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Information on EC 7.6.2.1 - P-type phospholipid transporter and Organism(s) Bos taurus and UniProt Accession C7EXK4
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7.6.2.1 P-type phospholipid transporterIUBMB Comments
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. Different forms of the enzyme move phospholipids such as phosphatidylcholine, lyso-phosphatidylcholine, phosphatidylserine, phosphatidylethanolamine, phosphatidyglycerol, sphingomyelin and glucosylceramide from one membrane face to the other ('flippase').
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Word Map
- 7.6.2.1
- leaflet
- cholestasis
-
aminophospholipids
- bile
-
asymmetry
- erythrocyte
-
intrahepatic
- atpases
- ca2+-atpase
- na+
- myosin
- biliary
-
canalicular
-
abcb11
-
k+-atpase
- phosphatidylethanolamine
-
scramble
-
actin-activated
- actomyosin
-
ca2+-dependent
-
flip-flop
- p-glycoproteins
- na+,k+-atpase
-
pro12ala
-
ca2+-activated
-
ursodeoxycholic
- cholelithiasis
- ouabain
- hepatobiliary
-
exoplasmic
- gallstone
-
o-antigens
- pruritus
- gizzard
-
proteoliposomes
-
lipid-linked
-
cholangiopathy
- meromyosin
-
3.6.1.3
-
actin-myosin
-
ptdser
-
ppargamma2
-
ca2+-stimulated
-
superprecipitation
- fr
-
ca2+-pumping
- analysis
- prothrombinase
-
photophosphorylation
- molecular biology
- undecaprenyl
- medicine
-
subfragment-1
The taxonomic range for the selected organisms is: Bos taurus
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Synonyms
mg2+-atpase, abcb4, flippase, plscr1, atp8b1, scramblase, aminophospholipid translocase, ala12, tat-2, drs2p, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aminophospholipid flippase
-
-
-
-
aminophospholipid flippase 10
-
-
-
-
aminophospholipid flippase 11
-
-
-
-
aminophospholipid flippase 12
-
-
-
-
aminophospholipid translocase
aminophospholipid translocase VC
-
-
-
-
Atp8a2
ATPase II
ATPVC
-
-
-
-
ATPVD
-
-
-
-
flippase
HUSSY-20
-
-
-
-
Mg2+-ATPase
-
-
-
-
Mg2+-ATPase A
-
-
-
-
additional information
aminophospholipid translocase
-
-
-
-
ATPase II
-
-
-
-
flippase
-
-
-
-
additional information
the enzyme belongs to the P4-ATPase subfamily of the of P-type ATPases
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + phospholipid [side 1] = ADP + phosphate + phospholipid [side 2]
P-type ATPase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
transmembrane transport
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (P-type, phospholipid-flipping)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. Different forms of the enzyme move phospholipids such as phosphatidylcholine, lyso-phosphatidylcholine, phosphatidylserine, phosphatidylethanolamine, phosphatidyglycerol, sphingomyelin and glucosylceramide from one membrane face to the other ('flippase').
CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
-
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
ATP + H2O + 1-oleoyl-2-[6-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]hexanoyl]-sn-glycero-3-phosphoserine[side 1]
ADP + phosphate + 1-oleoyl-2-[6-[(7-nitro-2-1,3-benzoxadiazol-4-yl)amino]hexanoyl]-sn-glycero-3-phosphoserine[side 2]
-
-
-
-
?
ATP + H2O + phosphatidylethanolamine/out
ADP + phosphate + phosphatidylethanolamine/in
-
transport from the exoplasmic to the cytosolic leaflet of the plasma membrane
-
-
?
ATP + H2O + phosphatidylserine[side 1]
ADP + phosphate + phosphatidylserine[side 2]
-
-
-
-
?
phosphatidylcholine/out
phosphatidylcholine/in
-
spin-labeled substrate, inward and outward movements, flip and flop, proceed in thermodynamic equilibrium in disc membrane vesicles between inner and out leaflets
-
-
r
phosphatidylethanolamine/out
phosphatidylethanolamine/in
-
spin-labeled substrate, inward and outward movements, flip and flop, proceed in thermodynamic equilibrium in disc membrane vesicles between inner and out leaflets
-
-
r
phosphatidylserine/out
phosphatidylserine/in
-
spin-labeled substrate, inward and outward movements, flip and flop, proceed in thermodynamic equilibrium in disc membrane vesicles between inner and out leaflets
-
-
r
ATP + H2O + phosphatidylethanolamine/in
ADP + phosphate + phosphatidylethanolamine/out
-
-
-
?
ATP + H2O + phosphatidylethanolamine/in
ADP + phosphate + phosphatidylethanolamine/out
the enzyme is specific for ATP and shows no activity with GTP, AMP-PNP, GDP, or ADP
-
-
?
ATP + H2O + phosphatidylserine/in
ADP + phosphate + phosphatidylserine/out
-
-
-
?
ATP + H2O + phosphatidylserine/in
ADP + phosphate + phosphatidylserine/out
the enzyme is specific for ATP and shows no activity with GTP, AMP-PNP, GDP, or ADP
-
-
?
ATP + H2O
ADP + phosphate
-
selectively pumps the aminophospholipids phospatidylserine and phosphatidylethanolamine from the outer to the inner monolayer of eukaryotic cells and is predominantly responsible for the asymmetric phospholipid distribution of the plasma membrane
-
-
?
ATP + H2O
ADP + phosphate
phosphatidylserine is essential for the dephosphorylation of the phosphoenzyme intermediate
-
?
ATP + H2O
ADP + phosphate
-
down-regulation of the aminophospholipid translocase activity is an early step in the programmed cell death in lymphocytes, a step that contributes to the appearance of phosphatidylserine on the cell surface as a recognition signal for phagocytosis
-
-
?
ATP + H2O
ADP + phosphate
the enzyme plays an important role in the maintenance of membrane phospholipid asymmetry, observed in plasma membrane and membranes of certain cellular organelles
-
-
?
ATP + H2O
ADP + phosphate
phosphatidylserine is essential for the dephosphorylation of the phosphoenzyme intermediate. Without phosphatidylserine, ATPase II accumulates as phosphoenzyme in the presence of ATP, resulting in the interruption of its catalytic cycle
-
-
?
ATP + H2O + phosphatidylserine/out
ADP + phosphate + phosphatidylserine/in
-
transport from the exoplasmic to the cytosolic leaflet of the plasma membrane
-
-
?
ATP + H2O + phosphatidylserine/out
ADP + phosphate + phosphatidylserine/in
-
transport from the exoplasmic to the cytosolic leaflet of the plasma membrane, and from the lumenal side of granules to the external side
-
-
?
additional information
?
-
Atp8a2 flipps fluorescent-labeled phosphatidylserine from the inner leaflet of liposomes, equivalent to the exocytoplasmic leaflet of cell membranes, to the outer leaflet, equivalent to cytoplasmic leaflet, in an ATP-dependent manner
-
-
?
additional information
?
-
dithionite NBD-lipid assay for detection of flippase activity
-
-
?
additional information
?
-
during the transport across the membrane, the phosphatidylserine head group passes near residue I364. I364 is critical to the release of the transported lipid into the cytosolic leaflet. Transmembrane segment M4 residue N359 is involved in recognition of the lipid substrate on the exoplasmic side. Residue I364 and adjacent hydrophobic residues function as a hydrophobic gate that separates the entry and exit sites of the lipid and directs sequential formation and annihilation of water-filled cavities, thereby enabling transport of the hydrophilic phospholipid head group in a groove outlined by the transmembrane segments M1, M2, M4, and M6, with the hydrocarbon chains following passively, still in the membrane lipid phase
-
-
?
additional information
?
-
-
the enzyme is a P-type ATPase involved in regulation of the lipid asymmetry of the cell membrane
-
-
?
additional information
?
-
-
no transport activity with phosphatidylinositol
-
-
?
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
ATP + H2O + phosphatidylethanolamine/in
ADP + phosphate + phosphatidylethanolamine/out
-
-
-
?
ATP + H2O + phosphatidylserine/in
ADP + phosphate + phosphatidylserine/out
-
-
-
?
ATP + H2O + phosphatidylethanolamine/out
ADP + phosphate + phosphatidylethanolamine/in
-
transport from the exoplasmic to the cytosolic leaflet of the plasma membrane
-
-
?
ATP + H2O + phosphatidylserine/out
ADP + phosphate + phosphatidylserine/in
-
transport from the exoplasmic to the cytosolic leaflet of the plasma membrane
-
-
?
ATP + H2O + phosphatidylserine[side 1]
ADP + phosphate + phosphatidylserine[side 2]
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
selectively pumps the aminophospholipids phospatidylserine and phosphatidylethanolamine from the outer to the inner monolayer of eukaryotic cells and is predominantly responsible for the asymmetric phospholipid distribution of the plasma membrane
-
-
?
ATP + H2O
ADP + phosphate
-
down-regulation of the aminophospholipid translocase activity is an early step in the programmed cell death in lymphocytes, a step that contributes to the appearance of phosphatidylserine on the cell surface as a recognition signal for phagocytosis
-
-
?
ATP + H2O
ADP + phosphate
the enzyme plays an important role in the maintenance of membrane phospholipid asymmetry, observed in plasma membrane and membranes of certain cellular organelles
-
-
?
ATP + H2O
ADP + phosphate
phosphatidylserine is essential for the dephosphorylation of the phosphoenzyme intermediate. Without phosphatidylserine, ATPase II accumulates as phosphoenzyme in the presence of ATP, resulting in the interruption of its catalytic cycle
-
-
?
additional information
?
-
Atp8a2 flipps fluorescent-labeled phosphatidylserine from the inner leaflet of liposomes, equivalent to the exocytoplasmic leaflet of cell membranes, to the outer leaflet, equivalent to cytoplasmic leaflet, in an ATP-dependent manner
-
-
?
additional information
?
-
-
the enzyme is a P-type ATPase involved in regulation of the lipid asymmetry of the cell membrane
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no activation by phosphatidylcholine or other membrane lipids
-
additional information
-
neither phosphatidylinositol nor phosphatidylinositol 4-phosphate have any significant effect on the phosphatidylserine-stimulated ATPase activity of the enzyme
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.016
ATP
mutant I364A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C
0.016
ATP
mutant I364S, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C
0.019
ATP
mutant I364Q, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C
0.02
ATP
mutant T369A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C
0.02
ATP
mutant V906A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C
0.023
ATP
mutant N360A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C
0.024
ATP
mutant I362A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C
0.027
ATP
mutant F88A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C
0.036
ATP
mutant Y358A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C
0.038
ATP
wild-type, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C
0.042
ATP
mutant F354A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C
0.045
ATP
mutant L112A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C
0.049
ATP
mutant E371Q, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C
0.049
ATP
mutant K374A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C
0.058
ATP
mutant L361A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C
0.068
ATP
mutant L367A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C
0.073
ATP
mutant I115A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C
0.103
ATP
mutant V906A, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C
0.104
ATP
mutant S365A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C
0.105
ATP
mutant I364S, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C
0.111
ATP
mutant I364E, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C
0.131
ATP
mutant I364A, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C
0.148
ATP
mutant I364M, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C
0.149
ATP
mutant I362A, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C
0.178
ATP
mutant I364F, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C
0.22
ATP
mutant N359A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C
0.25
ATP
mutant F88A, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C
0.288
ATP
mutant I364Q, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C
0.292
ATP
mutant I364E, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C
0.369
ATP
mutant I364M, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C
0.371
ATP
wild-type, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C
0.376
ATP
mutant I115A, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C
0.379
ATP
mutant L367A, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C
0.394
ATP
mutant L112A, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C
0.862
ATP
mutant S365A, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C
1.12
ATP
mutant I364F, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C
2.215
ATP
mutant N359A, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C
additional information
additional information
Michaelis-Menten kinetics, overview
-
additional information
additional information
-
kinetics of inward and outward movements
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
translocation velocity and phospholipid distribution in the membrane leaflets
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
outer segment disc membranes of rod and cone photoreceptor cells, high expression of atp8a2
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
localization study by immunofluorescence microscopy
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
P4-ATPases in general are implicated in the energy-dependent translocation of aminophospholipids across cell membranes. Atp8a2 is implicated in the generation and maintenance of phosphatidylserine asymmetry in photoreceptor disc membranes
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). AT8A2_BOVIN
1148
8
129037
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
the enzyme undergoes phosphorylation on the serine residue within a CaMKII target motif
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
I115A
biphasic phosphatidylserine concentration dependence with inhibition at the highest concentration
I364Q
activation phase is followed by an inhibition phase at high phosphatidylserine concentration
L112A
mutation does not appreciably affect Vmax, the apparent affinities for the substrates, or the phosphorylation rate
V906A
pronounced inhibition at high phosphatidylethanol concentration with only a slight inhibition at high phosphatidylserine concentration
E126A
-
the mutant shows about 10% of wild type activity. The mutation leads to reduced glycosylation of the accessory subunit CDC50A
I305A
-
the mutant shows about 50% of wild type activity. The mutation leads to reduced glycosylation of the accessory subunit CDC50A
L361A
-
the mutant shows about 15% of wild type activity. The mutation leads to reduced glycosylation of the accessory subunit CDC50A
L366A
-
the mutant shows about 40% of wild type activity. The mutation leads to reduced glycosylation of the accessory subunit CDC50A
S1138D
-
the mutant shows slightly reduced activity compared to the wild type enzyme
Y878A
-
the mutant shows about 25% of wild type activity. The mutation leads to reduced glycosylation of the accessory subunit CDC50A
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native Atp8a2 1887fold from photoreceptor outer segments by immunoaffinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene atp8a2, DNA and amino acid sequence determination and analysis, expression of 1D4-tagged Atp8a2 in HEK-293 cells
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
purified Atp8a2 is reconstituted into liposomes containing fluorescent-labeled phosphatidylserine to measure the ability of Atp8a2 to flip phosphatidylserine across the lipid bilayer. 30% of the reconstituted Atp8a2 is inaccessible to trypsin and correspondingly ATP
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Daleke, D.L.; Lyles, J.V.
Identification and purification of aminophospholipid flippases
Biochim. Biophys. Acta
1486
108-127
2000
Bos taurus, Homo sapiens
Devaux, P.F.; Zachowski, A.; Morrot, G.; Cribier, S.; Fellmann, P.; Geldwerth, D.; Bitbol, M.; Herve, P.
Control of the transmembrane phospholipid distribution in eukaryotic cells by aminophospholipid translocase
Biotechnol. Appl. Biochem.
12
517-522
1990
Bos taurus, Cavia porcellus, Homo sapiens, Rattus norvegicus, Sus scrofa
Tang, X.; Halleck, M.S.; Schlegel, R.A.; Williamson, P.
A subfamily of P-type ATPase with aminophospholipid transporting activity
Science
272
1495-1497
1996
Bos taurus
Ding, J.; Wu, Z.; Crider, B.P.; Ma, Y.; LI, X.; Slaughter, C.; Gong, L.; Xie, X.S.
Identification and functional expression of four isoforms of ATPase II, the putative aminophospholipid translocase
J. Biol. Chem.
275
23378-13386
2000
Bos taurus (Q29449), Bos taurus
Devaux, P.F.; Lopez-MOntero, I.; Bryde, S.
Proteins involved in lipid translocation in eukaryotic cells
Chem. Phys. Lipids
141
119-132
2006
Bos taurus, Saccharomyces cerevisiae, Homo sapiens, Leishmania infantum, Rattus norvegicus
Hessel, E.; Herrmann, A.; Mller, P.; Schmetkamp, P.P.M.; Hofmann, K.P.
The transbilayer distribution of phospholipids in disc membranes is a dynamic equilibrium. Evidence for rapid flip and flop movement
Eur. J. Biochem.
267
1473-1483
2000
Bos taurus
Coleman, J.A.; Kwok, M.C.; Molday, R.S.
Localization, purification, and functional reconstitution of the P4-ATPase Atp8a2, a phosphatidylserine flippase in photoreceptor disc membranes
J. Biol. Chem.
284
32670-32679
2009
Bos taurus (C7EXK4), Mus musculus (P98200), Homo sapiens (Q9NTI2)
Vestergaard, A.L.; Coleman, J.A.; Lemmin, T.; Mikkelsen, S.A.; Molday, L.L.; Vilsen, B.; Molday, R.S.; Dal Peraro, M.; Andersen, J.P.
Critical roles of isoleucine-364 and adjacent residues in a hydrophobic gate control of phospholipid transport by the mammalian P4-ATPase ATP8A2
Proc. Natl. Acad. Sci. USA
111
E1334-E1343
2014
Bos taurus (C7EXK4)
Vestergaard, A.L.; Mikkelsen, S.A.; Coleman, J.A.; Molday, R.S.; Vilsen, B.; Andersen, J.P.
Specific mutations in mammalian P4-ATPase ATP8A2 catalytic subunit entail differential glycosylation of the accessory CDC50A subunit
FEBS Lett.
589
3908-3914
2015
Bos taurus
EXTERNAL LINKS (specific for EC-Number 7.6.2.1)
Transporter Classification Database (TCDB): 3.A.3.8.1, 3.A.3.8.13, 3.A.3.8.8, 3.A.3.8.11, 3.A.1.211.13, 3.A.3.8.14, 8.A.17.1.1, 3.A.3.8.15, 3.A.3.8.2, 3.A.3.8.5, 3.A.3.8.4, 3.A.3.8.18, 3.A.3.8.20, 3.A.1.201.3, 3.A.3.8.24, 3.A.3.8.7, 3.A.3.8.9, 3.A.3.8.6, 3.A.3.8.16, 3.A.1.211.14, 3.A.1.211.1, 3.A.1.201.1, 3.A.3.8.26, 3.A.3.8.25, 3.A.3.8.17, 3.A.3.8.12, 3.A.1.211.5, 3.A.1.211.2, 3.A.1.211.10, 3.A.3.8.10, 3.A.3.8.3
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