BRENDA - Enzyme Database show
show all sequences of 7.6.2.8

Translocation of the ABC transporter ABCD4 from the endoplasmic reticulum to lysosomes requires the escort protein LMBD1

Kawaguchi, K.; Okamoto, T.; Morita, M.; Imanaka, T.; Sci. Rep. 6, 30183 (2016)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene ABCD4, stable recombinant expression of human ABCD4 in CHO cells, recombinant expression of N-terminally MBP-tagged enzyme, stable recombinant expression of wild-type and mutant HA-tagged ABCD4 in human hepatoma HuH7 cells and additional transient coexpression of wild-type and mutant GFP-tagged LMBRD1
Homo sapiens
Engineering
Amino acid exchange
Commentary
Organism
additional information
generation of chimeric ABCD4 proteins that are exchanged in terms of the corresponding putative transmembrane helix with ABCD1 (based on the secondary structure of the eukaryotic P-glycoprotein homolog CmABCB1) in HEK-293 cells, endogenous human ABCD1 does not interact with LMBD1. Construction of ABCD4 chimeras 1-6 and analysis of the localization of chimeric ABCD4s in CHO cells stably expressing LMBD1-GFP. The wild-type ABCD4 co-expressed with LMBD1 exhibits a punctate distribution that is superimposable on the distribution pattern of LMBD1. The distribution patterns of the ABCD4 chimeras 1, 3, 4 and 6 also display the same pattern as LMBD1. But ABCD4 chimeras 2 and 5 do not exhibit a punctate pattern, but rather, a reticulum-like distribution pattern that is not superimposable on LMBD1
Homo sapiens
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
endoplasmic reticulum membrane
translocation of the ABC transporter ABCD4 from the endoplasmic reticulum to lysosomes requires the escort protein LMBD1
Homo sapiens
5789
-
lysosomal membrane
translocation of the ABC transporter ABCD4 from the endoplasmic reticulum to lysosomes requires the escort protein LMBD1
Homo sapiens
5765
-
additional information
LMBD1 associates with ABCD4 at the ER membrane and transports ABCD4 to lysosomes, ABCD4 interacts with LMBD1. The translocation depends on the lysosomal targeting ability of LMBD1. Endogenous ABCD4 is localized to both lysosomes and the endoplasmic reticulum. ABCD4 lacks the NH2-teminal hydrophobic region that is responsible for the targeting to peroxisomes. ABCD4 and LMBD1 form complex in vitro. The regions around transmembrane helix 2 and 5 of ABCD4 are critically important for the translocation of ABCD4 to lysosomes along with LMBD1
Homo sapiens
-
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1]
Homo sapiens
-
ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1]
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
O14678
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1]
-
752200
Homo sapiens
ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1]
-
-
-
?
Subunits
Subunits
Commentary
Organism
homodimer
2 * 67000, about, SDS-PAGE
Homo sapiens
More
the regions around transmembrane domains (TMs) 2, 5 and 3 are critical for the correct dimerization of ABCD4
Homo sapiens
Cloned(Commentary) (protein specific)
Commentary
Organism
gene ABCD4, stable recombinant expression of human ABCD4 in CHO cells, recombinant expression of N-terminally MBP-tagged enzyme, stable recombinant expression of wild-type and mutant HA-tagged ABCD4 in human hepatoma HuH7 cells and additional transient coexpression of wild-type and mutant GFP-tagged LMBRD1
Homo sapiens
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
generation of chimeric ABCD4 proteins that are exchanged in terms of the corresponding putative transmembrane helix with ABCD1 (based on the secondary structure of the eukaryotic P-glycoprotein homolog CmABCB1) in HEK-293 cells, endogenous human ABCD1 does not interact with LMBD1. Construction of ABCD4 chimeras 1-6 and analysis of the localization of chimeric ABCD4s in CHO cells stably expressing LMBD1-GFP. The wild-type ABCD4 co-expressed with LMBD1 exhibits a punctate distribution that is superimposable on the distribution pattern of LMBD1. The distribution patterns of the ABCD4 chimeras 1, 3, 4 and 6 also display the same pattern as LMBD1. But ABCD4 chimeras 2 and 5 do not exhibit a punctate pattern, but rather, a reticulum-like distribution pattern that is not superimposable on LMBD1
Homo sapiens
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
endoplasmic reticulum membrane
translocation of the ABC transporter ABCD4 from the endoplasmic reticulum to lysosomes requires the escort protein LMBD1
Homo sapiens
5789
-
lysosomal membrane
translocation of the ABC transporter ABCD4 from the endoplasmic reticulum to lysosomes requires the escort protein LMBD1
Homo sapiens
5765
-
additional information
LMBD1 associates with ABCD4 at the ER membrane and transports ABCD4 to lysosomes, ABCD4 interacts with LMBD1. The translocation depends on the lysosomal targeting ability of LMBD1. Endogenous ABCD4 is localized to both lysosomes and the endoplasmic reticulum. ABCD4 lacks the NH2-teminal hydrophobic region that is responsible for the targeting to peroxisomes. ABCD4 and LMBD1 form complex in vitro. The regions around transmembrane helix 2 and 5 of ABCD4 are critically important for the translocation of ABCD4 to lysosomes along with LMBD1
Homo sapiens
-
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1]
Homo sapiens
-
ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1]
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1]
-
752200
Homo sapiens
ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1]
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
2 * 67000, about, SDS-PAGE
Homo sapiens
More
the regions around transmembrane domains (TMs) 2, 5 and 3 are critical for the correct dimerization of ABCD4
Homo sapiens
General Information
General Information
Commentary
Organism
malfunction
mutations in ABCD4 result in a failure to release vitamin B12 from lysosomes. A similar phenotype is caused by mutations in gene LMBRD1, which encodes the lysosomal membrane protein LMBD1. ABCD4 lysosomal localization is disturbed by knockout of LMBRD. Mutation of ABCD4, which is known as the cblJ complementation group, results in the failure of the release of cobalamin from lysosomes. A similar phenotype in patients within the cblF group is caused by mutations of LMBD1, a lysosomal membrane protein. Mistargeting of mutant LMBD1 affects the distribution of ABCD4. Thus, mutations of ABCD4 and LMBD1 result in a quite similar phenotype. A putative region of ABCD4 that interacts with LMBD1 might be masked by the exchange of the regions around transmembrane domains (TMs) 2 and 5
Homo sapiens
physiological function
ABCD4 is a transporter of cobalamin and forms a complex with LMBD1 for the proper targeting or functioning, or both. The two proteins function as a complex
Homo sapiens
General Information (protein specific)
General Information
Commentary
Organism
malfunction
mutations in ABCD4 result in a failure to release vitamin B12 from lysosomes. A similar phenotype is caused by mutations in gene LMBRD1, which encodes the lysosomal membrane protein LMBD1. ABCD4 lysosomal localization is disturbed by knockout of LMBRD. Mutation of ABCD4, which is known as the cblJ complementation group, results in the failure of the release of cobalamin from lysosomes. A similar phenotype in patients within the cblF group is caused by mutations of LMBD1, a lysosomal membrane protein. Mistargeting of mutant LMBD1 affects the distribution of ABCD4. Thus, mutations of ABCD4 and LMBD1 result in a quite similar phenotype. A putative region of ABCD4 that interacts with LMBD1 might be masked by the exchange of the regions around transmembrane domains (TMs) 2 and 5
Homo sapiens
physiological function
ABCD4 is a transporter of cobalamin and forms a complex with LMBD1 for the proper targeting or functioning, or both. The two proteins function as a complex
Homo sapiens
Other publictions for EC 7.6.2.8
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
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7
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2
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751644
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2
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751661
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Escherichia coli
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8
1652
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752215
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7
14296
2017
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752221
Mireku
Conformational change of a tr ...
Escherichia coli
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7
41575
2017
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1
8
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3
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750063
Priess
Release of entropic spring re ...
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110
2407-2418
2016
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751956
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11
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752200
Kawaguchi
Translocation of the ABC tran ...
Homo sapiens
Sci. Rep.
6
30183
2016
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734003
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Escherichia coli
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16
17933-17951
2015
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734281
Joseph
Conformational cycle of the vi ...
Escherichia coli
J. Biol. Chem.
289
3176-3185
2014
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734760
Korkhov
Structure of AMP-PNP-bound Btu ...
Escherichia coli
Nat. Struct. Mol. Biol.
21
1097-1099
2014
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734820
Gopinath
A vitamin B12 transporter in M ...
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Open Biology
3
120175
2013
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719509
Korkhov
Asymmetric states of vitamin B ...
Escherichia coli
FEBS Lett.
586
972-976
2012
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720849
Weng
-
The conformational transition ...
Escherichia coli
PLoS ONE
7
e305465
2012
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734771
Korkhov
Structure of AMP-PNP-bound vit ...
Escherichia coli
Nature
490
367-372
2012
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719930
Di Bartolo
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