Aldoa
entrez
11674
canonical
uniprot
P05064
canonical
ensembl
ENSMUSG00000030695
resolver
ensp
ENSMUSP00000032934
resolver
ensp
ENSMUSP00000084846
resolver
ensp
ENSMUSP00000101955
resolver
ensp
ENSMUSP00000202008
resolver
enst
ENSMUST00000032934
resolver
enst
ENSMUST00000087566
resolver
enst
ENSMUST00000106348
resolver
genesymbol
Aldoa
resolver
genesymbol_syn
Aldo1
resolver
uniprot
A6ZI44
resolver
uniprot
F6RLS4
resolver
uniprot
Q5FWB7
resolver
uniprot_entry
A6ZI44_MOUSE
resolver
uniprot_entry
ALDOA_MOUSE
resolver
uniprot_entry
F6RLS4_MOUSE
resolver
uniprot_entry
Q5FWB7_MOUSE
resolver
amino_acid_sequence
MPHPYPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACTQKFSNEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYIKRALANSLACQGKYTPSGQSGAAASESLFISNHAY
uniprot
proteins
ec_number
4.1.2.13
uniprot
proteins
function
FUNCTION: Catalyzes the reversible conversion of beta-D-fructose 1,6-bisphosphate (FBP) into two triose phosphate and plays a key role in glycolysis and gluconeogenesis (PubMed:40446798). In addition, also functions as a scaffolding protein (PubMed:28723898, PubMed:31204282). In response to glucose deprivation, FBP dissociates from aldolase and acts as an adapter that promotes AMP-activated protein kinase (AMPK) activity: mechanistically, associates with transient receptor potential channels TrpV (TRPV1-TRPV4), promoting inhibition of the V-ATPase complex on lysosomes and AMPK activation via the AXIN1-STK11/LKB1 axis (PubMed:28723898, PubMed:31204282). {ECO:0000269|PubMed:28723898, ECO:0000269|PubMed:31204282, ECO:0000269|PubMed:40446798}.
uniprot
proteins
mass_dalton
39356
uniprot
proteins
mutagenesis
MUTAGEN 34; /note="D->S: Strongly reduced conversion of beta-D-fructose 1,6-bisphosphate (FBP) into dihydroxyacetone phosphate, leading to accumulation of FBP in the active site. Abolished ability to activate AMPK in response to glusoce deprivation."; /evidence="ECO:0000269|PubMed:28723898"; MUTAGEN 39; /note="S->A: Decreased glycolysis."; /evidence="ECO:0000269|PubMed:40446798"; MUTAGEN 39; /note="S->E: Mimics phosphorylation; increased glycolysis."; /evidence="ECO:0000269|PubMed:40446798
uniprot
proteins
pathway_participation
PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Ser-39 in response to beta-arrestin-1 (ARRB1) signaling, promoting the fructose-bisphosphate aldolase activity, leading to enhanced glycolysis and improved glucose tolerance. {ECO:0000269|PubMed:40446798}.
uniprot
proteins
protein_family
Class I fructose-bisphosphate aldolase family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
2365699
uniprot
proteins
pubmed
28723898
uniprot
proteins
pubmed
3009179
uniprot
proteins
pubmed
31204282
uniprot
proteins
pubmed
3697100
uniprot
proteins
pubmed
40446798
uniprot
proteins
sequence_length
364
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, I band {ECO:0000250|UniProtKB:P00883}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000250|UniProtKB:P00883}. Note=In skeletal muscle, accumulates around the M line and within the I band, colocalizing with FBP2 on both sides of the Z line in the absence of Ca(2+). {ECO:0000250|UniProtKB:P00883}.
uniprot
proteins