF423816F CRC64;
MAAHCRGTEL DLSWISKVQV NHAAVLRRAQ QIQARRSVKK EWQAAWLLKA VTFIDLTTLS
GDDTFSNVQR LCYKAKYPIR ADLLKALNMD DKGITTAAVC VYPARVCDAV KALKAAGCSI
PVASVATGFP AGQTHLKTRL EEIRLAVEDG ATEIDVVINR TLVLTGQWEA LYDEVTQFRK
ACGEAHLKTI LATGELGSLT NVYKASLVAM MAGSDFIKTS TGKETVNATF PVAIVMLRAI
RDFFWKTGNK VGFKPAGGIR TAKESLAWLS LVKEELGDEW LTPDLFRIGA SSLLSDIERQ
IYHHVTGRYA AYHDLPMS
