Biomedical Engineering Reference
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ABCC1
dog Abcc1
mouse Abcc1
rat Abcc1
chicken Abcc1
ABCC3
mouse Abcc3
rat Abcc3
ABCC2
monkey Abcc2
dog Abcc2
rabbit Abcc2
mouse Abcc2
rat Abcc2
chicken Abcc2
zebrafish Abcc2
little skate Abcc2
ABCC6
mouse Abcc6
rat Abcc6
ABCC11
ABCC12
mouse Abcc12
rat Abcc12
ABCC5
mouse Abcc5
rat Abcc5
ABCC4
mouse Abcc4
rat Abcc4
chicken Abcc4
zebrafish Abcc4
ABCC10
mouse Abcc10
ABCC8/SUR1
ABCC9A/SUR2A
ABCC9B/SUR2B
ABCC7/CFTR
MSD0
MSD1
MSD2
ABCC1
NH
+
out
ABCC2
ABCC3
ABCC6
in
COO
−
NBD2
NBD1
ABCC10
MSD1
MSD2
ABCC4
ABCC5
ABCC11
ABCC12
out
in
NH
+
COO
−
NBD1
NBD2
(a)
FIGURE 11.1
Topology of the human ABBC subfamily members and phy-
logenetic tree of full-length amino acid sequences from ABCC orthologs. (
a
)
Schematic representation of the ABC core structure with two membrane-spanning
domains MSD1 and MSD2, each followed by the nucleotide-binding domains,
NBD1 and NBD2, respectively, shared by ABCC4, ABCC5, ABCC11, and
ABCC12. An additional amino terminal MSD0, which precedes the ABC core
structure, is predicted for ABCC1-3, ABCC6, and ABCC10. The number of
transmembrane segments in MSD2 of ABCC2 remains unclear, varying between
four and six depending on the algorithms used. (
b
) Phylogenetic tree reconstructed
from the pairwise evolutionary distance between aligned ABCC/Abcc sequences.
10 substitutions
per 100 amino acids
(b)
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