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Information on EC 3.1.3.74 - pyridoxal phosphatase and Organism(s) Homo sapiens and UniProt Accession Q8TCD6
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3.1.3.74 pyridoxal phosphataseIUBMB Comments
Requires Mg2+. This enzyme is specific for phosphorylated vitamin B6 compounds: it acts not only on pyridoxal phosphate (PLP), but also on pyridoxine phosphate (PNP), pyridoxamine phosphate (PMP), 4-pyridoxic acid phosphate and 4-deoxypyridoxine phosphate. This reaction can also be carried out by EC 3.1.3.1 (alkaline phosphatase) and EC 3.1.3.2 (acid phosphatase), but these enzymes have very broad substrate specificities.
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Word Map
- 3.1.3.74
- phosphatases
-
vitamer
- drug development
-
dehalogenase
-
haloacid
-
actin-depolymerizing
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
plpp/cin, plp phosphatase, pyridoxal phosphatase, pyridoxal phosphate phosphatase, plpase, pyridoxine phosphate phosphatase, pyridoxal-5'-phosphate phosphatase, pyridoxal-5'-phosphate phosphatase/chronophin, pnp phosphatase, pyridoxine 5'-phosphate phosphatase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
pyridoxal-5'-phosphate phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
pyridoxal-5'-phosphate phosphohydrolase
Requires Mg2+. This enzyme is specific for phosphorylated vitamin B6 compounds: it acts not only on pyridoxal phosphate (PLP), but also on pyridoxine phosphate (PNP), pyridoxamine phosphate (PMP), 4-pyridoxic acid phosphate and 4-deoxypyridoxine phosphate. This reaction can also be carried out by EC 3.1.3.1 (alkaline phosphatase) and EC 3.1.3.2 (acid phosphatase), but these enzymes have very broad substrate specificities.
CAS REGISTRY NUMBER
COMMENTARY
9076-92-0
-
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
N-(5'-phospho-4'-pyridoxyl)benzylamine + H2O
4'-pyridoxylbenzylamine + phosphate
-
-
-
-
?
N-(5'-phospho-4'-pyridoxyl)ethanolamine + H2O
4'-pyridoxylethanolamine + phosphate
-
-
-
-
?
N-(5'-phospho-4'-pyridoxyl)glycine + H2O
4'-pyridoxylglycine + phosphate
-
-
-
-
?
N-(5'-phospho-4'-pyridoxyl)phenylalanine + H2O
4'-pyridoxylphenylalanine + phosphate
-
much higher catalytic efficiency than with pyridoxine 5-phosphate
-
-
?
4-pyridoxic acid 5'-phosphate + H2O
4-pyridoxic acid + phosphate
-
highest catalytic efficiency with 4-pyridoxic acid 5-phosphate and pyridoxal 5-phosphate
-
-
?
4-pyridoxic acid 5'-phosphate + H2O
4-pyridoxic acid + phosphate
-
the catalytic efficiency decreases in the following order: pyridoxal 5-phosphate, 4-pyridoxic acid 5-phosphate, pyridoxine 5-phosphate and pyridoxamine 5-phosphate
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
enzyme probably plays an important role in the hydrolysis of pyridoxal 5-phosphate to pyridoxal in erythrocytes, may be important in the regulation of pyridoxal 5-phosphate concentration
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
best substrate, a cysteinyl residue at or near the active site is essential for activity, there may be only one free Cys per subunit
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
highest catalytic efficiency with pyridoxal 5-phosphate and 4-pyridoxic acid 5-phosphate
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
highest specificity constant followed by pyridoxine 5-phosphate
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
kinetic mechanism, random binding of pyridoxal phosphate and Mg2+, formation of a dead-end complex of phosphate with the enzyme-Mg complex
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
mechanism, a covalent phosphoenzyme intermediate is formed during catalysis, may be an acylphosphate intermediate
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
the catalytic efficiency decreases in the following order: pyridoxal 5-phosphate, 4-pyridoxic acid 5-phosphate, pyridoxine 5-phosphate and pyridoxamine 5-phosphate
-
-
?
pyridoxamine 5'-phosphate + H2O
pyridoxamine + phosphate
-
low hydrolysis rate
-
-
?
pyridoxamine 5'-phosphate + H2O
pyridoxamine + phosphate
-
the catalytic efficiency decreases in the following order: pyridoxal 5-phosphate, 4-pyridoxic acid 5-phosphate, pyridoxine 5-phosphate and pyridoxamine 5-phosphate
-
-
?
pyridoxine 5'-phosphate + H2O
pyridoxine + phosphate
-
-
-
-
?
pyridoxine 5'-phosphate + H2O
pyridoxine + phosphate
second highest specificity constant after pyridoxal 5-phosphate
-
-
?
pyridoxine 5'-phosphate + H2O
pyridoxine + phosphate
-
the catalytic efficiency decreases in the following order: pyridoxal 5-phosphate, 4-pyridoxic acid 5-phosphate, pyridoxine 5-phosphate and pyridoxamine 5-phosphate
-
-
?
additional information
?
-
-
probably plays an important role in the regulation of vitamin B6 metabolism
-
-
?
additional information
?
-
vitamin B6 metabolism, catabolism of pyridoxal 5-phosphate
-
-
?
additional information
?
-
-
vitamin B6 metabolism, catabolism of pyridoxal 5-phosphate
-
-
?
additional information
?
-
-
enzyme has phosphotransferase activity and transfers 20-25% of the phosphoryl group from either substrate to ethanol
-
-
?
additional information
?
-
-
hydrolyzes ten organic phosphates, but has maximum activity against pyridoxal phosphate
-
-
?
additional information
?
-
-
specifically dephosphorylates vitamin B6-phosphates, not: phenylphosphate, nucleotide phosphates, such as ATP, ADP, AMP, cAMP, FMN, phosphoamino acids, such as phosphoserine, phosphothreonine, phosphotyrosine, phosphoglycolate
-
-
?
additional information
?
-
-
specificity and active site properties, enzyme also catalyzes the dephosphorylation of 4-secondary amine derivatives of vitamin B6 phosphate, enzyme has the greatest catalytic efficiency with substrates that contain a negatively charged group on the 4-position of the pyridine ring, one or two positively charged groups at the active site of enzyme interacts with the substrates phosphate ester and 4-substituent, Arg and His residues are at or near the active site and may play roles in substrate binding and/or catalysis, very low activity with p-nitrophenylphosphate
-
-
?
additional information
?
-
very low activity with with p-nitrophenyl phosphate
-
-
?
additional information
?
-
-
very low activity with with p-nitrophenyl phosphate
-
-
?
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
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
-
enzyme probably plays an important role in the hydrolysis of pyridoxal 5-phosphate to pyridoxal in erythrocytes, may be important in the regulation of pyridoxal 5-phosphate concentration
-
-
?
additional information
?
-
-
probably plays an important role in the regulation of vitamin B6 metabolism
-
-
?
additional information
?
-
vitamin B6 metabolism, catabolism of pyridoxal 5-phosphate
-
-
?
additional information
?
-
-
vitamin B6 metabolism, catabolism of pyridoxal 5-phosphate
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Zn2+
-
activates somewhat at low concentrations, inhibits at higher concentrations
additional information
Mg2+
requirement for a divalent cation, Mg2+ is most effective in catalyzing the dephosphorylation of pyridoxal 5-phosphate
Mg2+
-
similar activation as by Co2+ and Ni2+, kinetics, probably the physiological activator
Mn2+
-
less activatory than Mg2+, Co2+ or Ni2+, inhibits above 0.05 mM, kinetics
additional information
-
not activated by 100 mM NaCl, KCl, NaBr, NaI, NaNO3 or sodium acetate
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-pyridoxic acid 5'-phosphate
-
very effective inhibitor, 0.02 mM, 50% inhibition of pyridoxine 5-phosphate hydrolysis
5,5'-dithiobis(2-nitrobenzoic acid)
-
50 nM, 50% inhibition, incorporation of 1 mol per mol of subunit leads to complete inactivation, phosphate or dithiothreitol protects
disulfide reagent
-
reactivation by excess dithiothreitol, inactivation is due to formation of a mixed disulfide between the reagent and a free cysteinyl residue at or near the active site of enzyme
-
EDTA
-
0.2 mM, complete inhibition in the absence of Mg2+, 50% inhibition in the presence of 1 mM Mg2+
p-nitrophenyl phosphate
-
poor, 4 mM, 50% inhibition of pyridoxine 5-phosphate hydrolysis
pyridoxal
-
weak, 11 mM, 50% inhibition of hydrolysis of pyridoxal 5-phosphate or pyridoxine 5-phosphate
pyridoxal 5'-phosphate
-
very effective inhibitor, 0.03 mM, 50% inhibition of pyridoxine 5-phosphate hydrolysis
pyridoxamine 5'-phosphate
-
0.5 mM, 50% inhibition of pyridoxine 5-phosphate hydrolysis, less effective than pyridoxal 5-phosphate or 4-pyridoxic acid 5-phosphate
Tetranitromethane
-
inactivates in a time-dependent manner, 10 mM, 70% inhibition in the absence of pyridoxal 5-phosphate and 30% in the presence of 0.15 mM pyridoxal 5-phosphate
thiol-specific reagent
-
a variety of thiol-specific reagents inactivate in a time- and concentration-dependent manner, pyridoxal phosphate or phosphate protects
-
2-ethyl-5-phenylisoxazolium-3'-sulfonate
-
0.25 mM, 5 min at 22°C, 60% loss of activity, inactivates in a concentration- and time-dependent manner, which follows pseudo-first-order kinetics, pyridoxal 5-phosphate, pyridoxine 5-phosphate or phosphate protects
diethyldicarbonate
-
inactivates by reacting with a group with a pKalpha of 6.7, kinetics, pyridoxine 5-phosphate protects, 100 mM neutral hydroxylamine partially reactivates
iodoacetate
-
0.075 mM, 50% inhibition, incorporation of 0.6 mol per mol of subunit leads to complete inactivation, phosphate protects, inhibition kinetics
N-ethylmaleimide
-
inactivated by low concentrations, low concentrations of a substrate, pyridoxine phosphate, or phosphate protect from inactivation, inhibition is not potentiated by MgCl2
N-ethylmaleimide
-
0.1 mM, 50% inhibition, incorporation of 0.6 mol per mol of subunit leads to complete inactivation, inhibition kinetics, phosphate protects
Phenylglyoxal
-
the incorporation of 1 mol per subunit inactivates, pyridoxal 5-phosphate protects, kinetics
phosphate
-
competitive inhibitor with respect to pyridoxine 5-phosphate, product inhibition
Zn2+
-
inhibits at higher concentrations, activates somewhat at low concentrations
Zn2+
-
very potent inhibitor, 50% inhibition in the presence of MgCl2 by 0.01 mM ZnCl2
additional information
-
not inhibited by nucleotide phosphates, phosphoamino acids, levamisole, L-phenylalanine, L(+)-tartrate, 5 mM ATP, 5 mM phosphoglycolate, 0.5 mM alpha- or beta-glycerophosphate, 0.5 mM 3-phosphoglycerate, 0.5 mM 2,3-bisphosphoglycerate, 5 mM pyridoxine, 5 mM pyridoxamine, 5 mM 4-pyridoxic acid, 5 mM 4-pyridine-carboxaldehyde, 5 mM isonicotinate, 5 mM 3-hydroxypyridine, 5 mM salicylaldehyde, 5 mM benzaldehyde
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetic data, effect of pH on Km for 4-pyridoxic acid 5-phosphate, pyridoxal 5-phosphate, pyridoxine 5-phosphate and pyridoxamine 5-phosphate
-
additional information
additional information
-
kinetic mechanism, kinetic properties
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.4
additional information
1.4
pH 7.4, 37°C, hydrolysis of pyridoxal 5-phosphate, recombinant enzyme
additional information
crude extract contains 0.13 units/mg, purified PEP-1-PLPP fusion protein contains 1.5 units/mg, after purification of recombinant enzyme, pH 7.4 in 40 mM triethanolamineamine-HCl, measuring absorbance reduction at 390 nm (3 min)
additional information
-
crude extract contains 0.13 units/mg, purified PEP-1-PLPP fusion protein contains 1.5 units/mg, after purification of recombinant enzyme, pH 7.4 in 40 mM triethanolamineamine-HCl, measuring absorbance reduction at 390 nm (3 min)
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
additional information
-
alkaline and acid pyridoxal phosphate phosphatase, not identical with alkaline and acid phosphatase
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
highly abundant in, most highly represented in all the regions of central nerve system except the spinal cord
additional information
mRNA is differentially expressed in a tissue-specific manner, tissue distribution
additional information
-
mRNA is differentially expressed in a tissue-specific manner, tissue distribution
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
subcellular localization in polymorphonuclear leukocytes
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
PDXP transgenic mice have immature spines with small heads, while PDXP knockout mice have gigantic spines. PDXP transgenic mice exhibit enhanced synaptic plasticity, while knockout mice show abnormal synaptic plasticity. PDXP also enhances N-methyl-D-aspartate receptor (GluN) functionality by regulating the coupling of GluN2A with interacting proteins, particularly postsynaptic density-95
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). PHOP2_HUMAN
241
0
27769
Swiss-Prot
other Location (Reliability: 3)
PLPP_HUMAN
296
0
31698
Swiss-Prot
other Location (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
31698
2 * 31698, sequence calculation, 2 * 32000, recombinant enzyme, SDS-PAGE
32000
33000
64000
32000
2 * 31698, sequence calculation, 2 * 32000, recombinant enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
2 * 31698, sequence calculation, 2 * 32000, recombinant enzyme, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
purified enzyme is unstable at low protein concentration, 0.002% Triton X-100 stabilizes, enzyme is unstable to freezing in the absence of glycerol
-
recombinant PEP-1-PLPP fusion protein transduced into PC12 cells is stable for 36 h
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, storage at concentrations of 0.3 mg/ml or greater, 30 mM phosphate, at least 6 months, stable
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-affinity chromatography
sonication of cells in binding buffer (5 mM imidazole, 0.5 M NaCl, 20 mM Tris-HCl, pH 7.9), centrifugation, Ni2+-nitrilotriacetic acid Sepharose affinity column, salt removed with PD10 column
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA, from brain, expression in Escherichia coli M15/pRER4, sequencing, ORF is located on chromosome 22q12.3, genomic organization
cloned into plasmid pET15b, expression in Escherichi coli BL21 (DE3) as His-tag fusion protein
-
PLPP gene fused with a PEP-1 peptide (PEP-1-PLPP) and 6His-tag and cloned into pET-15b. Expression in Escherichia coli BL21 (DE3) transduced into PC12 cells at various times and concentrations to evaluate the transduction ability (analyzed by Western blotting, fluorescence labeled). PLP concentration in cells PC12 cells changed by transduced PEP-1-PLPP fusion protein (spectroscopic measurement)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
lactoferrin activates expression of PDXP, which significantly up-regulates the synthesis of vitamin B6 and the phosphoinositide 3-kinase/serine/threonine-protein kinase/extracellular regulated protein kinases 1/2 pathway
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
transduction of the PEP-1-PLPP fusion protein into cells would be useful as therapeutic agent for various disorders related to this enzyme and vitamin B6
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gao, G.J.; Fonda, M.L.
Evidence for a phosphoenzyme intermediate formed during catalysis by pyridoxal phosphatase from human erythrocytes
Arch. Biochem. Biophys.
313
166-172
1994
Homo sapiens
Fonda, M.L.; Zhang, Y.N.
Kinetic mechanism and divalent metal activation of human erythrocyte pyridoxal phosphatase
Arch. Biochem. Biophys.
320
345-352
1995
Homo sapiens
Smith, G.P.; Peters, T.J.
Subcellular localization and properties of pyridoxal phosphate phosphatases of human polymorphonuclear leukocytes and their relationship to acid and alkaline phosphatase
Biochim. Biophys. Acta
661
287-294
1981
Homo sapiens
Fonda, M.L.
Purification and characterization of vitamin B6-phosphate phosphatase from human erythrocytes
J. Biol. Chem.
267
15978-15983
1992
Homo sapiens
Gao, G.J.; Fonda, M.L.
Kinetic analysis and chemical modification of vitamin B6 phosphatase from human erythrocytes
J. Biol. Chem.
269
7163-7168
1994
Homo sapiens
Gao, G.J.; Fonda, M.L.
Identification of an essential cysteine residue in pyridoxal phosphatase from human erythrocytes
J. Biol. Chem.
269
8234-8239
1994
Homo sapiens
Jang, Y.M.; Kim, D.W.; Kang, T.C.; Won, M.H.; Baek, N.I.; Moon, B.J.; Choi, S.Y.; Kwon, O.S.
Human pyridoxal phosphatase. Molecular cloning, functional expression, and tissue distribution
J. Biol. Chem.
278
50040-50046
2003
Homo sapiens (Q96GD0), Homo sapiens, Mus musculus (P60487), Mus musculus
Saraswathi, S.; Bachhawat, B.K.
Phosphatases from human brain. I. Purification and properties of pyridoxal phosphate phosphatase
J. Neurochem.
10
127-133
1963
Homo sapiens
Boe, A.S.; Bredholt, G.; Knappskog, P.M.; Storstein, A.; Vedeler, C.A.; Husebye, E.S.
Pyridoxal phosphatase is a novel cancer autoantigen in the central nervous system
Br. J. Cancer
91
1508-1514
2004
Homo sapiens (Q96GD0), Homo sapiens
Kim, D.W.; Eum, W.S.; Choi, H.S.; Kim, S.Y.; An, J.J.; Lee, S.H.; Sohn, E.J.; Hwang, S.I.; Kwon, O.S.; Kang, T.C.; Won, M.H.; Cho, S.W.; Lee, K.S.; Park, J.; Choi, S.Y.
Human brain pyridoxal-5'-phosphate phosphatase: production and characterization of monoclonal antibodies
J. Biochem. Mol. Biol.
38
703-708
2005
Bos taurus, Brachylagus idahoensis, Canis lupus familiaris, Felis catus, Gallus gallus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
Afjehi-Sadat, L.; Yang, J.W.; Pollak, A.; Kim, D.W.; Choi, S.Y.; Lubec, G.
Structural and functional analysis of hypothetical proteins in mouse hippocampus from two-dimensional gel electrophoresis
J. Proteome Res.
6
711-723
2007
Homo sapiens (Q96GD0), Mus musculus (Q8CHP8), Mus musculus
Lee, Y.P.; Kim, D.W.; Lee, M.J.; Jeong, M.S.; Kim, S.Y.; Lee, S.H.; Jang, S.H.; Park, J.; Kang, T.C.; Won, M.H.; Cho, S.W.; Kwon, O.S.; Eum, W.S.; Choi, S.Y.
Human brain pyridoxal-5-phosphate phosphatase (PLPP):protein transduction of PEP-1-PLPP into PC12 cells
BMB Rep.
41
408-413
2008
Homo sapiens (Q96GD0), Homo sapiens
Li, H.; Wang, Y.; Yang, H.; Liu, L.; Wang, J.; Zheng, N.
Lactoferrin induces the synthesis of vitamin B6 and protects HUVEC functions by activating PDXP and the PI3K/AKT/ERK1/2 pathway
Int. J. Mol. Sci.
20
587
2019
Homo sapiens (Q96GD0)
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