Alpl
entrez
11647
canonical
uniprot
P09242
canonical
ensembl
ENSMUSG00000028766
resolver
ensp
ENSMUSP00000030551
resolver
ensp
ENSMUSP00000218404
resolver
ensp
ENSMUSP00000218407
resolver
ensp
ENSMUSP00000335683
resolver
enst
ENSMUST00000030551
resolver
genesymbol
Alpl
resolver
genesymbol_syn
Akp-2
resolver
genesymbol_syn
Akp2
resolver
uniprot
Q3TQ02
resolver
uniprot
Q6P1B0
resolver
uniprot_entry
PPBT_MOUSE
resolver
uniprot_entry
Q3TQ02_MOUSE
resolver
uniprot_sec
Q6P1B0
resolver
activity_regulation
ACTIVITY REGULATION: Phosphatase activity is specifically inhibited by 5-((5-chloro-2-methoxyphenyl)sulfonamido)nicotinamide (SBI-425). {ECO:0000269|PubMed:29174347, ECO:0000269|PubMed:33981039}.
uniprot
proteins
amino_acid_sequence
MISPFLVLAIGTCLTNSFVPEKERDPSYWRQQAQETLKNALKLQKLNTNVAKNVIMFLGDGMGVSTVTAARILKGQLHHNTGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATERTRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAHSADRDWYSDNEMPPEALSQGCKDIAYQLMHNIKDIDVIMGGGRKYMYPKNRTDVEYELDEKARGTRLDGLDLISIWKSFKPRHKHSHYVWNRTELLALDPSRVDYLLGLFEPGDMQYELNRNNLTDPSLSEMVEVALRILTKNLKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDQAIGKAGAMTSQKDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMVSDTDKKPFTAILYGNGPGYKVVDGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFAKGPMAHLLHGVHEQNYIPHVMAYASCIGANLDHCAWAGSGSAPSPGALLLPLAVLSLRTLF
uniprot
proteins
ec_number
3.1.3.1
uniprot
proteins
ec_number
3.9.1.1
uniprot
proteins
function
FUNCTION: Alkaline phosphatase that metabolizes various phosphate compounds and plays a key role in skeletal mineralization and adaptive thermogenesis (PubMed:10620060, PubMed:11028439, PubMed:14982838, PubMed:23942722, PubMed:33981039). Has broad substrate specificity and can hydrolyze a considerable variety of compounds: however, only a few substrates, such as diphosphate (inorganic pyrophosphate; PPi), pyridoxal 5'-phosphate (PLP) and N-phosphocreatine are natural substrates (PubMed:19874193, PubMed:23942722, PubMed:33981039). Plays an essential role in skeletal and dental mineralization via its ability to hydrolyze extracellular diphosphate, a potent mineralization inhibitor, to phosphate: it thereby promotes hydroxyapatite crystal formation and increases inorganic phosphate concentration (PubMed:10620060, PubMed:11004006, PubMed:11028439, PubMed:12082181, PubMed:14982838, PubMed:32035618, PubMed:9056646). Acts in a non-redundant manner with PHOSPHO1 in skeletal mineralization: while PHOSPHO1 mediates the initiation of hydroxyapatite crystallization in the matrix vesicles (MVs), ALPL/TNAP catalyzes the spread of hydroxyapatite crystallization in the extracellular matrix (PubMed:20684022, PubMed:26457330). Also promotes dephosphorylation of osteopontin (SSP1), an inhibitor of hydroxyapatite crystallization in its phosphorylated state; it is however unclear whether ALPL/TNAP mediates SSP1 dephosphorylation via a direct or indirect manner (PubMed:23427088). Catalyzes dephosphorylation of PLP to pyridoxal (PL), the transportable form of vitamin B6, in order to provide a sufficient amount of PLP in the brain, an essential cofactor for enzymes catalyzing the synthesis of diverse neurotransmitters (PubMed:7550313). Additionally, also able to mediate ATP degradation in a stepwise manner to adenosine, thereby regulating the availability of ligands for purinergic receptors (PubMed:19874193, PubMed:23825434, PubMed:23942722, PubMed:32028019). Also capable of dephosphorylating microbial products, such as lipopolysaccharides (LPS) as well as other phosphorylated small-molecules, such as poly-inosine:cytosine (poly I:C) (By similarity). Acts as a key regulator of adaptive thermogenesis as part of the futile creatine cycle: localizes to the mitochondria of thermogenic fat cells and acts by mediating hydrolysis of N-phosphocreatine to initiate a futile cycle of creatine dephosphorylation and phosphorylation (PubMed:33981039). During the futile creatine cycle, creatine and N-phosphocreatine are in a futile cycle, which dissipates the high energy charge of N-phosphocreatine as heat without performing any mechanical or chemical work (PubMed:33981039). {ECO:0000250|UniProtKB:P05186, ECO:0000269|PubMed:10620060, ECO:0000269|PubMed:11004006, ECO:0000269|PubMed:11028439, ECO:0000269|PubMed:12082181, ECO:0000269|PubMed:14982838, ECO:0000269|PubMed:19874193, ECO:0000269|PubMed:20684022, ECO:0000269|PubMed:23427088, ECO:0000269|PubMed:23825434, ECO:0000269|PubMed:23942722, ECO:0000269|PubMed:26457330, ECO:0000269|PubMed:32028019, ECO:0000269|PubMed:32035618, ECO:0000269|PubMed:33981039, ECO:0000269|PubMed:7550313, ECO:0000269|PubMed:9056646}.
uniprot
proteins
mass_dalton
57514
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000250|UniProtKB:P05186}.
uniprot
proteins
protein_family
Alkaline phosphatase family
uniprot
proteins
pubmed
10620060
uniprot
proteins
pubmed
11004006
uniprot
proteins
pubmed
11028439
uniprot
proteins
pubmed
11169525
uniprot
proteins
pubmed
12082181
uniprot
proteins
pubmed
14982838
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19874193
uniprot
proteins
pubmed
20684022
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
2165496
uniprot
proteins
pubmed
23427088
uniprot
proteins
pubmed
23825434
uniprot
proteins
pubmed
23942722
uniprot
proteins
pubmed
24028588
uniprot
proteins
pubmed
26457330
uniprot
proteins
pubmed
29148101
uniprot
proteins
pubmed
29174347
uniprot
proteins
pubmed
32028019
uniprot
proteins
pubmed
32035618
uniprot
proteins
pubmed
33981039
uniprot
proteins
pubmed
3478679
uniprot
proteins
pubmed
7550313
uniprot
proteins
pubmed
7789278
uniprot
proteins
pubmed
9056646
uniprot
proteins
sequence_length
524
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05186}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P05186}. Extracellular vesicle membrane {ECO:0000269|PubMed:19874193, ECO:0000269|PubMed:23942722}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:33981039}. Mitochondrion membrane {ECO:0000269|PubMed:33981039}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:33981039}. Mitochondrion intermembrane space {ECO:0000269|PubMed:33981039}. Note=Localizes to special class of extracellular vesicles, named matrix vesicles (MVs), which are released by osteogenic cells (PubMed:19874193, PubMed:23942722). Localizes to the mitochondria of thermogenic fat cells: tethered to mitochondrial membranes via a GPI-anchor and probably resides in the mitochondrion intermembrane space (PubMed:33981039). {ECO:0000269|PubMed:19874193, ECO:0000269|PubMed:23942722, ECO:0000269|PubMed:33981039}.
uniprot
proteins