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Information on EC 3.1.3.2 - acid phosphatase and Organism(s) Mus musculus and UniProt Accession Q05117
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3.1.3.2 acid phosphataseIUBMB Comments
Wide specificity. Also catalyses transphosphorylations.
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Word Map
- 3.1.3.2
- osteoclast
- lysosomal
- resorption
- marrow
-
cytochemical
- rankl
-
osteoclastogenesis
- cathepsin
-
multinucleated
- collagen
- osteoporosis
- granule
- beta-glucuronidase
- osteocalcin
- lymphocyte
- monocyte
-
prostate-specific
- osteoprotegerin
-
histochemistry
- periodontal
- metastases
- phosphorus
- phagocytic
- alveolar
-
trabecular
-
seminal
-
rankl-induced
- parathyroid
-
ovariectomized
- tibia
- femur
-
cytochemistry
-
lumbar
- osteolysis
- nfatc1
-
resorb
- tooth
- calcitonin
- m-csf
-
dentin
- calvaria
-
bone-specific
-
orthodontic
-
telopeptide
-
postmenopausal
-
histomorphometric
-
micro-ct
-
micro-computed
- medicine
- synthesis
- molecular biology
- phytase
- diagnostics
-
n-acetyl-beta-d-glucosaminidase
- biotechnology
- agriculture
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
acid phosphatase, tartrate-resistant acid phosphatase, prostatic acid phosphatase, tracp, acpase, uteroferrin, tracp 5b, phosphatidic acid phosphatase, tracp5b, pp2a phosphatase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acid monophosphatase
-
-
-
-
acid nucleoside diphosphate phosphatase
-
-
-
-
Acid phosphatase PII
-
-
-
-
acid phosphohydrolase
-
-
-
-
acid phosphomoesterase
-
-
-
-
acid phosphomonoester hydrolase
-
-
-
-
ACP1
-
-
-
-
AcPase
-
-
-
-
Adipocyte acid phosphatase, isozyme alpha
-
-
-
-
Adipocyte acid phosphatase, isozyme beta
-
-
-
-
APase
-
-
-
-
APASE6
-
-
-
-
glycerophosphatase
-
-
-
-
HPAP
-
-
-
-
LAP
-
-
-
-
Low molecular weight phosphotyrosine protein phosphatase
-
-
-
-
Minor phosphate-irrepressible acid phosphatase
-
-
-
-
NSAP
-
-
-
-
P56
-
-
-
-
P60
-
-
-
-
PAP
-
-
-
-
pH 2.5 acid phosphatase
-
-
-
-
pH 6-optimum acid phosphatase
-
-
-
-
phosphomonoesterase
-
-
-
-
Stationary-phase survival protein surE
-
-
-
-
Tartrate-resistant acid ATPase
-
-
-
-
TR-AP
-
-
-
-
TrATPase
-
-
-
-
uteroferrin
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
SYSTEMATIC NAME
IUBMB Comments
phosphate-monoester phosphohydrolase (acid optimum)
Wide specificity. Also catalyses transphosphorylations.
CAS REGISTRY NUMBER
COMMENTARY
9001-77-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
6,8-difluoro-4-methylumbelliferyl phosphate + H2O
6,8-difluoro-4-methylumbelliferone + phosphate
-
-
-
?
AMP + H2O
adenosine + phosphate
at neutral pH: to a lesser extent also ATP is dephosphorylated, at pH 5.6: also ADP, and to a lesser extent ATP are dephosphorylated
-
-
?
additional information
?
-
ACP5 possesses a central role in removal of the mannose 6-phosphate recognition marker
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
ACP5 possesses a central role in removal of the mannose 6-phosphate recognition marker
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4'-O-(2-fluoromalonyl)-L-tyrosine-containing peptides
-
inhibitory potency, overview
phospho-L-tyrosine peptide analogues
-
inhibitory potency of several Fmoc-O,O-tert-butyl phospho-L-tyrosine analogue peptides, overview
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
the enzyme is widely expressed in many tissues, where it is associated with cells principally originating from the bone marrow, including those of osteoclast/macrophage lineage
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PPA5_MOUSE
327
0
36807
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
analysis of ACP5-deficient mice reveals that levels of mannose 6-phosphate glycoproteins are highly elevated in tissues that normally express ACP5, and this results from a failure to dephosphorylate lysosomal proteins
additional information
overexpression of ACP5 in N1E-115 neuroblastoma cells leads to an increased dephosphorylation of mannose 6-phosphate glycoproteins
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Spodopetra frugiperda Sf9 cells using the baculovirus infection system
-
His-tagged variant expressed in Hi5 insect cells using a baculovirus expression system
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
molecular biology
ACP5 possesses a central role in removal of the mannose 6-phosphate recognition marker
diagnostics
-
the tartrate-resistant acid phosphatase is a histochemical marker of the osteoclast. It is also characteristic of monohistiocytes, particularly alveolar macrophages, and is associated with diverse pathological conditions, including hairy cell leukemia and AIDS encephalopathy
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hollander, V.P.
Acid phosphatases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
4
449-498
1971
Bos taurus, Saccharomyces cerevisiae, Chaos carolinense, Drosophila melanogaster, Escherichia coli, Homo sapiens, Lupinus luteus, Staphylococcus aureus, Mus musculus, Neurospora crassa, Nicotiana tabacum, Rattus norvegicus, Saccharomyces mellis, Staphylococcus aureus PS 55
-
Hayman, A.R.; Bune, A.J.; Bradley, J.R.; Rashbass, J.; Cox, T.M.
Osteoclastic tartrate-resistant acid phosphatase (Acp 5): its localization to dendritic cells and diverse murine tissues
J. Histochem. Cytochem.
48
219-228
2000
Mus musculus
Valizadeh, M.; Schenk, G.; Nash, K.; Oddie, G.W.; Guddat, L.W.; Hume, D.A.; de Jersey, J.; Burke, T.R.; Hamilton, S.
Phosphotyrosyl peptides and analogues as substrates and inhibitors of purple acid phosphatases
Arch. Biochem. Biophys.
424
154-162
2004
Homo sapiens, Ipomoea batatas, Mus musculus, Phaseolus vulgaris, Sus scrofa (P09889)
Sun, P.; Sleat, D.E.; Lecocq, M.; Hayman, A.R.; Jadot, M.; Lobel, P.
Acid phosphatase 5 is responsible for removing the mannose 6-phosphate recognition marker from lysosomal proteins
Proc. Natl. Acad. Sci. USA
105
16590-16595
2008
Mus musculus (Q05117)
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