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A0A452SC01 · A0A452SC01_URSAM

Function

Catalytic activity

  • ADP + H2O = AMP + phosphate + H+
    This reaction proceeds in the forward direction.
  • AMP + H2O = adenosine + phosphate
    This reaction proceeds in the forward direction.
  • ATP + H2O = ADP + phosphate + H+
    This reaction proceeds in the forward direction.
  • N-phosphocreatine + H2O = creatine + phosphate
    This reaction proceeds in the forward direction.
    EC:3.9.1.1 (UniProtKB | ENZYME | Rhea)
  • phosphoethanolamine + H2O = ethanolamine + phosphate
    This reaction proceeds in the forward direction.
  • pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate
    This reaction proceeds in the forward direction.
  • a phosphate monoester + H2O = an alcohol + phosphate
    This reaction proceeds in the forward direction.
    EC:3.1.3.1 (UniProtKB | ENZYME | Rhea)
  • diphosphate + H2O = 2 phosphate + H+
    This reaction proceeds in the forward direction.

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion.
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 2 Zn2+ ions.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site60Mg2+ (UniProtKB | ChEBI)
Binding site60Zn2+ 2 (UniProtKB | ChEBI)
Active site110Phosphoserine intermediate
Binding site171Mg2+ (UniProtKB | ChEBI)
Binding site173Mg2+ (UniProtKB | ChEBI)
Binding site332Mg2+ (UniProtKB | ChEBI)
Binding site337Zn2+ 2 (UniProtKB | ChEBI)
Binding site341Zn2+ 2 (UniProtKB | ChEBI)
Binding site378Zn2+ 2 (UniProtKB | ChEBI)
Binding site379Zn2+ 2 (UniProtKB | ChEBI)
Binding site454Zn2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmitochondrial intermembrane space
Cellular Componentmitochondrial membrane
Cellular Componentplasma membrane
Cellular Componentside of membrane
Molecular FunctionADP phosphatase activity
Molecular Functionalkaline phosphatase activity
Molecular FunctionATP hydrolysis activity
Molecular Functioncalcium ion binding
Molecular Functioninorganic diphosphate phosphatase activity
Molecular Functionphosphoamidase activity
Molecular Functionphosphoethanolamine phosphatase activity
Molecular Functionpyridoxal phosphatase activity
Biological Processcalcium ion homeostasis
Biological Processdephosphorylation
Biological Processresponse to vitamin D

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Alkaline phosphatase
  • EC number

Gene names

    • Name
      ALPL

Organism names

Accessions

  • Primary accession
    A0A452SC01

Proteomes

Subcellular Location

Cell membrane
; Lipid-anchor, GPI-anchor
Extracellular vesicle membrane
; Lipid-anchor, GPI-anchor
Mitochondrion membrane
; Lipid-anchor, GPI-anchor

Keywords

PTM/Processing

Features

Showing features for signal, chain.

Type
IDPosition(s)Description
Signal1-17
ChainPRO_501952955218-524Alkaline phosphatase

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the alkaline phosphatase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    524
  • Mass (Da)
    57,484
  • Last updated
    2019-05-08 v1
  • MD5 Checksum
    4C94898A131B6202180E3B6A2A050010
MISLFLVLAVGTCLTNSFVPEKEKDPKYWRDQAQQTLKYALRLQKLNTNVAKNVIMFLGDGMGVSTVTATRILKGQLHHNPGEETRLEMDKFPYVALSKTYNTNAQVPDSAGTATAYLCGVKANEGTVGVSAATQRSQCNTTQGNEVTSILHWAKDAGKSVGIVTTTRVNHATPSAAYAHSADRDWYSDNEMPPEALRQGCKDIAYQLMHNVKDIEVIMGGGRKYMFPKNRTDVEYEMDEKSRGTRLDGLNLIDTWKSFKPRHKHSHYVWNRTELLTLDPHTVDYLLGLFEPGDLQYELNRNNTTDPSLSEMVEVAVKILSKNPKGFFLLVEGGRIDHGHHEGKAKLALHEAVEMDRAIGKAGTMTSLEDTLTIVTADHSHVFTFGGYTPRGNSIFGLAPMVSDTDNKPFTAILYGNGPGYKVVGGERENIYTVDYAHSNYQAQSAVPLRYETHGGEDVAVFAKGPMAHLLHGVHEQNYIAHVMAYAACVGANQDHCASASSAGGPSPGPLLLLLTLLPLGTLF

Keywords

Genome annotation databases

Similar Proteins

Disclaimer

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