ABCD1
entrez
215
canonical
uniprot
P33897
canonical
ensembl
ENSG00000101986
resolver
ensp
ENSP00000218104
resolver
ensp
ENSP00000532366
resolver
enst
ENST00000218104
resolver
genesymbol
ABCD1
resolver
genesymbol_syn
ALD
resolver
hgnc
HGNC:61
resolver
uniprot
Q6GTZ2
resolver
uniprot_entry
ABCD1_HUMAN
resolver
uniprot_sec
Q6GTZ2
resolver
activity_regulation
ACTIVITY REGULATION: The cysteine-reactive reagent p-chloromercuribenzoic acid (pCMB) strongly decreased the ACOT activity. The serine esterase inhibitors phenylmethylsulfonyl fluoride (PMSF), diisopropylfluorophosphate (DFP) and bis-(4-nitrophenyl)phosphate (BNPP) moderately reduced the ACOT activity. The histidine-reacting reagent diethyl pyrocarbonate (DEPC) has no effect on the ACOT activity. {ECO:0000269|PubMed:33500543}.
uniprot
proteins
amino_acid_sequence
MPVLSRPRPWRGNTLKRTAVLLALAAYGAHKVYPLVRQCLAPARGLQAPAGEPTQEASGVAAAKAGMNRVFLQRLLWLLRLLFPRVLCRETGLLALHSAALVSRTFLSVYVARLDGRLARCIVRKDPRAFGWQLLQWLLIALPATFVNSAIRYLEGQLALSFRSRLVAHAYRLYFSQQTYYRVSNMDGRLRNPDQSLTEDVVAFAASVAHLYSNLTKPLLDVAVTSYTLLRAARSRGAGTAWPSAIAGLVVFLTANVLRAFSPKFGELVAEEARRKGELRYMHSRVVANSEEIAFYGGHEVELALLQRSYQDLASQINLILLERLWYVMLEQFLMKYVWSASGLLMVAVPIITATGYSESDAEAVKKAALEKKEEELVSERTEAFTIARNLLTAAADAIERIMSSYKEVTELAGYTARVHEMFQVFEDVQRCHFKRPRELEDAQAGSGTIGRSGVRVEGPLKIRGQVVDVEQGIICENIPIVTPSGEVVVASLNIRVEEGMHLLITGPNGCGKSSLFRILGGLWPTYGGVLYKPPPQRMFYIPQRPYMSVGSLRDQVIYPDSVEDMQRKGYSEQDLEAILDVVHLHHILQREGGWEAMCDWKDVLSGGEKQRIGMARMFYHRPKYALLDECTSAVSIDVEGKIFQAAKDAGIALLSITHRPSLWKYHTHLLQFDGEGGWKFEKLDSAARLSLTEEKQRLEQQLAGIPKMQRRLQELCQILGEAVAPAHVPAPSPQGPGGLQGAST
uniprot
proteins
disease_involvement
DISEASE: Adrenoleukodystrophy (ALD) [MIM:300100]: A peroxisomal metabolic disorder characterized by progressive multifocal demyelination of the central nervous system and by peripheral adrenal insufficiency (Addison disease). It results in mental deterioration, corticospinal tract dysfunction, and cortical blindness. Different clinical manifestations exist like: cerebral childhood ALD (CALD), adult cerebral ALD (ACALD), adrenomyeloneuropathy (AMN) and 'Addison disease only' (ADO) phenotype. {ECO:0000269|PubMed:10190819, ECO:0000269|PubMed:10227685, ECO:0000269|PubMed:10369742, ECO:0000269|PubMed:10480364, ECO:0000269|PubMed:10551832, ECO:0000269|PubMed:10737980, ECO:0000269|PubMed:10980539, ECO:0000269|PubMed:11248239, ECO:0000269|PubMed:11438993, ECO:0000269|PubMed:11748843, ECO:0000269|PubMed:11810273, ECO:0000269|PubMed:20661612, ECO:0000269|PubMed:21700483, ECO:0000269|PubMed:21889498, ECO:0000269|PubMed:21966424, ECO:0000269|PubMed:23651979, ECO:0000269|PubMed:26686776, ECO:0000269|PubMed:28456143, ECO:0000269|PubMed:7561948, ECO:0000269|PubMed:7581394, ECO:0000269|PubMed:7668254, ECO:0000269|PubMed:7717396, ECO:0000269|PubMed:7825602, ECO:0000269|PubMed:7849723, ECO:0000269|PubMed:7860075, ECO:0000269|PubMed:7904210, ECO:0000269|PubMed:8040304, ECO:0000269|PubMed:8566952, ECO:0000269|PubMed:8651290, ECO:0000269|PubMed:9452087, ECO:0000269|PubMed:9553942, ECO:0000269|PubMed:9584268}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Note=The promoter region of ABCD1 is deleted in the chromosome Xq28 deletion syndrome which involves ABCD1 and the neighboring gene BCAP31. {ECO:0000269|PubMed:11992258}.
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 involved in the transport of very long chain fatty acid (VLCFA)-CoA from the cytosol to the peroxisome lumen (PubMed:11248239, PubMed:15682271, PubMed:16946495, PubMed:18757502, PubMed:21145416, PubMed:23671276, PubMed:29397936, PubMed:33500543). Coupled to the ATP-dependent transporter activity also has a fatty acyl-CoA thioesterase activity (ACOT) and hydrolyzes VLCFA-CoA into VLCFA prior their ATP-dependent transport into peroxisomes, the ACOT activity is essential during this transport process (PubMed:29397936, PubMed:33500543). Thus, plays a role in regulation of VLCFAs and energy metabolism namely, in the degradation and biosynthesis of fatty acids by beta-oxidation, mitochondrial function and microsomal fatty acid elongation (PubMed:21145416, PubMed:23671276). Involved in several processes; namely, controls the active myelination phase by negatively regulating the microsomal fatty acid elongation activity and may also play a role in axon and myelin maintenance. Also controls the cellular response to oxidative stress by regulating mitochondrial functions such as mitochondrial oxidative phosphorylation and depolarization. And finally controls the inflammatory response by positively regulating peroxisomal beta-oxidation of VLCFAs (By similarity). {ECO:0000250|UniProtKB:P48410, ECO:0000269|PubMed:11248239, ECO:0000269|PubMed:15682271, ECO:0000269|PubMed:16946495, ECO:0000269|PubMed:18757502, ECO:0000269|PubMed:21145416, ECO:0000269|PubMed:23671276, ECO:0000269|PubMed:29397936, ECO:0000269|PubMed:33500543}.
uniprot
proteins
mass_dalton
82937
uniprot
proteins
mutagenesis
MUTAGEN 67; /note="M->P: Does not affect PEX19 interaction."; /evidence="ECO:0000269|PubMed:15781447"; MUTAGEN 68; /note="N->P: Does not affect PEX19 interaction."; /evidence="ECO:0000269|PubMed:15781447"; MUTAGEN 69; /note="R->P: Does not affect PEX19 interaction."; /evidence="ECO:0000269|PubMed:15781447"; MUTAGEN 70; /note="V->P: Does not affect PEX19 interaction."; /evidence="ECO:0000269|PubMed:15781447"; MUTAGEN 71; /note="F->P: Does not affect PEX19 interaction."; /evidence="ECO:0000269|PubMed:15781447"; MUTAGEN 72; /note="L->P: Does not affect PEX19 interaction."; /evidence="ECO:0000269|PubMed:15781447"; MUTAGEN 73; /note="Q->P: Does not affect PEX19 interaction."; /evidence="ECO:0000269|PubMed:15781447"; MUTAGEN 74; /note="R->P: Does not affect PEX19 interaction."; /evidence="ECO:0000269|PubMed:15781447"; MUTAGEN 75; /note="L->P: Impairs PEX19 interaction."; /evidence="ECO:0000269|PubMed:15781447"; MUTAGEN 76; /note="L->P: Impairs PEX19 interaction."; /evidence="ECO:0000269|PubMed:15781447"; MUTAGEN 77; /note="W->P: Does not affect PEX19 interaction."; /evidence="ECO:0000269|PubMed:15781447"; MUTAGEN 78; /note="L->P: Impairs PEX19 interaction."; /evidence="ECO:0000269|PubMed:15781447"; MUTAGEN 79; /note="L->P: Impairs PEX19 interaction."; /evidence="ECO:0000269|PubMed:15781447"; MUTAGEN 80; /note="R->P: Does not affect PEX19 interaction."; /evidence="ECO:0000269|PubMed:15781447"; MUTAGEN 81; /note="L->P: Does not affect PEX19 interaction."; /evidence="ECO:0000269|PubMed:15781447"; MUTAGEN 82; /note="L->P: Does not affect PEX19 interaction."; /evidence="ECO:0000269|PubMed:15781447"; MUTAGEN 83; /note="F->P: Does not affect PEX19 interaction."; /evidence="ECO:0000269|PubMed:15781447"; MUTAGEN 513; /note="K->A: Does not affect ACOT activity. Transport activity of VLCFA is strongly reduced."; /evidence="ECO:0000269|PubMed:33500543
uniprot
proteins
post_translational_modification
PTM: Tyrosine-phosphorylated. {ECO:0000250|UniProtKB:D3ZHR2}.
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
10190819
uniprot
proteins
pubmed
10227685
uniprot
proteins
pubmed
10369742
uniprot
proteins
pubmed
10480364
uniprot
proteins
pubmed
10551832
uniprot
proteins
pubmed
10704444
uniprot
proteins
pubmed
10737980
uniprot
proteins
pubmed
10777694
uniprot
proteins
pubmed
10980539
uniprot
proteins
pubmed
11248239
uniprot
proteins
pubmed
11438993
uniprot
proteins
pubmed
11748843
uniprot
proteins
pubmed
11810273
uniprot
proteins
pubmed
11992258
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15643618
uniprot
proteins
pubmed
15682271
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
15781447
uniprot
proteins
pubmed
16213491
uniprot
proteins
pubmed
16946495
uniprot
proteins
pubmed
17609205
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18757502
uniprot
proteins
pubmed
20661612
uniprot
proteins
pubmed
21145416
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21700483
uniprot
proteins
pubmed
21889498
uniprot
proteins
pubmed
21966424
uniprot
proteins
pubmed
23651979
uniprot
proteins
pubmed
23671276
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26686776
uniprot
proteins
pubmed
28456143
uniprot
proteins
pubmed
29397936
uniprot
proteins
pubmed
33500543
uniprot
proteins
pubmed
34337821
uniprot
proteins
pubmed
7561948
uniprot
proteins
pubmed
7581394
uniprot
proteins
pubmed
7668254
uniprot
proteins
pubmed
7717396
uniprot
proteins
pubmed
7825602
uniprot
proteins
pubmed
7849723
uniprot
proteins
pubmed
7860075
uniprot
proteins
pubmed
7904210
uniprot
proteins
pubmed
8040304
uniprot
proteins
pubmed
8441467
uniprot
proteins
pubmed
8566952
uniprot
proteins
pubmed
8651290
uniprot
proteins
pubmed
9452087
uniprot
proteins
pubmed
9553942
uniprot
proteins
pubmed
9584268
uniprot
proteins
sequence_length
745
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:10777694, ECO:0000269|PubMed:16946495, ECO:0000269|PubMed:17609205, ECO:0000269|PubMed:18757502, ECO:0000269|PubMed:29397936}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:16946495}; Multi-pass membrane protein. Lysosome membrane {ECO:0000269|PubMed:16946495}; Multi-pass membrane protein. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16946495}; Multi-pass membrane protein.
uniprot
proteins
transmembrane_region
TRANSMEM 92..112; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 131..151; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 238..258; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 333..353; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"; TRANSMEM 473..493; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00441
uniprot
proteins