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Information on EC 7.6.2.4 - ABC-type fatty-acyl-CoA transporter and Organism(s) Mus musculus and UniProt Accession Q61285
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7.6.2.4 ABC-type fatty-acyl-CoA transporterIUBMB 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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- 7.6.2.4
- cerebral
- cardiac
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admission
- consciousness
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admitted
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resuscitation
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survivors
- artery
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discharge
- intracranial
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hypothermia
- hemorrhage
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glasgow
- stroke
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out-of-hospital
- trauma
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x-linked
- seizure
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traumatic
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ventilation
- encephalopathy
- brainstem
- reflex
- woman
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angiography
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cardiopulmonary
- hematoma
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subarachnoid
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unconscious
- epilepticus
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somatosensory
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sedation
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electroencephalogram
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electroencephalography
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subdural
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vlcfas
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neurosurgical
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intubation
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awaken
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pupillary
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evacuation
- pupil
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rewarming
- hemiparesis
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herniation
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in-hospital
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normothermia
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nontraumatic
- medicine
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craniectomy
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prehospital
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
fatty-acyl-CoA-transporting ATPase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
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
9000-83-3
-
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 + fatty acyl CoA[side 1]
ADP + phosphate + fatty acyl CoA[side 2]
-
-
-
?
ATP + H2O + fatty acyl CoA[side 1]
ADP + phosphate + fatty acyl CoA[side 2]
-
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
-
-
?
ATP + H2O + fatty acyl CoA/cis
ADP + phosphate + fatty acyl CoA/trans
-
-
-
?
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 + fatty acyl CoA[side 1]
ADP + phosphate + fatty acyl CoA[side 2]
-
-
-
?
ATP + H2O + fatty acyl CoA[side 1]
ADP + phosphate + fatty acyl CoA[side 2]
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
the microglial cells expressing ABCD2 chimeric homodimers (ABCD2-ABCD2 plus ABCD2-ABCD2-EGFP) also show tetramer formation of the proteins
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
ABCD1 and its homologue ABCD2 exist mainly as homotetramers in the peroxisomal membrane, quaternary structure of the ABCD2 protein in the peroxisomal membrane, overview
ABCD1 and its homologue ABCD2 exist mainly as homotetramers in the peroxisomal membrane, quaternary structure of the ABCD1 protein in the peroxisomal membrane, overview
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the ABCD2 transporter belongs to the D subfamily of the ATP-binding cassette (ABC)2 transporter family and is encoded by the ABCD1 gene
physiological function
ABCD1 and its homologue ABCD2 are peroxisomal ATP-binding cassette (ABC) half-transporters of fatty acyl-CoAs with both distinct and overlapping substrate specificities
evolution
the ABCD1 transporter belongs to the D subfamily of the ATP-binding cassette (ABC)2 transporter family and is encoded by the ABCD1 gene
physiological function
ABCD1 and its homologue ABCD2 are peroxisomal ATP-binding cassette (ABC) half-transporters of fatty acyl-CoAs with both distinct and overlapping substrate specificities
additional information
additional information
absence of interaction between solubilized ABCD1 and ABCD2 within supradimeric assemblies, but ABCD1 interacts with ABCD2 in the BV-2 microglial cell line and in cell lysates, interaction analysis. ABCD1 and ABCD2 tetrameric assemblies remain unchanged during the catalytic cycle of the transporters
additional information
absence of interaction between solubilized ABCD1 and ABCD2 within supradimeric assemblies, but ABCD1 interacts with ABCD2 in the BV-2 microglial cell line and in cell lysates, interaction analysis. ABCD1 and ABCD2 tetrameric assemblies remain unchanged during the catalytic cycle of the transporters
additional information
absence of interaction between solubilized ABCD1 and ABCD2 within supradimeric assemblies, but ABCD1 interacts with ABCD2 in the BV-2 microglial cell line and in cell lysates, interaction analysis. ABCD1 and ABCD2 tetrameric assemblies remain unchanged during the catalytic cycle of the transporters
additional information
absence of interaction between solubilized ABCD1 and ABCD2 within supradimeric assemblies, but ABCD1 interacts with ABCD2 in the BV-2 microglial cell line and in cell lysates, interaction analysis. ABCD1 and ABCD2 tetrameric assemblies remain unchanged during the catalytic cycle of the transporters
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). ABCD2_MOUSE
741
0
83457
Swiss-Prot
Mitochondrion (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
111000
monomer of EGFP-tagged ABCD2 protein, sucrose density sedimentation centrifugation analysis
270000 - 515000
tetramer of EGFP-tagged ABCD2 protein, sucrose density sedimentation centrifugation analysis
215000 - 415000
tetramer of ABCD1 protein, sucrose density sedimentation centrifugation analysis
300000 - 400000
-
PMP70, ALDP and ALDPR are found as large protein complexes upon sucrose density gradient centrifugation, since the sedimentation properties of a solubilized membrane protein also depend on its partial specific volume, shape and amount and type of protein-bound detergents/membrane lipids, no conclusions about regarding the true size of the observed protein complexes can be inferred
82000
monomer of ABCD1 protein, sucrose density sedimentation centrifugation analysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotetramer
quaternary structure of the ABCD2 protein in the peroxisomal membrane, overview
homodimer
quaternary structure of the ABCD2 protein in the peroxisomal membrane, overview
homotetramer
quaternary structure of the ABCD2 protein in the peroxisomal membrane, overview
heterotetramer
quaternary structure of the ABCD1 protein in the peroxisomal membrane, overview
homodimer
quaternary structure of the ABCD1 protein in the peroxisomal membrane, overview
homotetramer
quaternary structure of the ABCD1 protein in the peroxisomal membrane, overview
additional information
additional information
both transporters, ABCD1 and ABCD2, exist as both homo- and heterotetramers, with a predominance of homotetramers. In addition to tetramers, some larger molecular ABCD assemblies are also found but represent only a minor fraction
additional information
both transporters, ABCD1 and ABCD2, exist as both homo- and heterotetramers, with a predominance of homotetramers. In addition to tetramers, some larger molecular ABCD assemblies are also found but represent only a minor fraction
additional information
-
ALDP, ALDRP and PMP70 have the structure of ABC half-transporters
additional information
both transporters, ABCD1 and ABCD2, exist as both homo- and heterotetramers, with a predominance of homotetramers. In addition to tetramers, some larger molecular ABCD assemblies are also found but represented only a minor fraction
additional information
both transporters, ABCD1 and ABCD2, exist as both homo- and heterotetramers, with a predominance of homotetramers. In addition to tetramers, some larger molecular ABCD assemblies are also found but represented only a minor fraction
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ALDP, preparative immunoprecipitation, PMP70, incubation in ATP-agarose and sucrose gradient centrifugation
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of EGFP-tagged enzyme in COS-7 cells and in Rattus norvegicus H4IIEC3 hepatoma cell model, microglial BV-2 cells expressing ABCD2 chimeric homodimers (ABCD2-ABCD2 plus ABCD2-ABCD2-EGFP) also show tetramer formation of the proteins
gene ABCD1, recombinant expression of the enzyme in COS-7 cells and in Rattus norvegicus H4IIEC3 hepatoma cell model
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
a correction of the biochemical defect of X-linked adrenoleukodystrophy could be possible by drug-induced overexpression or ectopic expression of adrenoleukodystrophy-related protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
Guimaraes, C.P.; Domingues, P.; Aubourg, P.; Fouquet, F.; Pujol, A.; Jimenez-Sanchez, G.; Sa-Miranda, C.; Azevedo, J.E.
Mouse liver PMP70 and ALDP: homomeric interactions prevail in vivo
Biochim. Biophys. Acta
1689
235-243
2004
Mus musculus
Geillon, F.; Gondcaille, C.; Raas, Q.; Dias, A.M.M.; Pecqueur, D.; Truntzer, C.; Lucchi, G.; Ducoroy, P.; Falson, P.; Savary, S.; Trompier, D.
Peroxisomal ATP-binding cassette transporters form mainly tetramers
J. Biol. Chem.
292
6965-6977
2017
Mus musculus (P48410), Mus musculus (Q61285)
EXTERNAL LINKS (specific for EC-Number 7.6.2.4)
Transporter Classification Database (TCDB): 3.A.1.203.5
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