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Information on EC 7.6.2.4 - ABC-type fatty-acyl-CoA transporter and Organism(s) Homo sapiens and UniProt Accession P28288

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IUBMB Comments
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. An animal and yeast enzyme that transports fatty acyl CoA into and out of peroxisomes. In humans, it is associated with Zellweger's syndrome.
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Homo sapiens
UNIPROT: P28288
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
+
+
fatty acyl CoA[side 1]
=
+
+
fatty acyl CoA[side 2]
Synonyms
comatose, abcd1, abcd2, pmp70, abcd3, adrenoleukodystrophy protein, aldrp, pat1p, 70-kda peroxisomal membrane protein, peroxisomal abc transporter, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ATP-binding cassette sub-family D member 3
UniProt
70-kDa peroxisomal membrane protein
-
-
ABCD1
ABCD2
adrenoleukodystrophy protein
-
-
ALDRP
-
-
fatty-acyl-CoA-transporting ATPase
peroxisomal ABC transporter
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
transmembrane transport
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (ABC-type, fatty-acyl-CoA-transporting)
An ATP-binding cassette (ABC) type transporter, characterized by the presence of two similar ATP-binding domains/proteins and two integral membrane domains/proteins. Does not undergo phosphorylation during the transport process. An animal and yeast enzyme that transports fatty acyl CoA into and out of peroxisomes. In humans, it is associated with Zellweger's syndrome.
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 + C10-carnitine[side 1]
ADP + phosphate + C10-carnitine[side 2]
show the reaction diagram
low activity
-
-
?
ATP + H2O + C12-carnitine[side 1]
ADP + phosphate + C12-carnitine[side 2]
show the reaction diagram
-
-
-
?
ATP + H2O + C16-carnitine[side 1]
ADP + phosphate + C16-carnitine[side 2]
show the reaction diagram
-
-
-
?
ATP + H2O + fatty acyl CoA[side 1]
ADP + phosphate + fatty acyl CoA[side 2]
show the reaction diagram
ATP + H2O + lauroyl-CoA[side 1]
ADP + phosphate + lauroyl-CoA[side 2]
show the reaction diagram
-
-
-
?
ATP + H2O + NBD-palmitoyl-CoA[side 1]
ADP + phosphate + NBD-palmitoyl-CoA[side 2]
show the reaction diagram
-
-
-
?
ATP + H2O + palmitoyl-CoA[side 1]
ADP + phosphate + palmitoyl-CoA[side 2]
show the reaction diagram
-
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
show the reaction diagram
ATP + H2O + fatty acyl CoA[side 1]
ADP + phosphate + fatty acyl CoA[side 2]
show the reaction diagram
ATP + H2O + NBD-palmitoyl-CoA[side 1]
ADP + phosphate + NBD-palmitoyl-CoA[side 2]
show the reaction diagram
-
-
-
?
additional information
?
-
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 + C12-carnitine[side 1]
ADP + phosphate + C12-carnitine[side 2]
show the reaction diagram
-
-
-
?
ATP + H2O + C16-carnitine[side 1]
ADP + phosphate + C16-carnitine[side 2]
show the reaction diagram
-
-
-
?
ATP + H2O + fatty acyl CoA[side 1]
ADP + phosphate + fatty acyl CoA[side 2]
show the reaction diagram
ATP + H2O + lauroyl-CoA[side 1]
ADP + phosphate + lauroyl-CoA[side 2]
show the reaction diagram
-
-
-
?
ATP + H2O + palmitoyl-CoA[side 1]
ADP + phosphate + palmitoyl-CoA[side 2]
show the reaction diagram
-
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
show the reaction diagram
ATP + H2O + fatty acyl CoA[side 1]
ADP + phosphate + fatty acyl CoA[side 2]
show the reaction diagram
additional information
?
-
peroxisomes accept the CoA and carnitine ester of C12:0 andC16:0 as substrate in a mechanism possibly involving ABCD3. Production of CO2 and acid-soluble products from[1-14C]C16-carnitine. Concentrations of the C16:1-, C16-, C18:2-, C18:1-, and C18-carnitines and the ratio (C16+C18:1) in CPT2 inhibited cells, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
AlF3
moderate inhibition of the ATPase activity of liposome-reconstituted His-hABCD3
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Pex19p
-
protein required for the peroxisomal membrane synthesis, binds to PMP70 co-translationally and keeps PMP70 in a proper conformation for the localization to peroxisome, PMP70 forms 75% aggregates during translation in the absence of Pex19p
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
X-ALD fibroblast lacking ALDP
Manually annotated by BRENDA team
-
SV40-transformed, from a patient with X-linked adrenoleukodystrophy missense mutation A626T
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
when the N-terminal 80 amino acid residue (N80)-segment preceding transmembrane segment (TM) 1 is deleted and the TM1-TM2 region is fused to EGFP, the TM1 segment induces endoplasmic reticulum-targeting
Manually annotated by BRENDA team
-
when the N-terminal 80-segment is fused to EGFP, the fusion protein is targeted to the outer mitochondrial membrane
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
the peroxisomal import of fatty acids is mediated by 3 ATP-binding cassette transporters (ABCD1, -2, and -3). Transport mediated by ABCD3 is crucial in the peroxisomal degradation of medium-chain fatty acids and might be involved in the production of CO2 and acid-soluble products from C16-carnitine. Mitochondrial FAO inhibition with etomoxir does not lead to significant accumulation of any acylcarnitine species
physiological function
the D-bifunctional protein (HSD17B4) and the peroxisomal ABC transporter ABCD3 are essential in peroxisomal oxidation of lauric and palmitic acid, besides mitochondrial carnitine palmitoyltransferase (CPT)2 (EC 2.3.1.21), leading to the production of peroxisomal acylcarnitine intermediates. Peroxisomes accept acyl-CoAs and oxidize acylcarnitines in a similar biochemical pathway as the mitochondria. Peroxisomal fatty acid beta-oxidation (FAO) is important when mitochondrial FAO is defective or overloaded. The peroxisomal import of fatty acids is mediated by 3 ATP-binding cassette transporters (ABCD1, -2, and -3). Transport mediated by ABCD3 is crucial in the peroxisomal degradation of medium-chain fatty acids. The peroxisomal ABC transporters transport acyl-CoA intermediates and C12/C16-carnitines, peroxisomes accept the CoA and carnitine ester of C12:0 and C16:0 as substrate in a mechanism possibly involving ABCD3
evolution
physiological function
-
ABC transporter ALDP interacts with ACLY and FATP4, ABC transporter PMP70 interacts with FASN and FATP4 involved in fatty acid metabolism, thus constituting a fatty acid synthesis-transport machinery at the cytoplasmic side of the peroxisomal membrane
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ABCD3_HUMAN
659
0
75476
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70000
75000
-
monomer, SDS-PAGE and immunoblotting
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 70000, recombinant His-tagged ABCD3
homodimer
dimerization is considered as an obligatory step for stability and function of peroxisomal ABC transporters
dimer
homodimer
dimerization is considered as an obligatory step for stability and function of peroxisomal ABC transporters
additional information
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ALDP390
-
mutant, comprises the amino acids 1 to 390
ALDP550
-
mutant, comprises the amino acids 1 to 550
ALDP658
-
mutant, comprises the amino acids 1 to 658
ALDPDELTA551-657
-
mutant, residues 551-657 are deleted
ALDPDELTANBF
-
mutant, residues 391-657 are deleted
G116R
-
naturally occuring missense mutation
H667D
-
naturally occuring missense mutation
Q544R
-
naturally occuring missense mutation
R104C
-
naturally occuring missense mutation
R617H
-
naturally occuring missense mutation
S342P
-
naturally occuring missense mutation
S606L
-
naturally occuring missense mutation
S606P
-
naturally occuring missense mutation
Y174C
-
naturally occuring missense mutation
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dimerization is considered as an obligatory step for stability and function of peroxisomal ABC transporters
dimerization is considered as an obligatory step for stability and function of peroxisomal ABC transporters
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged protein ABCD3 from Pichia pastoris strain SMD1168 by detergent solubilization and nickel affinity chromatography, evaluation of diverse detergents
recombinant His-tagged protein ABCD1 from Pichia pastoris strain SMD1168 by detergent solubilization and nickel affinity chromatography, evaluation of diverse detergents
recombinant His-tagged protein ABCD2 from Pichia pastoris strain SMD1168 by detergent solubilization and nickel affinity chromatography, evaluation of diverse detergents
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ABCD3, recombinant expression in enzyme-deficient CPT2/ABCD3 KO cells
gene ABCD3, recombinant expression of protein ABCD3 in Pichia pastoris strain SMD1168
gene ABCD1, recombinant expression of His-tagged protein ABCD1 in Pichia pastoris strain SMD1168
gene ABCD1, sequence comparisons with ABCD2 and ABCD3
gene ABCD2, recombinant expression of protein ABCD2 in Pichia pastoris strain SMD1168
into pECFP-N1 and pEYFP-N1 vectors for transfection of VERO cells
-
into pECFP-N1, pEYFP-N1, or pECFP-C1 vectors for transfection of VERO cells
-
into the pMAM2-BSD, pEGFPN-1 and pcDNA4HisMax TOP vector for transfection of CHO cells, and as templates for the construction of mutant cDNAs
-
using transient transfection of COS cells
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged protein ABCD3 protein solubilization and reconstitution in proteoliposomes
recombinant His-tagged protein ABCD1 protein solubilization and reconstitution in proteoliposomes
recombinant His-tagged protein ABCD2 protein solubilization and reconstitution in proteoliposomes, the liposome-reconstituted His-hABCD1 shows ATPase activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gartner, J.; Jimenez-Sanchez, G.; Roerig, P.; Valle, D.
Genomic organization of the 70-kDa peroxisomal membrane protein gene (PXMP1)
Genomics
48
203-208
1998
Homo sapiens
Manually annotated by BRENDA team
Liu, L.X.; Janvier, K.; Berteaux-Lecellier, V.; Cartier, N.; Benarous, R.; Aubourg, P.
Homo- and heterodimerization of peroxisomal ATP-binding cassette half-transporters
J. Biol. Chem.
274
32738-32743
1999
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Netik, A.; Forss-Petter, S.; Holzinger, A.; Molzer, B.; Unterrainer, G.; Berger, J.
Adrenoleukodystrophy-related protein can compensate functionally for adrenoleukodystrophy protein deficiency (X-ALD): implications for therapy
Hum. Mol. Genet.
8
907-913
1999
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Shani, N.; Valle, D.
A Saccharomyces cerevisiae homolog of the human adrenoleukodystrophy transporter is a heterodimer of two half ATP-binding cassette transporters
Proc. Natl. Acad. Sci. USA
93
11901-11906
1996
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
Kashiwayama, Y.; Asahina, K.; Shibata, H.; Morita, M.; Muntau, A.C.; Roscher, A.A.; Wanders, R.J.; Shimozawa, N.; Sakaguchi, M.; Kato, H.; Imanaka, T.
Role of Pex19p in the targeting of PMP70 to peroxisome
Biochim. Biophys. Acta
1746
116-128
2005
Homo sapiens
Manually annotated by BRENDA team
Hillebrand, M.; Verrier, S.E.; Ohlenbusch, A.; Schaefer, A.; Soeling, H.D.; Wouters, F.S.; Gaertner, J.
Live cell FRET microscopy: homo- and heterodimerization of two human peroxisomal ABC transporters, the adrenoleukodystrophy protein (ALDP, ABCD1) and PMP70 (ABCD3)
J. Biol. Chem.
282
26997-27005
2007
Homo sapiens
Manually annotated by BRENDA team
Takahashi, N.; Morita, M.; Maeda, T.; Harayama, Y.; Shimozawa, N.; Suzuki, Y.; Furuya, H.; Sato, R.; Kashiwayama, Y.; Imanaka, T.
Adrenoleukodystrophy: subcellular localization and degradation of adrenoleukodystrophy protein (ALDP/ABCD1) with naturally occurring missense mutations
J. Neurochem.
101
1632-1643
2007
Homo sapiens
Manually annotated by BRENDA team
Iwashita, S.; Tsuchida, M.; Tsukuda, M.; Yamashita, Y.; Emi, Y.; Kida, Y.; Komori, M.; Kashiwayama, Y.; Imanaka, T.; Sakaguchi, M.
Multiple organelle-targeting signals in the N-terminal portion of peroxisomal membrane protein PMP70
J. Biochem.
147
581-590
2010
Homo sapiens
Manually annotated by BRENDA team
van Roermund, C.W.; Visser, W.F.; Ijlst, L.; Waterham, H.R.; Wanders, R.J.
Differential substrate specificities of human ABCD1 and ABCD2 in peroxisomal fatty acid ?-oxidation
Biochim. Biophys. Acta
1811
148-152
2011
Homo sapiens, Homo sapiens (P33897)
Manually annotated by BRENDA team
Hillebrand, M.; Gersting, S.W.; Lotz-Havla, A.S.; Schaefer, A.; Rosewich, H.; Valerius, O.; Muntau, A.C.; Gaertner, J.
Identification of a new fatty acid synthesis-transport machinery at the peroxisomal membrane
J. Biol. Chem.
287
210-221
2012
Homo sapiens
Manually annotated by BRENDA team
Okamoto, T.; Kawaguchi, K.; Watanabe, S.; Agustina, R.; Ikejima, T.; Ikeda, K.; Nakano, M.; Morita, M.; Imanaka, T.
Characterization of human ATP-binding cassette protein subfamily D reconstituted into proteoliposomes
Biochem. Biophys. Res. Commun.
496
1122-1127
2018
Homo sapiens (P28288), Homo sapiens (P33897), Homo sapiens (Q9UBJ2)
Manually annotated by BRENDA team
Violante, S.; Achetib, N.; van Roermund, C.W.T.; Hagen, J.; Dodatko, T.; Vaz, F.M.; Waterham, H.R.; Chen, H.; Baes, M.; Yu, C.; Argmann, C.A.; Houten, S.M.
Peroxisomes can oxidize medium- and long-chain fatty acids through a pathway involving ABCD3 and HSD17B4
FASEB J.
33
4355-4364
2019
Homo sapiens (P28288)
Manually annotated by BRENDA team
Andreoletti, P.; Raas, Q.; Gondcaille, C.; Cherkaoui-Malki, M.; Trompier, D.; Savary, S.
Predictive structure and topology of peroxisomal ATP-binding cassette (ABC) transporters
Int. J. Mol. Sci.
18
E1593-E1607
2017
Homo sapiens (P28288), Homo sapiens (P33897), Homo sapiens (Q9UBJ2), Homo sapiens
Manually annotated by BRENDA team