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Information on EC 7.2.2.9 - P-type Cu2+ transporter and Organism(s) Rattus norvegicus and UniProt Accession P70705
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7.2.2.9 P-type Cu2+ transporterIUBMB Comments
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. The enzyme from the termophilic archaeon Archaeoglobus fulgidus is involved in copper extrusion from the cell [1,2].
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Word Map
- 7.2.2.9
-
3.6.1.3
- ceruloplasmin
- cisplatin
- atpases
-
copper-dependent
-
x-linked
- na+
- platinum
- triphosphatase
-
trans-golgi
-
metal-binding
- biliary
- overload
-
copper-binding
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disease-causing
- metallothioneins
-
k+-atpase
- oxaliplatin
- ouabain
-
copper-induced
- carboplatin
-
platinum-based
- mg2+-atpase
-
toxicosis
-
occipital
-
kayser-fleischer
- copa
- adenosinetriphosphatase
- na+,k+-atpase
- phosphoenzyme
- d-penicillamine
-
cisplatin-resistant
- ferroxidase
-
mottled
-
long-evans
-
copper-containing
-
copperi
- tetrathiomolybdate
-
copper-deficient
-
metallochaperone
-
kinky
- cinnamon
-
k+-stimulated
-
cddp-resistant
-
multicopper
- bathocuproine
- medicine
-
cu-induced
- drug development
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3.1.3.5
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terrier
-
k+-dependent
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
atp7b, atp7a, copper transporter, copper-transporting atpase, copper-transporting p-type atpase, menkes protein, cu-atpase, copper transporting p-type atpase, copper atpase, copper-transporting p-type, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosine 5'-triphosphatase
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-
-
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ATP hydrolase
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-
-
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ATP phosphohydrolase
-
-
-
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ATP7B
ATPase
-
-
-
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complex V
-
-
-
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Cu2+-ATPase
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-
-
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CUA-1 ATPase
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-
-
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Menkes disease-associated protein
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-
-
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Menkes disease-associated protein homolog
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-
-
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Menkes P-type ATPase
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-
-
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MNK
-
-
-
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Pinal night-specific ATPase
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-
-
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WCBD
-
-
-
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Wilson copper-transporting P-type ATPase
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-
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Wilson disease copper-transporting ATPase
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-
-
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Wilson disease protein
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-
-
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Wilson disease-associated protein
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-
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Wilson disease-associated protein homolog
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-
-
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ATP7B
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
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-
-
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transmembrane transport
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (P-type, Cu2+-exporting)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. The enzyme from the termophilic archaeon Archaeoglobus fulgidus is involved in copper extrusion from the cell [1,2].
CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
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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 + Cu2+/in
ADP + phosphate + Cu2+/out
role of ATP7A in protective effect of copper in neuronal cells analyzed
-
-
?
ATP + H2O + Cu2+/in
ADP + phosphate + Cu2+/out
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in normal conditions ATP7B regulates Cu homeostasis and biosynthesis of holo cuproenzymes and cuproenzyme-related neurotransmission in the brain regions. Neurotoxicity due to abnormal copper accumulation or irregular regulation of cuproenzymes in the critical brain regions by mutation of the ATP7B gene leads to neurological dysfunctions of Wilson disease
-
?
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 + Cu2+/in
ADP + phosphate + Cu2+/out
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in normal conditions ATP7B regulates Cu homeostasis and biosynthesis of holo cuproenzymes and cuproenzyme-related neurotransmission in the brain regions. Neurotoxicity due to abnormal copper accumulation or irregular regulation of cuproenzymes in the critical brain regions by mutation of the ATP7B gene leads to neurological dysfunctions of Wilson disease
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cu+
the metal-dependent conformational changes observed in the N-terminal region of the ATPase may not require the presence of the CXXC motif on every domain, as long as the domain has the proper shape, which is an heavy metal-associated-domain-like fold, and as long as some of them contain the CXXC metal binding site. At a certain point during the cooperative binding of Cu(I), protein/protein interactions among the heavy metal-associated -domains begin to dominate the conformational changes in rat ATP7B, while metal binding to the heavy metal-associated -domains makes a smaller contribution
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
connection between copper homeostasis and NMDA receptor activity, ATP7A required for copper-dependent effects
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Menkes protein could be involved in copper secretion from acinar cells into saliva
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intensely detected in neuronal cells of the hippocampal formation, olfactory bulbs, cerebellum, cerebral cortex and nuclei in the brainstem
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polarized sorting of the Cu2+ transporter ATP7B to the somatodendritic domain of rat hippocampal neurons is mediated by recognition of dileucine-based signals in the cytosolic domains of the proteins by the sigma1 subunit of the clathrin adaptor AP-1. Under basal Cu2+ conditions, ATP7B is localized to the trans-Golgi network and the plasma membrane of the soma and dendrites but not the axon. Mutation of a dileucine-based signal in ATP7B or overexpression of a dominant-negative sigma1 mutant results in nonpolarized distribution of ATP7B between the somatodendritic and axonal domains. Addition of high Cu2+ concentrations causes loss of trans-Golgi network localization and somatodendritic polarity of ATP7B
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
immunohistochemic localization analysis, overview
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-
polarized sorting of the Cu2+ transporter ATP7B to the somatodendritic domain of rat hippocampal neurons is mediated by recognition of dileucine-based signals in the cytosolic domains of the proteins by the sigma1 subunit of the clathrin adaptor AP-1. Under basal Cu2+ conditions, ATP7B is localized to the trans-Golgi network and the plasma membrane of the soma and dendrites but not the axon. Mutation of a dileucine-based signal in ATP7B or overexpression of a dominant-negative sigma1 mutant results in nonpolarized distribution of ATP7B between the somatodendritic and axonal domains. Addition of high Cu2+ concentrations causes loss of trans-Golgi network localization and somatodendritic polarity of ATP7B
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
mutation of ATP7A is involved in Menkes disease, a severe infantile-onset neurodegenerative disorder
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). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
64000
-
x * 97000, splicing variant in cytosol and plasma membrane, SDS-PAGE, x * 64000, splicing variant in nucleus, SDS-PAGE
97000
-
x * 97000, splicing variant in cytosol and plasma membrane, SDS-PAGE, x * 64000, splicing variant in nucleus, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 97000, splicing variant in cytosol and plasma membrane, SDS-PAGE, x * 64000, splicing variant in nucleus, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of the DNA segment coding for the N-terminal copper-binding region into a GST pGEX-6P-2 vector
gene ATP7A, genetic mapping and expression analysis of splicing variants, overview
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Saito, T.; Okabe, M.; Hosokawa, T.; Kurasaki, M.; Hata, A.; Endo, F.; Nagano, K.; Matsuda, I.; Urakami, K.; Saito, K.
Immunohistochemical determination of the Wilson copper-transporting P-type ATPase in the brain tissue of the rat
Neurosci. Lett.
266
13-16
1999
Rattus norvegicus
DAmico, F.; Skarmoutsou, E.; Sanfilippo, S.; Camakaris, J.
Menkes protein localization in rat parotid acinar cells
Acta Histochem.
107
373-378
2005
Rattus norvegicus (P70705)
Tsay, M.J.; Fatemi, N.; Narindrasorasak, S.; Forbes, J.R.; Sarkar, B.
Identification of the "missing domain" of the rat copper-transporting ATPase, atp7b: insight into the structural and metal binding characteristics of its N-terminal copper-binding domain
Biochim. Biophys. Acta
1688
78-85
2004
Rattus norvegicus (Q64535)
Schlief, M.L.; West, T.; Craig, A.M.; Holtzman, D.M.; Gitlin, J.D.
Role of the Menkes copper-transporting ATPase in NMDA receptor-mediated neuronal toxicity
Proc. Natl. Acad. Sci. USA
103
14919-14924
2006
Rattus norvegicus (P70705), Mus musculus (Q64430)
Collins, J.F.; Hua, P.; Lu, Y.; Ranganathan, P.N.
Alternative splicing of the Menkes copper Atpase (Atp7a) transcript in the rat intestinal epithelium
Am. J. Physiol. Gastrointest. Liver Physiol.
297
G695-G707
2009
Homo sapiens, Rattus norvegicus
EXTERNAL LINKS (specific for EC-Number 7.2.2.9)
Transporter Classification Database (TCDB): 3.A.3.5.12, 3.A.3.5.10
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