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Information on EC 7.2.2.8 - P-type Cu+ transporter and Organism(s) Mus musculus and UniProt Accession Q64430

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IUBMB Comments
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme transports Cu+ or Ag+, and cannot transport the divalent ions, contrary to EC 7.2.2.9, P-type Cu2+ transporter, which mainly transports the divalent copper ion.
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Mus musculus
UNIPROT: Q64430
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The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
slc31a1, copt1, ctra2, cu(+)-atpase, copa1, copa2, copper-transporting atpase 2, ctra3, cu atpase, copper export atpase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
copper transporter
-
Cu+-exporting ATPase
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (P-type, Cu+-exporting)
A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme transports Cu+ or Ag+, and cannot transport the divalent ions, contrary to EC 7.2.2.9, P-type Cu2+ transporter, which mainly transports the divalent copper ion.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
a second di-leucine motif in the carboxy tail of ATP7A (1459LL) is essential for steady-state localization in the trans-Golgi network by functioning in endosome-to-trans-Golgi network trafficking. Multiple di-leucine signals are required for recycling ATP7A from the plasma membrane to the trans-Golgi network
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
role of extracellular superoxide dismutase SOD3 and ATP7A in endothelial dysfunction in type 1 diabetes mellitus. Type 1 diabetes mellitus-induced endothelial dysfunction and decrease of SOD3 activity are rescued in transgenic mice overexpressing the enzyme ATP7A, a copper transporter. Copper transporter ATP7A protein expression is significantly reduced in blood vessels from type 1 diabetes mellitus mice in part due to the insulin deficiency but not high glucose. Transgenic mice overexpressing ATP7A restore type 1 diabetes mellitus-induced impaired SOD3 activity and endothelial function by reducing superoxide levels
physiological function
physiological function
transporter ATP7B maintains a Cu gradient along the duodenal crypt-villus axis and buffers Cu levels in the cytosol of enterocytes, mediated by rapid Cu-dependent enlargement of ATP7B-containing vesicles and increased levels of ATP7B. Intestines of Atp7b-/- mice show reduced Cu storage pools in intestine, Cu depletion, accumulation of triglyceride-filled vesicles in enterocytes, mislocalization of apolipoprotein B, and loss of chylomicrons
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ATP7A_MOUSE
1491
7
161959
Swiss-Prot
other Location (Reliability: 2)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme overexpression in transgenic mmice
expression in Escherichia coli. The use of DNA synthesis to generate silent mutations across the majority of both mouse and human ATP7A open reading frames is sufficient to stabilize the genes in high-copy plasmids
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
copper transporter ATP7A protein expression is significantly reduced in blood vessels from type 1 diabetes mellitus mice
insulin treatment, but not high glucose, increases enzyme ATP7A expression in vascular smooth muscles cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sudhahar, V.; Urao, N.; Oshikawa, J.; McKinney, R.D.; Llanos, R.M.; Mercer, J.F.; Ushio-Fukai, M.; Fukai, T.
Copper transporter ATP7A protects against endothelial dysfunction in type 1 diabetic mice by regulating extracellular superoxide dismutase
Diabetes
62
3839-3850
2013
Mus musculus (Q64430), Mus musculus C57/BL6J (Q64430)
Manually annotated by BRENDA team
Sudhahar, V.; Okur, M.N.; Bagi, Z.; OBryan, J.P.; Hay, N.; Makino, A.; Patel, V.S.; Phillips, S.A.; Stepp, D.; Ushio-Fukai, M.; Fukai, T.
Akt2 (protein kinase B beta) stabilizes ATP7A, a copper transporter for extracellular superoxide dismutase, in vascular smooth muscle novel mechanism to limit endothelial dysfunction in type 2 diabetes mellitus
Arterioscler. Thromb. Vasc. Biol.
38
529-541
2018
Homo sapiens (Q04656), Mus musculus (Q64430)
Manually annotated by BRENDA team
Pierson, H.; Muchenditsi, A.; Kim, B.E.; Ralle, M.; Zachos, N.; Huster, D.; Lutsenko, S.
The function of ATPase copper transporter ATP7B in intestine
Gastroenterology
154
168-180.e5
2018
Mus musculus (Q64446)
Manually annotated by BRENDA team
Ladomersky, E.; Khan, A.; Shanbhag, V.; Cavet, J.; Chan, J.; Weisman, G.; Petris, M.
Host and pathogen copper-transporting P-type ATPases function antagonistically during Salmonella infection
Infect. Immun.
85
e00351-17
2017
Salmonella enterica subsp. enterica serovar Typhimurium (A0A0H3NA56), Mus musculus (Q64430), Salmonella enterica subsp. enterica serovar Typhimurium SL1344 (A0A0H3NA56)
Manually annotated by BRENDA team
Zhu, S.; Shanbhag, V.; Wang, Y.; Lee, J.; Petris, M.
A role for the ATP7A copper transporter in tumorigenesis and cisplatin resistance
J. Cancer
8
1952-1958
2017
Mus musculus (Q64430)
Manually annotated by BRENDA team
Zhu, S.; Shanbhag, V.; Hodgkinson, V.L.; Petris, M.J.
Multiple di-leucines in the ATP7A copper transporter are required for retrograde trafficking to the trans-Golgi network
Metallomics
8
993-1001
2016
Mus musculus (Q64430)
Manually annotated by BRENDA team