ABCD3
entrez
5825
canonical
uniprot
P28288
canonical
ensembl
ENSG00000117528
resolver
ensp
ENSP00000326880
resolver
ensp
ENSP00000359233
resolver
ensp
ENSP00000536948
resolver
genesymbol
ABCD3
resolver
genesymbol_syn
PMP70
resolver
genesymbol_syn
PXMP1
resolver
hgnc
HGNC:67
resolver
uniprot
D3DT46
resolver
uniprot
Q15271
resolver
uniprot
Q6NUN5
resolver
uniprot
Q96DA3
resolver
uniprot
Q9H529
resolver
uniprot_entry
ABCD3_HUMAN
resolver
uniprot_sec
D3DT46
resolver
uniprot_sec
Q15271
resolver
uniprot_sec
Q6NUN5
resolver
uniprot_sec
Q96DA3
resolver
uniprot_sec
Q9H529
resolver
activity_regulation
ACTIVITY REGULATION: Substrate binding induces the dimerization of NBD domains and stimulation of ATPase activity. {ECO:0000269|PubMed:41428872}.
uniprot
proteins
amino_acid_sequence
MAAFSKYLTARNSSLAGAAFLLLCLLHKRRRALGLHGKKSGKPPLQNNEKEGKKERAVVDKVFFSRLIQILKIMVPRTFCKETGYLVLIAVMLVSRTYCDVWMIQNGTLIESGIIGRSRKDFKRYLLNFIAAMPLISLVNNFLKYGLNELKLCFRVRLTKYLYEEYLQAFTYYKMGNLDNRIANPDQLLTQDVEKFCNSVVDLYSNLSKPFLDIVLYIFKLTSAIGAQGPASMMAYLVVSGLFLTRLRRPIGKMTITEQKYEGEYRYVNSRLITNSEEIAFYNGNKREKQTVHSVFRKLVEHLHNFILFRFSMGFIDSIIAKYLATVVGYLVVSRPFLDLSHPRHLKSTHSELLEDYYQSGRMLLRMSQALGRIVLAGREMTRLAGFTARITELMQVLKDLNHGKYERTMVSQQEKGIEGVQVIPLIPGAGEIIIADNIIKFDHVPLATPNGDVLIRDLNFEVRSGANVLICGPNGCGKSSLFRVLGELWPLFGGRLTKPERGKLFYVPQRPYMTLGTLRDQVIYPDGREDQKRKGISDLVLKEYLDNVQLGHILEREGGWDSVQDWMDVLSGGEKQRMAMARLFYHKPQFAILDECTSAVSVDVEGYIYSHCRKVGITLFTVSHRKSLWKHHEYYLHMDGRGNYEFKQITEDTVEFGS
uniprot
proteins
disease_involvement
DISEASE: Congenital bile acid synthesis defect 5 (CBAS5) [MIM:616278]: An autosomal recessive disorder characterized by hepatosplenomegaly, hepatic fibrosis, progressive liver failure, and accumulation of peroxisomal C27-bile acid intermediates in plasma. {ECO:0000269|PubMed:25168382}. Note=The disease may be caused by variants affecting the gene represented in this entry.; DISEASE: Oculopharyngodistal myopathy 5 (OPDM5) [MIM:621446]: An autosomal dominant form of oculopharyngodistal myopathy, a muscle disorder characterized by progressive ptosis, external ophthalmoplegia, and weakness of the masseter, facial, pharyngeal, and distal limb muscles. The myopathological features are the presence of rimmed vacuoles in the muscle fibers and myopathic changes of differing severity. {ECO:0000269|PubMed:39068203}. Note=The disease is caused by variants affecting the gene represented in this entry. Pathogenic CCG repeat expansions in the 5'-UTR of ABCD3 have been found in patients of European ancestry. {ECO:0000269|PubMed:39068203}.
uniprot
proteins
ec_number
3.1.2.-
uniprot
proteins
ec_number
7.6.2.-
uniprot
proteins
function
FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC) family that catalyzes the transport of long- and very-long-chain fatty acyl-CoAs and probably bile acyl-CoAs from the cytosol to the peroxisome matrix for beta-oxydation. Appears to be specifically involved in the peroxisomal transport of branched-chain fatty acyl-CoAs (BCFA-CoAs) and dicarboxylic acyl CoAs (DCA-CoAs) (PubMed:11248239, PubMed:23671276, PubMed:24333844, PubMed:25168382, PubMed:29397936, PubMed:39223112, PubMed:41428872). Has fatty acyl-CoA thioesterase and ATPase activities. Probably hydrolyzes fatty acyl-CoAs into free fatty acids prior to their ATP-dependent transport into peroxisomes. {ECO:0000269|PubMed:11248239, ECO:0000269|PubMed:23671276, ECO:0000269|PubMed:24333844, ECO:0000269|PubMed:25168382, ECO:0000269|PubMed:25944712, ECO:0000269|PubMed:29397936, ECO:0000269|PubMed:39223112, ECO:0000269|PubMed:41428872}.
uniprot
proteins
mass_dalton
75476
uniprot
proteins
mutagenesis
MUTAGEN 21..23; /note="LLL->QQQ: Abolishes localization to peroxisomes."; /evidence="ECO:0000269|PubMed:17761678"; MUTAGEN 70..71; /note="IL->NQ: Abolishes localization to peroxisomes."; /evidence="ECO:0000269|PubMed:17761678"; MUTAGEN 96; /note="R->A: Significantly decreases phytanoyl-CoA-stimulated ATPase activity."; /evidence="ECO:0000269|PubMed:39223112"; MUTAGEN 111; /note="E->A: Significantly decreases phytanoyl-CoA-stimulated ATPase activity."; /evidence="ECO:0000269|PubMed:39223112"; MUTAGEN 144; /note="K->A: Significantly decreases substrate-stimulated ATPase activity."; /evidence="ECO:0000269|PubMed:39223112"; MUTAGEN 205; /note="S->A: Significantly decreases phytanoyl-CoA-stimulated ATPase activity."; /evidence="ECO:0000269|PubMed:39223112"; MUTAGEN 209; /note="K->A: Significantly decreases phytanoyl-CoA-stimulated ATPase activity."; /evidence="ECO:0000269|PubMed:39223112"; MUTAGEN 307..308; /note="IL->AA: Abolishes localization to peroxisomes."; /evidence="ECO:0000269|PubMed:17761678"; MUTAGEN 322; /note="K->A: Significantly decreases phytanoyl-CoA-stimulated ATPase activity."; /evidence="ECO:0000269|PubMed:39223112"; MUTAGEN 323; /note="Y->A: Significantly decreases phytanoyl-CoA-stimulated ATPase activity."; /evidence="ECO:0000269|PubMed:39223112"; MUTAGEN 330; /note="Y->A: Significantly decreases phytanoyl-CoA-stimulated ATPase activity."; /evidence="ECO:0000269|PubMed:39223112"; MUTAGEN 373; /note="R->A: Significantly decreases phytanoyl-CoA-stimulated ATPase activity."; /evidence="ECO:0000269|PubMed:39223112"; MUTAGEN 379; /note="R->A: Significantly decreases substrate-stimulated ATPase activity."; /evidence="ECO:0000269|PubMed:39223112"; MUTAGEN 383; /note="R->A: Significantly decreases substrate-stimulated ATPase activity."; /evidence="ECO:0000269|PubMed:39223112"; MUTAGEN 478; /note="G->R: Decreases ATP-binding affinity."; /evidence="ECO:0000269|PubMed:11248239"; MUTAGEN 572; /note="S->I: Decreases ATPase activity."; /evidence="ECO:0000269|PubMed:11248239"; MUTAGEN 596; /note="E->Q: No effect on ATP-binding affinity. Decreases ATPase activity, yielding a Vmax roughly one-third of the levels observed in the wild-type."; /evidence="ECO:0000269|PubMed:39223112
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation. {ECO:0000305|PubMed:23671276, ECO:0000305|PubMed:24333844}.; PATHWAY: Lipid metabolism; branched-chain fatty acid metabolism. {ECO:0000305|PubMed:24333844}.
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated by PEX2 during pexophagy in response to starvation, leading to its degradation. {ECO:0000269|PubMed:27597759}.
uniprot
proteins
protein_family
ABC transporter superfamily
uniprot
proteins
protein_family
ABCD family
uniprot
proteins
protein_family
Peroxisomal fatty acyl CoA transporter (TC 3.A.1.203) subfamily
uniprot
proteins
pubmed
10551832
uniprot
proteins
pubmed
10704444
uniprot
proteins
pubmed
10777694
uniprot
proteins
pubmed
11248239
uniprot
proteins
pubmed
1301993
uniprot
proteins
pubmed
1536884
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16344115
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17609205
uniprot
proteins
pubmed
17761678
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23671276
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24333844
uniprot
proteins
pubmed
25168382
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27597759
uniprot
proteins
pubmed
29397936
uniprot
proteins
pubmed
39068203
uniprot
proteins
pubmed
39223112
uniprot
proteins
pubmed
39419991
uniprot
proteins
pubmed
41428872
uniprot
proteins
pubmed
9521874
uniprot
proteins
pubmed
9539740
uniprot
proteins
sequence_length
659
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:10704444, ECO:0000269|PubMed:16344115, ECO:0000269|PubMed:17761678, ECO:0000269|PubMed:24333844, ECO:0000269|PubMed:29397936}; Multi-pass membrane protein {ECO:0000305|PubMed:39223112}.
uniprot
proteins
transmembrane_region
TRANSMEM 83..103; /note="Helical"; /evidence="ECO:0000305|PubMed:39223112, ECO:0000312|PDB:8Z0F"; TRANSMEM 128..149; /note="Helical"; /evidence="ECO:0000305|PubMed:39223112, ECO:0000312|PDB:8Z0F"; TRANSMEM 199..218; /note="Helical"; /evidence="ECO:0000305|PubMed:39223112, ECO:0000312|PDB:8Z0F"; TRANSMEM 232..248; /note="Helical"; /evidence="ECO:0000305|PubMed:39223112, ECO:0000312|PDB:8Z0F"; TRANSMEM 307..328; /note="Helical"; /evidence="ECO:0000305|PubMed:39223112, ECO:0000312|PDB:8Z0F"; TRANSMEM 363..382; /note="Helical"; /evidence="ECO:0000305|PubMed:39223112, ECO:0000312|PDB:8Z0F
uniprot
proteins