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Information on EC 5.6.1.6 - channel-conductance-controlling ATPase and Organism(s) Danio rerio and UniProt Accession Q1LX78

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IUBMB Comments
ABC-type (ATP-binding cassette-type) ATPase, characterized by the presence of two similar ATP-binding domains. The enzyme is found in animals, and in humans its absence brings about cystic fibrosis. Unlike most of the ABC transporters, chloride pumping is not directly coupled to ATP hydrolysis. Instead, the passive flow of anions through the channel is gated by cycles of ATP binding and hydrolysis by the ATP-binding domains. The enzyme is also involved in the functioning of other transmembrane channels.
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This record set is specific for:
Danio rerio
UNIPROT: Q1LX78
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Word Map
The taxonomic range for the selected organisms is: Danio rerio
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
+
+
closed Cl- channel
=
+
+
open Cl- channel
Synonyms
cystic fibrosis transmembrane conductance regulator, cystic fibrosis transmembrane regulator, cftr channel, cftr cl- channel, cystic fibrosis conductance regulator, abcc7, epithelial basolateral chloride conductance regulator, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cystic fibrosis transmembrane conductance regulator
-
cystic fibrosis transmembrane conductance regulator
cystic-fibrosis membrane-conductance protein
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
transmembrane transport
-
-
-
-
hydrolysis of phosphate bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (channel-conductance-controlling)
ABC-type (ATP-binding cassette-type) ATPase, characterized by the presence of two similar ATP-binding domains. The enzyme is found in animals, and in humans its absence brings about cystic fibrosis. Unlike most of the ABC transporters, chloride pumping is not directly coupled to ATP hydrolysis. Instead, the passive flow of anions through the channel is gated by cycles of ATP binding and hydrolysis by the ATP-binding domains. The enzyme is also involved in the functioning of other transmembrane channels.
CAS REGISTRY NUMBER
COMMENTARY hide
9000-83-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O + closed Cl- channel
ADP + phosphate + open Cl- channel
show the reaction diagram
-
-
-
?
ATP + H2O + closed Cl- channel
ADP + phosphate + open Cl- channel
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O + closed Cl- channel
ADP + phosphate + open Cl- channel
show the reaction diagram
-
-
-
?
ATP + H2O + closed Cl- channel
ADP + phosphate + open Cl- channel
show the reaction diagram
-
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CFTR_DANRE
1485
10
168400
Swiss-Prot
other Location (Reliability: 3), other Location (Reliability: 1)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
phosphorylation of the enzyme leads to structural transitions that promote channel widening while ahead of extracellular gate opening
phosphoprotein
-
the enzyme is activated by protein kinase A-dependent phosphorylation
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E1372Q
the mutation abolishes ATP hydrolysis and slows the pore-closing rate by about 1000fold as compared to the wild type enzyme
E1372Q
-
the mutation abolishes the ATPase activity of the enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
GFP nanobody-coupled resin column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in HEK-293S cells
expressed in CHO cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhang, Z.; Liu, F.; Chen, J.
Conformational changes of CFTR upon phosphorylation and ATP binding
Cell
170
483-491.e8
2017
Danio rerio (Q1LX78), Danio rerio
Manually annotated by BRENDA team
Zhang, J.; Yu, Y.C.; Yeh, J.T.; Hwang, T.C.
Functional characterization reveals that zebrafish CFTR prefers to occupy closed channel conformations
PLoS ONE
13
e0209862
2018
Danio rerio
Manually annotated by BRENDA team