Alpl
entrez
25586
canonical
uniprot
P08289
canonical
ensembl
ENSRNOG00000013954
resolver
ensembl
ENSRNOG00055024897
resolver
ensembl
ENSRNOG00060029423
resolver
ensembl
ENSRNOG00065024638
resolver
ensp
ENSRNOP00000019004
resolver
ensp
ENSRNOP00055035041
resolver
ensp
ENSRNOP00060042506
resolver
ensp
ENSRNOP00065034613
resolver
enst
ENSRNOT00000019004
resolver
enst
ENSRNOT00055042918
resolver
enst
ENSRNOT00060051094
resolver
enst
ENSRNOT00065042311
resolver
genesymbol
Alpl
resolver
uniprot
P14055
resolver
uniprot
P70707
resolver
uniprot_entry
PPBT_RAT
resolver
uniprot_sec
P14055
resolver
uniprot_sec
P70707
resolver
activity_regulation
ACTIVITY REGULATION: Phosphatase activity is specifically inhibited by 5-((5-chloro-2-methoxyphenyl)sulfonamido)nicotinamide (SBI-425). {ECO:0000250|UniProtKB:P09242}.
uniprot
proteins
amino_acid_sequence
MILPFLVLAIGTCLTNSFVPEKEKDPSYWRQQAQETLKNALKLQKLNTNVAKNIIMFLGDGMGVSTVTAARILKGQLHHNTGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATERTRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAHSADRDWYSDNEMPPEALSQGCKDIAYQLMHNIKDIDVIMGGGRKYMYPKNRTDVEYELDEKARGTRLDGLDLISIWKSFKPRHKHSHYVWNRTELLALDPSRVDYLLGLFEPGDMQYELNRNNLTDPSLSEMVEVALRILTKNPKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDEAIGKAGTMTSQKDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMVSDTDKKPFTAILYGNGPGYKVVDGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFAKGPMAHLLHGVHEQNYIPHVMAYASCIGANLDHCAWASSASSPSPGALLLPLALFPLRTLF
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. 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. 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. 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. 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. 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. Additionally, also able to mediate ATP degradation in a stepwise manner to adenosine, thereby regulating the availability of ligands for purinergic receptors (By similarity). 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. 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 (By similarity). {ECO:0000250|UniProtKB:P05186, ECO:0000250|UniProtKB:P09242}.
uniprot
proteins
mass_dalton
57659
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000250|UniProtKB:P05186}.
uniprot
proteins
protein_family
Alkaline phosphatase family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
2544423
uniprot
proteins
pubmed
2834351
uniprot
proteins
pubmed
2895632
uniprot
proteins
pubmed
32710882
uniprot
proteins
pubmed
3422431
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:32710882}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P09242}. Mitochondrion membrane {ECO:0000250|UniProtKB:P09242}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P09242}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:P09242}. Note=Localizes to special class of extracellular vesicles, named matrix vesicles (MVs), which are released by osteogenic cells (PubMed:32710882). Localizes to the mitochondria of thermogenic fat cells: tethered to mitochondrial membranes via a GPI-anchor and probably resides in the mitochondrion intermembrane space (By similarity). {ECO:0000250|UniProtKB:P09242, ECO:0000269|PubMed:32710882}.
uniprot
proteins