ALDOB_MOUSE
ID ALDOB_MOUSE Reviewed; 364 AA.
AC Q91Y97; Q8K034; Q91W73;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Fructose-bisphosphate aldolase B;
DE EC=4.1.2.13;
DE AltName: Full=Aldolase 2;
DE AltName: Full=Liver-type aldolase;
GN Name=Aldob; Synonyms=Aldo2;
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 [GENOMIC DNA].
RC STRAIN=129/Sv;
RA Funari V.A., Tolan D.R.;
RT "Mouse aldolase B (aldo2) genomic sequence of the open reading frame
RT including first poly A site and signals.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, Kidney, and Liver;
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 PROTEIN SEQUENCE OF 2-12 AND 108-120, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Skeletal muscle;
RA Kanor S., Quadroni M., Bienvenut W.V.;
RL Submitted (MAR-2006) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND THR-39, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; THR-39 AND SER-206, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, and Liver;
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).
RN [6]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-13; LYS-121 AND LYS-317, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-
CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC -!- SUBUNIT: Homotetramer. Interacts with BBS1, BBS2, BBS4 and BBS7.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriolar satellite {ECO:0000250}.
CC -!- MISCELLANEOUS: In vertebrates, 3 forms of this ubiquitous glycolytic
CC enzyme are found, aldolase A in muscle, aldolase B in liver and
CC aldolase C in brain.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
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DR EMBL; AF403567; AAL06323.1; -; Genomic_DNA.
DR EMBL; AF403565; AAL06323.1; JOINED; Genomic_DNA.
DR EMBL; AF403566; AAL06323.1; JOINED; Genomic_DNA.
DR EMBL; BC016435; AAH16435.1; -; mRNA.
DR EMBL; BC022113; AAH22113.1; -; mRNA.
DR EMBL; BC024056; AAH24056.1; -; mRNA.
DR EMBL; BC024112; AAH24112.1; -; mRNA.
DR EMBL; BC026577; AAH26577.1; -; mRNA.
DR EMBL; BC030724; AAH30724.1; -; mRNA.
DR EMBL; BC030725; AAH30725.1; -; mRNA.
DR EMBL; BC034169; AAH34169.1; -; mRNA.
DR EMBL; BC034171; AAH34171.1; -; mRNA.
DR EMBL; BC034172; AAH34172.1; -; mRNA.
DR EMBL; BC034173; AAH34173.1; -; mRNA.
DR EMBL; BC036130; AAH36130.1; -; mRNA.
DR EMBL; BC036131; AAH36131.1; -; mRNA.
DR EMBL; BC036132; AAH36132.1; -; mRNA.
DR EMBL; BC036133; AAH36133.1; -; mRNA.
DR CCDS; CCDS18176.1; -.
DR RefSeq; NP_659152.1; NM_144903.3.
DR AlphaFoldDB; Q91Y97; -.
DR SMR; Q91Y97; -.
DR BioGRID; 230944; 1.
DR STRING; 10090.ENSMUSP00000029987; -.
DR CarbonylDB; Q91Y97; -.
DR iPTMnet; Q91Y97; -.
DR MetOSite; Q91Y97; -.
DR PhosphoSitePlus; Q91Y97; -.
DR SwissPalm; Q91Y97; -.
DR CPTAC; non-CPTAC-3333; -.
DR CPTAC; non-CPTAC-3334; -.
DR jPOST; Q91Y97; -.
DR MaxQB; Q91Y97; -.
DR PaxDb; Q91Y97; -.
DR PeptideAtlas; Q91Y97; -.
DR PRIDE; Q91Y97; -.
DR ProteomicsDB; 285809; -.
DR Antibodypedia; 1025; 416 antibodies from 33 providers.
DR DNASU; 230163; -.
DR Ensembl; ENSMUST00000029987; ENSMUSP00000029987; ENSMUSG00000028307.
DR GeneID; 230163; -.
DR KEGG; mmu:230163; -.
DR UCSC; uc008svw.1; mouse.
DR CTD; 229; -.
DR MGI; MGI:87995; Aldob.
DR VEuPathDB; HostDB:ENSMUSG00000028307; -.
DR eggNOG; KOG1557; Eukaryota.
DR GeneTree; ENSGT00950000182987; -.
DR HOGENOM; CLU_031243_0_0_1; -.
DR InParanoid; Q91Y97; -.
DR OMA; ANCQAAQ; -.
DR OrthoDB; 799973at2759; -.
DR PhylomeDB; Q91Y97; -.
DR TreeFam; TF314203; -.
DR Reactome; R-MMU-70171; Glycolysis.
DR Reactome; R-MMU-70263; Gluconeogenesis.
DR Reactome; R-MMU-70350; Fructose catabolism.
DR UniPathway; UPA00109; UER00183.
DR BioGRID-ORCS; 230163; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Aldob; mouse.
DR PRO; PR:Q91Y97; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q91Y97; protein.
DR Bgee; ENSMUSG00000028307; Expressed in right kidney and 110 other tissues.
DR ExpressionAtlas; Q91Y97; baseline and differential.
DR Genevisible; Q91Y97; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0005815; C:microtubule organizing center; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0030868; C:smooth endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI.
DR GO; GO:0070061; F:fructose binding; ISO:MGI.
DR GO; GO:0061609; F:fructose-1-phosphate aldolase activity; IMP:MGI.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0031210; F:phosphatidylcholine binding; ISO:MGI.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; ISO:MGI.
DR GO; GO:0006001; P:fructose catabolic process; IDA:MGI.
DR GO; GO:0061624; P:fructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate; IMP:MGI.
DR GO; GO:0006000; P:fructose metabolic process; ISO:MGI.
DR GO; GO:0006096; P:glycolytic process; ISO:MGI.
DR GO; GO:0061625; P:glycolytic process through fructose-1-phosphate; IC:MGI.
DR GO; GO:0061615; P:glycolytic process through fructose-6-phosphate; IC:MGI.
DR GO; GO:0006116; P:NADH oxidation; ISO:MGI.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISO:MGI.
DR GO; GO:0043434; P:response to peptide hormone; ISO:MGI.
DR GO; GO:0010043; P:response to zinc ion; ISO:MGI.
DR GO; GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; ISO:MGI.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR029768; Aldolase_I_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000741; FBA_I.
DR PANTHER; PTHR11627; PTHR11627; 1.
DR Pfam; PF00274; Glycolytic; 1.
DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Glycolysis; Lyase; Phosphoprotein; Reference proteome; Schiff base.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3"
FT CHAIN 2..364
FT /note="Fructose-bisphosphate aldolase B"
FT /id="PRO_0000216941"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 230
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT BINDING 56
FT /ligand="substrate"
FT BINDING 147
FT /ligand="substrate"
FT SITE 364
FT /note="Necessary for preference for fructose 1,6-
FT bisphosphate over fructose 1-phosphate"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.3"
FT MOD_RES 13
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 39
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05062"
FT MOD_RES 119
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05062"
FT MOD_RES 121
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05062"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05062"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05062"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00884"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00884"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05062"
FT MOD_RES 317
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 81
FT /note="H -> Y (in Ref. 2; AAH34173)"
FT /evidence="ECO:0000305"
FT CONFLICT 155..156
FT /note="AD -> DH (in Ref. 1; AAL06323)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 364 AA; 39507 MW; E6CD995D0073ED47 CRC64;
MAHRFPALTP EQKKELSEIA QRIVANGKGI LAADESVGTM GNRLQRIKVE NTEENRRQFR
ELLFSVDNSI SQSIGGVILF HETLYQKDSQ GNLFRNVLKE KGIVVGIKLD QGGAPLAGTN
KETTIQGLDG LSERCAQYKK DGVDFGKWRA VLRIADQCPS SLAIQENANA LARYASICQQ
NGLVPIVEPE VLPDGDHDLE HCQYVSEKVL AAVYKALNDH HVYLEGTLLK PNMVTAGHAC
TKKYTPEQVA MATVTALHRT VPAAVPGICF LSGGMSEEDA TLNLNAINRC PLPRPWKLSF
SYGRALQASA LAAWGGKAAN KKATQEAFMK RAMANCQAAQ GQYVHTGSSG AAATQSLFTA
SYTY
