ABCD1_HUMAN
ID ABCD1_HUMAN Reviewed; 745 AA.
AC P33897; Q6GTZ2;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 236.
DE RecName: Full=ATP-binding cassette sub-family D member 1 {ECO:0000305};
DE EC=3.1.2.- {ECO:0000269|PubMed:29397936, ECO:0000269|PubMed:33500543};
DE EC=7.6.2.- {ECO:0000269|PubMed:11248239, ECO:0000269|PubMed:29397936, ECO:0000269|PubMed:33500543, ECO:0000305|PubMed:16946495, ECO:0000305|PubMed:23671276};
DE AltName: Full=Adrenoleukodystrophy protein {ECO:0000303|PubMed:10777694};
DE Short=ALDP {ECO:0000303|PubMed:16946495, ECO:0000303|PubMed:18757502};
GN Name=ABCD1 {ECO:0000312|HGNC:HGNC:61}; Synonyms=ALD;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=8441467; DOI=10.1038/361726a0;
RA Mosser J., Douar A.-M., Sarde C.-O., Kioschis P., Feil R., Moser H.,
RA Poustka A.-M., Mandel J.-L., Aubourg P.;
RT "Putative X-linked adrenoleukodystrophy gene shares unexpected homology
RT with ABC transporters.";
RL Nature 361:726-730(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBUNIT, AND CHARACTERIZATION OF VARIANTS ALD HIS-389; GLN-401; ARG-484 AND
RP GLN-591.
RX PubMed=10551832; DOI=10.1074/jbc.274.46.32738;
RA Liu L.X., Janvier K., Berteaux-Lecellier V., Cartier N., Benarous R.,
RA Aubourg P.;
RT "Homo- and heterodimerization of peroxisomal ATP-binding cassette half-
RT transporters.";
RL J. Biol. Chem. 274:32738-32743(1999).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND CHARACTERIZATION OF VARIANTS ALD SER-512
RP AND LEU-606.
RX PubMed=11248239; DOI=10.1016/s0014-5793(01)02235-9;
RA Roerig P., Mayerhofer P., Holzinger A., Gaertner J.;
RT "Characterization and functional analysis of the nucleotide binding fold in
RT human peroxisomal ATP binding cassette transporters.";
RL FEBS Lett. 492:66-72(2001).
RN [6]
RP INTERACTION WITH PEX19, SUBCELLULAR LOCATION, AND REGION.
RC TISSUE=Brain;
RX PubMed=10777694; DOI=10.1006/bbrc.2000.2572;
RA Gloeckner C.J., Mayerhofer P.U., Landgraf P., Muntau A.C., Holzinger A.,
RA Gerber J.-K., Kammerer S., Adamski J., Roscher A.A.;
RT "Human adrenoleukodystrophy protein and related peroxisomal ABC
RT transporters interact with the peroxisomal assembly protein PEX19p.";
RL Biochem. Biophys. Res. Commun. 271:144-150(2000).
RN [7]
RP INTERACTION WITH PEX19.
RX PubMed=10704444; DOI=10.1083/jcb.148.5.931;
RA Sacksteder K.A., Jones J.M., South S.T., Li X., Liu Y., Gould S.J.;
RT "PEX19 binds multiple peroxisomal membrane proteins, is predominantly
RT cytoplasmic, and is required for peroxisome membrane synthesis.";
RL J. Cell Biol. 148:931-944(2000).
RN [8]
RP INDUCTION.
RX PubMed=16213491; DOI=10.1016/j.febslet.2005.09.014;
RA Weinhofer I., Forss-Petter S., Kunze M., Zigman M., Berger J.;
RT "X-linked adrenoleukodystrophy mice demonstrate abnormalities in
RT cholesterol metabolism.";
RL FEBS Lett. 579:5512-5516(2005).
RN [9]
RP REGION, AND MUTAGENESIS OF MET-67; ASN-68; ARG-69; VAL-70; PHE-71; LEU-72;
RP GLN-73; ARG-74; LEU-75; LEU-76; TRP-77; LEU-78; LEU-79; ARG-80; LEU-81;
RP LEU-82 AND PHE-83.
RX PubMed=15781447; DOI=10.1074/jbc.m501750200;
RA Halbach A., Lorenzen S., Landgraf C., Volkmer-Engert R., Erdmann R.,
RA Rottensteiner H.;
RT "Function of the PEX19-binding site of human adrenoleukodystrophy protein
RT as targeting motif in man and yeast. PMP targeting is evolutionarily
RT conserved.";
RL J. Biol. Chem. 280:21176-21182(2005).
RN [10]
RP FUNCTION, AND DOMAIN.
RX PubMed=15682271; DOI=10.1007/s10038-004-0226-4;
RA Guimaraes C.P., Sa-Miranda C., Azevedo J.E.;
RT "Probing substrate-induced conformational alterations in
RT adrenoleukodystrophy protein by proteolysis.";
RL J. Hum. Genet. 50:99-105(2005).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=16946495; DOI=10.1248/bpb.29.1836;
RA Morita M., Kurisu M., Kashiwayama Y., Yokota S., Imanaka T.;
RT "ATP-binding and -hydrolysis activities of ALDP (ABCD1) and ALDRP (ABCD2),
RT human peroxisomal ABC proteins, overexpressed in Sf21 cells.";
RL Biol. Pharm. Bull. 29:1836-1842(2006).
RN [12]
RP INTERACTION WITH ABCD3, SUBUNIT, SUBCELLULAR LOCATION, AND REGION.
RX PubMed=17609205; DOI=10.1074/jbc.m702122200;
RA Hillebrand M., Verrier S.E., Ohlenbusch A., Schaefer A., Soeling H.D.,
RA Wouters F.S., Gaertner J.;
RT "Live cell FRET microscopy: homo- and heterodimerization of two human
RT peroxisomal ABC transporters, the adrenoleukodystrophy protein (ALDP,
RT ABCD1) and PMP70 (ABCD3).";
RL J. Biol. Chem. 282:26997-27005(2007).
RN [13]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=18757502; DOI=10.1096/fj.08-110866;
RA van Roermund C.W., Visser W.F., Ijlst L., van Cruchten A., Boek M.,
RA Kulik W., Waterham H.R., Wanders R.J.;
RT "The human peroxisomal ABC half transporter ALDP functions as a homodimer
RT and accepts acyl-CoA esters.";
RL FASEB J. 22:4201-4208(2008).
RN [14]
RP FUNCTION, AND SUBSTRATE SPECIFICITY.
RX PubMed=21145416; DOI=10.1016/j.bbalip.2010.11.010;
RA van Roermund C.W., Visser W.F., Ijlst L., Waterham H.R., Wanders R.J.;
RT "Differential substrate specificities of human ABCD1 and ABCD2 in
RT peroxisomal fatty acid beta-oxidation.";
RL Biochim. Biophys. Acta 1811:148-152(2011).
RN [15]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23671276; DOI=10.1074/jbc.m112.445445;
RA Wiesinger C., Kunze M., Regelsberger G., Forss-Petter S., Berger J.;
RT "Impaired very long-chain acyl-CoA beta-oxidation in human X-linked
RT adrenoleukodystrophy fibroblasts is a direct consequence of ABCD1
RT transporter dysfunction.";
RL J. Biol. Chem. 288:19269-19279(2013).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-733, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-733, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [21]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=29397936; DOI=10.1016/j.bbrc.2018.01.153;
RA Okamoto T., Kawaguchi K., Watanabe S., Agustina R., Ikejima T., Ikeda K.,
RA Nakano M., Morita M., Imanaka T.;
RT "Characterization of human ATP-binding cassette protein subfamily D
RT reconstituted into proteoliposomes.";
RL Biochem. Biophys. Res. Commun. 496:1122-1127(2018).
RN [22]
RP CATALYTIC ACTIVITY, FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP LYS-513.
RX PubMed=33500543; DOI=10.1038/s41598-021-81949-3;
RA Kawaguchi K., Mukai E., Watanabe S., Yamashita A., Morita M., So T.,
RA Imanaka T.;
RT "Acyl-CoA thioesterase activity of peroxisomal ABC protein ABCD1 is
RT required for the transport of very long-chain acyl-CoA into peroxisomes.";
RL Sci. Rep. 11:2192-2192(2021).
RN [23]
RP VARIANT ALD LYS-291.
RX PubMed=7904210; DOI=10.1093/hmg/2.11.1949;
RA Cartier N., Sarde C.-O., Douar A.-M., Mosser J., Mandel J.-L., Aubourg P.;
RT "Abnormal messenger RNA expression and a missense mutation in patients with
RT X-linked adrenoleukodystrophy.";
RL Hum. Mol. Genet. 2:1949-1951(1993).
RN [24]
RP VARIANTS ALD SER-148; ASP-174; ARG-266; GLN-401; TRP-418 AND PHE-515.
RX PubMed=7849723; DOI=10.1093/hmg/3.10.1903;
RA Fuchs S., Sarde C.-O., Wedemann H., Schwinger E., Mandel J.-L., Gal A.;
RT "Missense mutations are frequent in the gene for X-chromosomal
RT adrenoleukodystrophy (ALD).";
RL Hum. Mol. Genet. 3:1903-1905(1994).
RN [25]
RP VARIANTS ALD TRP-518; LEU-606; CYS-617 AND HIS-617.
RX PubMed=8040304; DOI=10.1172/jci117363;
RA Fanen P., Guidoux S., Sarde C.-O., Mandel J.-L., Goossens M., Aubourg P.;
RT "Identification of mutations in the putative ATP-binding domain of the
RT adrenoleukodystrophy gene.";
RL J. Clin. Invest. 94:516-520(1994).
RN [26]
RP VARIANTS ALD.
RX PubMed=7825602;
RA Ligtenberg M.J.L., Kemp S., Sarde C.-O., van Geel B.M., Kleijer W.J.,
RA Barth P.G., Mandel J.-L., van Oost B.A., Bolhuis P.A.;
RT "Spectrum of mutations in the gene encoding the adrenoleukodystrophy
RT protein.";
RL Am. J. Hum. Genet. 56:44-50(1995).
RN [27]
RP VARIANTS ALD HIS-104; GLU-178; GLY-528 DEL AND LEU-560.
RX PubMed=7717396;
RA Braun A., Ambach H., Kammerer S., Rolinski B., Stoeckler S., Rabl W.,
RA Gaertner J., Zierz S., Roscher A.A.;
RT "Mutations in the gene for X-linked adrenoleukodystrophy in patients with
RT different clinical phenotypes.";
RL Am. J. Hum. Genet. 56:854-861(1995).
RN [28]
RP VARIANTS ALD.
RX PubMed=7581394; DOI=10.1002/humu.1380060203;
RA Kok F., Neumann S., Sarde C.-O., Zheng S., Wu K.-H., Wei H.-M., Bergin J.,
RA Watkins P.A., Gould S., Sack G., Moser H., Mandel J.-L., Smith K.D.;
RT "Mutational analysis of patients with X-linked adrenoleukodystrophy.";
RL Hum. Mutat. 6:104-115(1995).
RN [29]
RP VARIANTS ALD.
RX PubMed=8651290;
RA Feigenbaum V., Lombard-Platet G., Guidoux S., Sarde C.-O., Mandel J.-L.,
RA Aubourg P.;
RT "Mutational and protein analysis of patients and heterozygous women with X-
RT linked adrenoleukodystrophy.";
RL Am. J. Hum. Genet. 58:1135-1144(1996).
RN [30]
RP VARIANTS ALD PRO-107; ASP-174; MET-254; GLY-389; GLN-401; TRP-418; LYS-609;
RP CYS-617 AND GLY-617.
RX PubMed=8566952; DOI=10.1007/bf02265264;
RA Krasemann E.W., Meier V., Korenke G.C., Hunneman D.H., Hanefeld F.;
RT "Identification of mutations in the ALD-gene of 20 families with
RT adrenoleukodystrophy/adrenomyeloneuropathy.";
RL Hum. Genet. 97:194-197(1996).
RN [31]
RP VARIANT ALD ARG-679.
RX PubMed=9452087; DOI=10.1002/humu.1380110166;
RA Korenke G.C., Krasemann E., Meier V., Beuche W., Hunneman D.H.,
RA Hanefeld F.;
RT "First missense mutation (W679R) in exon 10 of the adrenoleukodystrophy
RT gene in siblings with adrenomyeloneuropathy.";
RL Hum. Mutat. Suppl. 1:S204-S206(1998).
RN [32]
RP VARIANTS ALD PRO-105; SER-143; SER-148; PRO-190; ASP-298; SER-529 AND
RP TYR-638.
RX PubMed=10480364; DOI=10.1007/s004399900090;
RA Wichers M., Kohler W., Brennemann W., Boese V., Sokolowski P.,
RA Bidlingmaier F., Ludwig M.;
RT "X-linked adrenomyeloneuropathy associated with 14 novel ALD-gene
RT mutations: no correlation between type of mutation and age of onset.";
RL Hum. Genet. 105:116-119(1999).
RN [33]
RP VARIANTS ALD LEU-108 AND SER-143.
RX PubMed=10369742; DOI=10.1006/mcpr.1999.0232;
RA Perusi C., Gomez-Lira M., Mottes M., Pignatti P.F., Bertini E., Cappa M.,
RA Vigliani M.C., Schiffer D., Rizzuto N., Salviati A.;
RT "Two novel missense mutations causing adrenoleukodystrophy in Italian
RT patients.";
RL Mol. Cell. Probes 13:179-182(1999).
RN [34]
RP VARIANTS ALD ARG-103; ARG-116; SER-152; CYS-174; TRP-189; THR-218; PRO-229;
RP ASP-298; GLN-401; TRP-401; TRP-418; LEU-543; HIS-554; VAL-616; ARG-633 AND
RP PRO-646.
RX PubMed=10737980;
RX DOI=10.1002/(sici)1098-1004(200004)15:4<348::aid-humu7>3.0.co;2-n;
RA Lachtermacher M.B., Seuanez H.N., Moser A.B., Moser H.W., Smith K.D.;
RT "Determination of 30 X-linked adrenoleukodystrophy mutations, including 15
RT not previously described.";
RL Hum. Mutat. 15:348-353(2000).
RN [35]
RP VARIANTS ALD GLN-401; TRP-418; LEU-543 AND ARG-556.
RX PubMed=10980539;
RX DOI=10.1002/1098-1004(200009)16:3<271::aid-humu15>3.0.co;2-d;
RA Lira M.G., Mottes M., Pignatti P.F., Medica I., Uziel G., Cappa M.,
RA Bertini E., Rizzuto N., Salviati A.;
RT "Detection of mutations in the ALD gene (ABCD1) in seven Italian families:
RT description of four novel mutations.";
RL Hum. Mutat. 16:271-271(2000).
RN [36]
RP VARIANT ALD VAL-GLY-GLN-300 INS.
RX PubMed=11810273; DOI=10.1007/s00439-001-0632-z;
RA Guimaraes C.P., Lemos M., Menezes I., Coelho T., Sa-Miranda C.,
RA Azevedo J.E.;
RT "Characterisation of two mutations in the ABCD1 gene leading to low levels
RT of normal ALDP.";
RL Hum. Genet. 109:616-622(2001).
RN [37]
RP VARIANTS ALD LEU-98; ASP-99; GLU-217; GLN-518; ASP-608; ILE-633 AND
RP PRO-660, VARIANT THR-13, CHARACTERIZATION OF VARIANT ALD GLU-217, AND
RP CHARACTERIZATION OF VARIANT THR-13.
RX PubMed=11438993; DOI=10.1002/humu.1149;
RA Dvorakova L., Storkanova G., Unterrainer G., Hujova J., Kmoch S., Zeman J.,
RA Hrebicek M., Berger J.;
RT "Eight novel ABCD1 gene mutations and three polymorphisms in patients with
RT X-linked adrenoleukodystrophy: the first polymorphism causing an amino acid
RT exchange.";
RL Hum. Mutat. 18:52-60(2001).
RN [38]
RP INVOLVEMENT IN CONTIGUOUS ABCD1/DXS1375E DELETION SYNDROME.
RX PubMed=11992258; DOI=10.1086/340849;
RA Corzo D., Gibson W., Johnson K., Mitchell G., LePage G., Cox G.F.,
RA Casey R., Zeiss C., Tyson H., Cutting G.R., Raymond G.V., Smith K.D.,
RA Watkins P.A., Moser A.B., Moser H.W., Steinberg S.J.;
RT "Contiguous deletion of the X-linked adrenoleukodystrophy gene (ABCD1) and
RT DXS1357E: a novel neonatal phenotype similar to peroxisomal biogenesis
RT disorders.";
RL Am. J. Hum. Genet. 70:1520-1531(2002).
RN [39]
RP VARIANTS ALD TRP-88; CYS-152; CYS-181; SER-343; PRO-503; ARG-514 AND
RP HIS-554.
RX PubMed=15643618; DOI=10.1002/humu.9303;
RA Montagna G., Di Biase A., Cappa M., Melone M.A.B., Piantadosi C.,
RA Colabianchi D., Patrono C., Attori L., Cannelli N., Cotrufo R., Salvati S.,
RA Santorelli F.M.;
RT "Identification of seven novel mutations in ABCD1 by a DHPLC-based assay in
RT Italian patients with X-linked adrenoleukodystrophy.";
RL Hum. Mutat. 25:222-222(2005).
RN [40]
RP VARIANTS ALD GLN-401; PRO-516; LEU-560; PRO-606 AND GLN-660.
RX PubMed=21889498; DOI=10.1016/j.cca.2011.08.026;
RA Shukla P., Gupta N., Gulati S., Ghosh M., Vasisht S., Sharma R.,
RA Gupta A.K., Kalra V., Kabra M.;
RT "Molecular analysis of ABCD1 gene in Indian patients with X-linked
RT adrenoleukodystrophy.";
RL Clin. Chim. Acta 412:2289-2295(2011).
RN [41]
RP VARIANTS ALD LEU-139 DEL; ARG-198; ARG-266; GLU-266; TRP-401; GLN-518;
RP PHE-523; CYS-540; LEU-560; PRO-606; HIS-617; THR-626; PRO-632; ARG-633;
RP LYS-640 AND ASP-677.
RX PubMed=21700483; DOI=10.1016/j.ymgme.2011.05.016;
RA Wang Y., Busin R., Reeves C., Bezman L., Raymond G., Toomer C.J.,
RA Watkins P.A., Snowden A., Moser A., Naidu S., Bibat G., Hewson S., Tam K.,
RA Clarke J.T., Charnas L., Stetten G., Karczeski B., Cutting G.,
RA Steinberg S.;
RT "X-linked adrenoleukodystrophy: ABCD1 de novo mutations and mosaicism.";
RL Mol. Genet. Metab. 104:160-166(2011).
RN [42]
RP VARIANT ALD ASP-95.
RX PubMed=23651979; DOI=10.1159/000346680;
RA Kallabi F., Hadj Salem I., Ben Salah G., Ben Turkia H., Ben Chehida A.,
RA Tebib N., Fakhfakh F., Kamoun H.;
RT "Molecular characterization of X-linked adrenoleukodystrophy in a Tunisian
RT family: identification of a novel missense mutation in the ABCD1 gene.";
RL Neurodegener. Dis. 12:207-211(2013).
RN [43]
RP VARIANT ALD PRO-316.
RX PubMed=26686776; DOI=10.1016/j.cca.2015.12.014;
RA Kallabi F., Ellouz E., Tabebi M., Ben Salah G., Kaabechi N., Keskes L.,
RA Triki C., Kamoun H.;
RT "Phenotypic variability in a Tunisian family with X-linked
RT adrenoleukodystrophy caused by the p.Gln316Pro novel mutation.";
RL Clin. Chim. Acta 453:141-146(2015).
CC -!- FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC)
CC family involved in the transport of very long chain fatty acid (VLCFA)-
CC CoA from the cytosol to the peroxisome lumen (PubMed:11248239,
CC PubMed:15682271, PubMed:16946495, PubMed:18757502, PubMed:21145416,
CC PubMed:23671276, PubMed:29397936, PubMed:33500543). Coupled to the ATP-
CC dependent transporter activity has also a fatty acyl-CoA thioesterase
CC activity (ACOT) and hydrolyzes VLCFA-CoA into VLCFA prior their ATP-
CC dependent transport into peroxisomes, the ACOT activity is essential
CC during this transport process (PubMed:33500543, PubMed:29397936). Thus,
CC plays a role in regulation of VLCFAs and energy metabolism namely, in
CC the degradation and biosynthesis of fatty acids by beta-oxidation,
CC mitochondrial function and microsomal fatty acid elongation
CC (PubMed:23671276, PubMed:21145416). Involved in several processes;
CC namely, controls the active myelination phase by negatively regulating
CC the microsomal fatty acid elongation activity and may also play a role
CC in axon and myelin maintenance. Controls also the cellular response to
CC oxidative stress by regulating mitochondrial functions such as
CC mitochondrial oxidative phosphorylation and depolarization. And finally
CC controls the inflammatory response by positively regulating peroxisomal
CC beta-oxidation of VLCFAs (By similarity).
CC {ECO:0000250|UniProtKB:P48410, ECO:0000269|PubMed:11248239,
CC ECO:0000269|PubMed:15682271, ECO:0000269|PubMed:16946495,
CC ECO:0000269|PubMed:18757502, ECO:0000269|PubMed:21145416,
CC ECO:0000269|PubMed:23671276, ECO:0000269|PubMed:29397936,
CC ECO:0000269|PubMed:33500543}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very long-chain fatty acyl-CoA + H2O = a very long-chain
CC fatty acid + CoA + H(+); Xref=Rhea:RHEA:67072, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:58950,
CC ChEBI:CHEBI:138261; Evidence={ECO:0000269|PubMed:29397936,
CC ECO:0000269|PubMed:33500543};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67073;
CC Evidence={ECO:0000305|PubMed:33500543};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very long-chain fatty acid(in) + ATP + H2O = a very long-
CC chain fatty acid(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:67080,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58950, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:11248239, ECO:0000269|PubMed:29397936,
CC ECO:0000269|PubMed:33500543, ECO:0000305|PubMed:16946495,
CC ECO:0000305|PubMed:21145416, ECO:0000305|PubMed:23671276};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67081;
CC Evidence={ECO:0000305|PubMed:33500543};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + tetracosanoyl-CoA = CoA + H(+) + tetracosanoate;
CC Xref=Rhea:RHEA:40787, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:31014, ChEBI:CHEBI:57287, ChEBI:CHEBI:65052;
CC Evidence={ECO:0000269|PubMed:33500543};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40788;
CC Evidence={ECO:0000305|PubMed:33500543};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + tetracosanoate(in) = ADP + H(+) + phosphate +
CC tetracosanoate(out); Xref=Rhea:RHEA:67088, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:31014,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000305|PubMed:21145416};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67089;
CC Evidence={ECO:0000305|PubMed:33500543};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexacosanoyl-CoA = CoA + H(+) + hexacosanoate;
CC Xref=Rhea:RHEA:40791, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:31013, ChEBI:CHEBI:57287, ChEBI:CHEBI:64868;
CC Evidence={ECO:0000269|PubMed:33500543};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40792;
CC Evidence={ECO:0000305|PubMed:33500543};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + hexacosanoate(in) = ADP + H(+) +
CC hexacosanoate(out) + phosphate; Xref=Rhea:RHEA:67084,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:31013, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000305|PubMed:21145416, ECO:0000305|PubMed:23671276};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67085;
CC Evidence={ECO:0000305|PubMed:21145416};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=docosanoyl-CoA + H2O = CoA + docosanoate + H(+);
CC Xref=Rhea:RHEA:40783, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:23858, ChEBI:CHEBI:57287, ChEBI:CHEBI:65059;
CC Evidence={ECO:0000269|PubMed:33500543};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40784;
CC Evidence={ECO:0000305|PubMed:33500543};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + docosanoate(in) + H2O = ADP + docosanoate(out) + H(+) +
CC phosphate; Xref=Rhea:RHEA:67092, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:23858, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000305|PubMed:23671276};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67093;
CC Evidence={ECO:0000305|PubMed:23671276};
CC -!- ACTIVITY REGULATION: The cysteine-reactive reagent p-
CC chloromercuribenzoic acid (pCMB) strongly decreased the ACOT activity.
CC The serine esterase inhibitors phenylmethylsulfonyl fluoride (PMSF),
CC diisopropylfluorophosphate (DFP) and bis-(4-nitrophenyl)phosphate
CC (BNPP) moderately reduced the ACOT activity. The histidine-reacting
CC reagent diethyl pyrocarbonate (DEPC) has no effect on the ACOT
CC activity. {ECO:0000269|PubMed:33500543}.
CC -!- SUBUNIT: Can form homodimers and heterodimers with ABCD2 and ABCD3.
CC Dimerization is necessary to form an active transporter
CC (PubMed:17609205, PubMed:10551832) (Probable). The minimal functional
CC unit is a homodimer but the major oligomeric form in peroxisomal
CC membrane is a homotetramer (By similarity). Forms heterotramers with
CC ABCD2 (By similarity). Interacts with PEX19; facilitates ABCD1
CC insertion into the peroxisome membrane (PubMed:10777694,
CC PubMed:10704444). {ECO:0000250|UniProtKB:D3ZHR2,
CC ECO:0000269|PubMed:10551832, ECO:0000269|PubMed:10704444,
CC ECO:0000269|PubMed:10777694, ECO:0000269|PubMed:17609205,
CC ECO:0000305|PubMed:18757502}.
CC -!- INTERACTION:
CC P33897; P33897: ABCD1; NbExp=2; IntAct=EBI-81045, EBI-81045;
CC P33897; P28288: ABCD3; NbExp=2; IntAct=EBI-81045, EBI-80992;
CC P33897; P40855: PEX19; NbExp=3; IntAct=EBI-81045, EBI-594747;
CC P33897; P48410: Abcd1; Xeno; NbExp=2; IntAct=EBI-81045, EBI-81118;
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:10777694,
CC ECO:0000269|PubMed:16946495, ECO:0000269|PubMed:17609205,
CC ECO:0000269|PubMed:18757502, ECO:0000269|PubMed:29397936}; Multi-pass
CC membrane protein {ECO:0000255}. Mitochondrion membrane
CC {ECO:0000269|PubMed:16946495}; Multi-pass membrane protein. Lysosome
CC membrane {ECO:0000269|PubMed:16946495}; Multi-pass membrane protein.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:16946495}; Multi-
CC pass membrane protein.
CC -!- INDUCTION: Up-regulated by degradation or export of cholesterol.
CC {ECO:0000269|PubMed:16213491}.
CC -!- DOMAIN: The NH2-terminal transmembrane domaine (TMD) is involved in the
CC recognition of substrates, and undergoes a conformational change upon
CC ATP binding to the COOH-terminal nucleotide binding domain (NBD).
CC {ECO:0000269|PubMed:15682271}.
CC -!- PTM: Tyrosine-phosphorylated. {ECO:0000250|UniProtKB:D3ZHR2}.
CC -!- DISEASE: Adrenoleukodystrophy (ALD) [MIM:300100]: A peroxisomal
CC metabolic disorder characterized by progressive multifocal
CC demyelination of the central nervous system and by peripheral adrenal
CC insufficiency (Addison disease). It results in mental deterioration,
CC corticospinal tract dysfunction, and cortical blindness. Different
CC clinical manifestations exist like: cerebral childhood ALD (CALD),
CC adult cerebral ALD (ACALD), adrenomyeloneuropathy (AMN) and 'Addison
CC disease only' (ADO) phenotype. {ECO:0000269|PubMed:10369742,
CC ECO:0000269|PubMed:10480364, ECO:0000269|PubMed:10551832,
CC ECO:0000269|PubMed:10737980, ECO:0000269|PubMed:10980539,
CC ECO:0000269|PubMed:11248239, ECO:0000269|PubMed:11438993,
CC ECO:0000269|PubMed:11810273, ECO:0000269|PubMed:15643618,
CC ECO:0000269|PubMed:21700483, ECO:0000269|PubMed:21889498,
CC ECO:0000269|PubMed:23651979, ECO:0000269|PubMed:26686776,
CC ECO:0000269|PubMed:7581394, ECO:0000269|PubMed:7717396,
CC ECO:0000269|PubMed:7825602, ECO:0000269|PubMed:7849723,
CC ECO:0000269|PubMed:7904210, ECO:0000269|PubMed:8040304,
CC ECO:0000269|PubMed:8566952, ECO:0000269|PubMed:8651290,
CC ECO:0000269|PubMed:9452087}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Note=The promoter region of ABCD1 is deleted in the chromosome
CC Xq28 deletion syndrome which involves ABCD1 and the neighboring gene
CC BCAP31. {ECO:0000269|PubMed:11992258}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCD family.
CC Peroxisomal fatty acyl CoA transporter (TC 3.A.1.203) subfamily.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=X-ALD gene mutation database;
CC URL="https://adrenoleukodystrophy.info/";
CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC proteins;
CC URL="http://abcm2.hegelab.org/search";
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DR EMBL; Z21876; CAA79922.1; -; mRNA.
DR EMBL; Z31348; CAA83230.1; -; Genomic_DNA.
DR EMBL; Z31006; CAA83230.1; JOINED; Genomic_DNA.
DR EMBL; Z31007; CAA83230.1; JOINED; Genomic_DNA.
DR EMBL; Z31008; CAA83230.1; JOINED; Genomic_DNA.
DR EMBL; Z31009; CAA83230.1; JOINED; Genomic_DNA.
DR EMBL; Z31010; CAA83230.1; JOINED; Genomic_DNA.
DR EMBL; U52111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015541; AAH15541.1; -; mRNA.
DR EMBL; BC025358; AAH25358.1; -; mRNA.
DR CCDS; CCDS14728.1; -.
DR PIR; G02500; G02500.
DR RefSeq; NP_000024.2; NM_000033.3.
DR PDB; 7RR9; EM; 3.50 A; A/B=1-745.
DR PDB; 7RRA; EM; 4.40 A; A/B=1-745.
DR PDB; 7SHM; EM; 3.14 A; A/B=2-745.
DR PDB; 7SHN; EM; 3.10 A; A/B=2-686.
DR PDBsum; 7RR9; -.
DR PDBsum; 7RRA; -.
DR PDBsum; 7SHM; -.
DR PDBsum; 7SHN; -.
DR AlphaFoldDB; P33897; -.
DR SMR; P33897; -.
DR BioGRID; 106717; 71.
DR IntAct; P33897; 27.
DR MINT; P33897; -.
DR STRING; 9606.ENSP00000218104; -.
DR SwissLipids; SLP:000000458; -.
DR TCDB; 3.A.1.203.3; the atp-binding cassette (abc) superfamily.
DR GlyGen; P33897; 1 site.
DR iPTMnet; P33897; -.
DR PhosphoSitePlus; P33897; -.
DR BioMuta; ABCD1; -.
DR DMDM; 67476960; -.
DR EPD; P33897; -.
DR jPOST; P33897; -.
DR MassIVE; P33897; -.
DR MaxQB; P33897; -.
DR PaxDb; P33897; -.
DR PeptideAtlas; P33897; -.
DR PRIDE; P33897; -.
DR ProteomicsDB; 54928; -.
DR Antibodypedia; 30940; 439 antibodies from 35 providers.
DR DNASU; 215; -.
DR Ensembl; ENST00000218104.6; ENSP00000218104.3; ENSG00000101986.12.
DR GeneID; 215; -.
DR KEGG; hsa:215; -.
DR MANE-Select; ENST00000218104.6; ENSP00000218104.3; NM_000033.4; NP_000024.2.
DR UCSC; uc004fif.2; human.
DR CTD; 215; -.
DR DisGeNET; 215; -.
DR GeneCards; ABCD1; -.
DR GeneReviews; ABCD1; -.
DR HGNC; HGNC:61; ABCD1.
DR HPA; ENSG00000101986; Low tissue specificity.
DR MalaCards; ABCD1; -.
DR MIM; 300100; phenotype.
DR MIM; 300371; gene.
DR neXtProt; NX_P33897; -.
DR OpenTargets; ENSG00000101986; -.
DR Orphanet; 139399; Adrenomyeloneuropathy.
DR Orphanet; 369942; CADDS.
DR Orphanet; 388; Hirschsprung disease.
DR Orphanet; 139396; X-linked cerebral adrenoleukodystrophy.
DR PharmGKB; PA24396; -.
DR VEuPathDB; HostDB:ENSG00000101986; -.
DR eggNOG; KOG0064; Eukaryota.
DR GeneTree; ENSGT00950000182955; -.
DR HOGENOM; CLU_007587_1_1_1; -.
DR InParanoid; P33897; -.
DR OMA; IPRWNSK; -.
DR OrthoDB; 309052at2759; -.
DR PhylomeDB; P33897; -.
DR TreeFam; TF105205; -.
DR BRENDA; 7.6.2.4; 2681.
DR PathwayCommons; P33897; -.
DR Reactome; R-HSA-1369062; ABC transporters in lipid homeostasis.
DR Reactome; R-HSA-2046105; Linoleic acid (LA) metabolism.
DR Reactome; R-HSA-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-HSA-390247; Beta-oxidation of very long chain fatty acids.
DR Reactome; R-HSA-5684045; Defective ABCD1 causes ALD.
DR Reactome; R-HSA-9603798; Class I peroxisomal membrane protein import.
DR SignaLink; P33897; -.
DR BioGRID-ORCS; 215; 23 hits in 705 CRISPR screens.
DR ChiTaRS; ABCD1; human.
DR GeneWiki; ABCD1; -.
DR GenomeRNAi; 215; -.
DR Pharos; P33897; Tbio.
DR PRO; PR:P33897; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P33897; protein.
DR Bgee; ENSG00000101986; Expressed in ileal mucosa and 128 other tissues.
DR ExpressionAtlas; P33897; baseline and differential.
DR Genevisible; P33897; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0015607; F:ABC-type fatty-acyl-CoA transporter activity; IDA:UniProtKB.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:UniProtKB.
DR GO; GO:0043531; F:ADP binding; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; IGI:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0036109; P:alpha-linolenic acid metabolic process; TAS:Reactome.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IDA:UniProtKB.
DR GO; GO:0030497; P:fatty acid elongation; ISS:UniProtKB.
DR GO; GO:0055089; P:fatty acid homeostasis; ISS:UniProtKB.
DR GO; GO:0043651; P:linoleic acid metabolic process; TAS:Reactome.
DR GO; GO:0042758; P:long-chain fatty acid catabolic process; IMP:UniProtKB.
DR GO; GO:0015910; P:long-chain fatty acid import into peroxisome; IGI:UniProtKB.
DR GO; GO:0043217; P:myelin maintenance; ISS:UniProtKB.
DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; ISS:UniProtKB.
DR GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; ISS:UniProtKB.
DR GO; GO:1990535; P:neuron projection maintenance; ISS:UniProtKB.
DR GO; GO:0015919; P:peroxisomal membrane transport; NAS:UniProtKB.
DR GO; GO:0007031; P:peroxisome organization; IDA:UniProtKB.
DR GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; IMP:UniProtKB.
DR GO; GO:2001280; P:positive regulation of unsaturated fatty acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:1900407; P:regulation of cellular response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0031998; P:regulation of fatty acid beta-oxidation; ISS:UniProtKB.
DR GO; GO:0051900; P:regulation of mitochondrial depolarization; ISS:UniProtKB.
DR GO; GO:0002082; P:regulation of oxidative phosphorylation; ISS:UniProtKB.
DR GO; GO:0055092; P:sterol homeostasis; ISS:UniProtKB.
DR GO; GO:0042760; P:very long-chain fatty acid catabolic process; IDA:UniProtKB.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IDA:UniProtKB.
DR GO; GO:0036113; P:very long-chain fatty-acyl-CoA catabolic process; IMP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR031237; ALDP.
DR InterPro; IPR005283; FA_transporter.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11384:SF21; PTHR11384:SF21; 1.
DR Pfam; PF06472; ABC_membrane_2; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR TIGRFAMs; TIGR00954; 3a01203; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Disease variant; Endoplasmic reticulum;
KW Glycoprotein; Hydrolase; Lysosome; Membrane; Mitochondrion;
KW Nucleotide-binding; Peroxisome; Phosphoprotein; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..745
FT /note="ATP-binding cassette sub-family D member 1"
FT /id="PRO_0000093304"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 94..386
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 474..700
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 67..186
FT /note="Interaction with PEX19"
FT /evidence="ECO:0000269|PubMed:10777694"
FT REGION 67..84
FT /note="PEX19 binding site and required for peroxisomal
FT targeting"
FT /evidence="ECO:0000269|PubMed:15781447"
FT REGION 658..745
FT /note="Required for homodimerization"
FT /evidence="ECO:0000269|PubMed:17609205"
FT BINDING 507..514
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 733
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 13
FT /note="N -> T (does not affect fatty acid beta-oxidation;
FT dbSNP:rs183021839)"
FT /evidence="ECO:0000269|PubMed:11438993"
FT /id="VAR_013340"
FT VARIANT 88
FT /note="C -> W (in ALD)"
FT /evidence="ECO:0000269|PubMed:15643618"
FT /id="VAR_023004"
FT VARIANT 90
FT /note="E -> K (in ALD)"
FT /id="VAR_009349"
FT VARIANT 95
FT /note="A -> D (in ALD)"
FT /evidence="ECO:0000269|PubMed:23651979"
FT /id="VAR_075284"
FT VARIANT 98
FT /note="S -> L (in ALD; CALD type; dbSNP:rs1557052294)"
FT /evidence="ECO:0000269|PubMed:11438993"
FT /id="VAR_000024"
FT VARIANT 99
FT /note="A -> D (in ALD; AMN-type)"
FT /evidence="ECO:0000269|PubMed:11438993"
FT /id="VAR_013341"
FT VARIANT 103
FT /note="S -> R (in ALD)"
FT /evidence="ECO:0000269|PubMed:10737980"
FT /id="VAR_009350"
FT VARIANT 104
FT /note="R -> C (in ALD)"
FT /id="VAR_000025"
FT VARIANT 104
FT /note="R -> H (in ALD; ADO-type; dbSNP:rs1557052302)"
FT /evidence="ECO:0000269|PubMed:7717396"
FT /id="VAR_000026"
FT VARIANT 105
FT /note="T -> I (in ALD; ADO-type)"
FT /id="VAR_000027"
FT VARIANT 105
FT /note="T -> P (in ALD)"
FT /evidence="ECO:0000269|PubMed:10480364"
FT /id="VAR_009351"
FT VARIANT 107
FT /note="L -> P (in ALD; ALD/AMN/ADO-types and asymptomatic;
FT dbSNP:rs1569540688)"
FT /evidence="ECO:0000269|PubMed:8566952"
FT /id="VAR_000028"
FT VARIANT 108
FT /note="S -> L (in ALD)"
FT /evidence="ECO:0000269|PubMed:10369742"
FT /id="VAR_009352"
FT VARIANT 108
FT /note="S -> W (in ALD; CALD and AMN-types)"
FT /id="VAR_000029"
FT VARIANT 113
FT /note="R -> C (in ALD; dbSNP:rs1557052306)"
FT /id="VAR_009353"
FT VARIANT 113
FT /note="R -> P (in ALD)"
FT /id="VAR_013342"
FT VARIANT 116
FT /note="G -> R (in ALD; CALD-type; dbSNP:rs398123110)"
FT /evidence="ECO:0000269|PubMed:10737980"
FT /id="VAR_000030"
FT VARIANT 138..141
FT /note="Missing (in ALD; ALD-type; dbSNP:rs1557052351)"
FT /id="VAR_000032"
FT VARIANT 139
FT /note="Missing (in ALD; dbSNP:rs1557052351)"
FT /evidence="ECO:0000269|PubMed:21700483"
FT /id="VAR_067239"
FT VARIANT 141
FT /note="A -> T (in ALD; dbSNP:rs193922097)"
FT /id="VAR_000033"
FT VARIANT 143
FT /note="P -> S (in ALD)"
FT /evidence="ECO:0000269|PubMed:10369742,
FT ECO:0000269|PubMed:10480364"
FT /id="VAR_009354"
FT VARIANT 148
FT /note="N -> S (in ALD; ADO-type; dbSNP:rs128624216)"
FT /evidence="ECO:0000269|PubMed:10480364,
FT ECO:0000269|PubMed:7849723"
FT /id="VAR_000034"
FT VARIANT 149
FT /note="S -> N (in ALD)"
FT /id="VAR_000035"
FT VARIANT 152
FT /note="R -> C (in ALD; ADO-type; dbSNP:rs1569540693)"
FT /evidence="ECO:0000269|PubMed:15643618"
FT /id="VAR_000036"
FT VARIANT 152
FT /note="R -> L (in ALD)"
FT /id="VAR_009355"
FT VARIANT 152
FT /note="R -> P (in ALD)"
FT /id="VAR_000037"
FT VARIANT 152
FT /note="R -> S (in ALD)"
FT /evidence="ECO:0000269|PubMed:10737980"
FT /id="VAR_009356"
FT VARIANT 161
FT /note="S -> P (in ALD)"
FT /id="VAR_009357"
FT VARIANT 163
FT /note="R -> H (in ALD; dbSNP:rs1057517954)"
FT /id="VAR_000038"
FT VARIANT 163
FT /note="R -> P (in ALD)"
FT /id="VAR_009358"
FT VARIANT 174
FT /note="Y -> C (in ALD; dbSNP:rs1557052390)"
FT /evidence="ECO:0000269|PubMed:10737980"
FT /id="VAR_009359"
FT VARIANT 174
FT /note="Y -> D (in ALD; ALD-type; dbSNP:rs128624217)"
FT /evidence="ECO:0000269|PubMed:7849723,
FT ECO:0000269|PubMed:8566952"
FT /id="VAR_000039"
FT VARIANT 174
FT /note="Y -> S (in ALD; CALD-type; dbSNP:rs1557052390)"
FT /id="VAR_000040"
FT VARIANT 178
FT /note="Q -> E (in ALD; AMN-type)"
FT /evidence="ECO:0000269|PubMed:7717396"
FT /id="VAR_000041"
FT VARIANT 181
FT /note="Y -> C (in ALD; ALMD-type)"
FT /evidence="ECO:0000269|PubMed:15643618"
FT /id="VAR_000042"
FT VARIANT 182
FT /note="R -> P (in ALD)"
FT /id="VAR_000043"
FT VARIANT 189
FT /note="R -> W (in ALD; dbSNP:rs1131691916)"
FT /evidence="ECO:0000269|PubMed:10737980"
FT /id="VAR_009360"
FT VARIANT 190
FT /note="L -> P (in ALD)"
FT /evidence="ECO:0000269|PubMed:10480364"
FT /id="VAR_009361"
FT VARIANT 194
FT /note="D -> H (in ALD)"
FT /id="VAR_000044"
FT VARIANT 198
FT /note="T -> K (in ALD)"
FT /id="VAR_009362"
FT VARIANT 198
FT /note="T -> R (in ALD)"
FT /evidence="ECO:0000269|PubMed:21700483"
FT /id="VAR_067240"
FT VARIANT 200
FT /note="D -> N (in ALD)"
FT /id="VAR_009363"
FT VARIANT 200
FT /note="D -> V (in ALD; CALD-type)"
FT /id="VAR_000045"
FT VARIANT 207
FT /note="S -> SAAS (in ALD)"
FT /id="VAR_013343"
FT VARIANT 211
FT /note="L -> P (in ALD)"
FT /id="VAR_000046"
FT VARIANT 213
FT /note="S -> C (in ALD)"
FT /id="VAR_009364"
FT VARIANT 214
FT /note="N -> D (in ALD)"
FT /id="VAR_009365"
FT VARIANT 217
FT /note="K -> E (in ALD; not able to restore defective beta-
FT oxidation in fibroblast from patients with ALD)"
FT /evidence="ECO:0000269|PubMed:11438993"
FT /id="VAR_013344"
FT VARIANT 218
FT /note="P -> T (in ALD)"
FT /evidence="ECO:0000269|PubMed:10737980"
FT /id="VAR_009366"
FT VARIANT 220
FT /note="L -> P (in ALD)"
FT /id="VAR_000047"
FT VARIANT 221
FT /note="D -> G (in ALD; CALD and AMN-types)"
FT /id="VAR_000048"
FT VARIANT 224
FT /note="V -> E (in ALD)"
FT /id="VAR_013345"
FT VARIANT 229
FT /note="L -> P (in ALD)"
FT /evidence="ECO:0000269|PubMed:10737980"
FT /id="VAR_009367"
FT VARIANT 254
FT /note="T -> M (in ALD; AMN-type; dbSNP:rs1131691743)"
FT /evidence="ECO:0000269|PubMed:8566952"
FT /id="VAR_000049"
FT VARIANT 254
FT /note="T -> P (in ALD; AMN-type)"
FT /id="VAR_000050"
FT VARIANT 263
FT /note="P -> L (in ALD; CALD, AMN and AD-types)"
FT /id="VAR_000051"
FT VARIANT 266
FT /note="G -> E (in ALD)"
FT /evidence="ECO:0000269|PubMed:21700483"
FT /id="VAR_067241"
FT VARIANT 266
FT /note="G -> R (in ALD; dbSNP:rs128624218)"
FT /evidence="ECO:0000269|PubMed:21700483,
FT ECO:0000269|PubMed:7849723"
FT /id="VAR_000052"
FT VARIANT 271
FT /note="E -> K (in ALD)"
FT /id="VAR_009368"
FT VARIANT 274
FT /note="R -> W (in ALD; dbSNP:rs782760033)"
FT /id="VAR_013346"
FT VARIANT 276
FT /note="K -> E (in ALD; CALD-type)"
FT /id="VAR_000053"
FT VARIANT 277
FT /note="G -> GN (in ALD; ADO-type)"
FT /id="VAR_000055"
FT VARIANT 277
FT /note="G -> R (in ALD; AMN-type; dbSNP:rs1603232195)"
FT /id="VAR_000054"
FT VARIANT 277
FT /note="G -> W (in ALD)"
FT /id="VAR_000056"
FT VARIANT 280
FT /note="R -> C (in ALD; dbSNP:rs193922098)"
FT /id="VAR_013347"
FT VARIANT 285
FT /note="R -> P (in ALD)"
FT /id="VAR_009369"
FT VARIANT 291
FT /note="E -> D (in ALD; ACALD and CALD-types)"
FT /id="VAR_000057"
FT VARIANT 291
FT /note="E -> K (in ALD; dbSNP:rs128624213)"
FT /evidence="ECO:0000269|PubMed:7904210"
FT /id="VAR_000058"
FT VARIANT 291
FT /note="Missing (in ALD; ALD-type)"
FT /id="VAR_000059"
FT VARIANT 294
FT /note="A -> T (in ALD; AMN-type; dbSNP:rs1131691954)"
FT /id="VAR_000060"
FT VARIANT 296
FT /note="Y -> C (in ALD; dbSNP:rs797044610)"
FT /id="VAR_009370"
FT VARIANT 298
FT /note="G -> D (in ALD)"
FT /evidence="ECO:0000269|PubMed:10480364,
FT ECO:0000269|PubMed:10737980"
FT /id="VAR_009371"
FT VARIANT 300
FT /note="E -> EVGQ (in ALD)"
FT /evidence="ECO:0000269|PubMed:11810273"
FT /id="VAR_013348"
FT VARIANT 302
FT /note="E -> K (in ALD)"
FT /id="VAR_009372"
FT VARIANT 316
FT /note="Q -> P (in ALD)"
FT /evidence="ECO:0000269|PubMed:26686776"
FT /id="VAR_075285"
FT VARIANT 322
FT /note="L -> P (in ALD)"
FT /id="VAR_009373"
FT VARIANT 336
FT /note="K -> M (in ALD)"
FT /id="VAR_009374"
FT VARIANT 339
FT /note="W -> R (in ALD; dbSNP:rs1603233120)"
FT /id="VAR_013349"
FT VARIANT 342
FT /note="S -> P (in ALD; AMN-type)"
FT /id="VAR_000061"
FT VARIANT 343
FT /note="G -> D (in ALD)"
FT /id="VAR_013350"
FT VARIANT 343
FT /note="G -> S (in ALD)"
FT /evidence="ECO:0000269|PubMed:15643618"
FT /id="VAR_023005"
FT VARIANT 389
FT /note="R -> G (in ALD; AMN-type; dbSNP:rs128624215)"
FT /evidence="ECO:0000269|PubMed:8566952"
FT /id="VAR_000062"
FT VARIANT 389
FT /note="R -> H (in ALD; does not affect protein stability,
FT homo- and heterodimerization with ABCD2 and ABCD3;
FT dbSNP:rs886044777)"
FT /evidence="ECO:0000269|PubMed:10551832"
FT /id="VAR_000063"
FT VARIANT 401
FT /note="R -> Q (in ALD; ALD and AMN-types; does not affect
FT protein stability, homo- and heterodimerization with ABCD2
FT and ABCD3; dbSNP:rs128624219)"
FT /evidence="ECO:0000269|PubMed:10551832,
FT ECO:0000269|PubMed:10737980, ECO:0000269|PubMed:10980539,
FT ECO:0000269|PubMed:21889498, ECO:0000269|PubMed:7849723,
FT ECO:0000269|PubMed:8566952"
FT /id="VAR_000064"
FT VARIANT 401
FT /note="R -> W (in ALD; dbSNP:rs727503786)"
FT /evidence="ECO:0000269|PubMed:10737980,
FT ECO:0000269|PubMed:21700483"
FT /id="VAR_009375"
FT VARIANT 418
FT /note="R -> W (in ALD; AMN-type; dbSNP:rs128624220)"
FT /evidence="ECO:0000269|PubMed:10737980,
FT ECO:0000269|PubMed:10980539, ECO:0000269|PubMed:7849723,
FT ECO:0000269|PubMed:8566952"
FT /id="VAR_000065"
FT VARIANT 427
FT /note="Missing (in ALD)"
FT /id="VAR_013351"
FT VARIANT 484
FT /note="P -> R (in ALD; CALD, AMN and ADO-types;
FT significantly decreases homodimerization and abolishes
FT heterodimerization with ABCD2 and ABCD3;
FT dbSNP:rs128624214)"
FT /evidence="ECO:0000269|PubMed:10551832"
FT /id="VAR_000066"
FT VARIANT 503
FT /note="L -> P (in ALD)"
FT /evidence="ECO:0000269|PubMed:15643618"
FT /id="VAR_023006"
FT VARIANT 507
FT /note="G -> V (in ALD; CALD-types)"
FT /id="VAR_000067"
FT VARIANT 512
FT /note="G -> S (in ALD; CALD and AS-types; reduced ATPase
FT activity; dbSNP:rs1569541088)"
FT /evidence="ECO:0000269|PubMed:11248239"
FT /id="VAR_000068"
FT VARIANT 514
FT /note="S -> R (in ALD)"
FT /evidence="ECO:0000269|PubMed:15643618"
FT /id="VAR_023007"
FT VARIANT 515
FT /note="S -> F (in ALD; dbSNP:rs128624223)"
FT /evidence="ECO:0000269|PubMed:7849723"
FT /id="VAR_000069"
FT VARIANT 516
FT /note="L -> P (in ALD)"
FT /evidence="ECO:0000269|PubMed:21889498"
FT /id="VAR_067328"
FT VARIANT 518
FT /note="R -> Q (in ALD; CALD-type; dbSNP:rs398123102)"
FT /evidence="ECO:0000269|PubMed:11438993,
FT ECO:0000269|PubMed:21700483"
FT /id="VAR_000070"
FT VARIANT 518
FT /note="R -> W (in ALD; CALD-type; dbSNP:rs128624224)"
FT /evidence="ECO:0000269|PubMed:8040304"
FT /id="VAR_000071"
FT VARIANT 522
FT /note="G -> W (in ALD; AD-type)"
FT /id="VAR_000072"
FT VARIANT 523
FT /note="L -> F (in ALD; dbSNP:rs1159943880)"
FT /evidence="ECO:0000269|PubMed:21700483"
FT /id="VAR_067242"
FT VARIANT 528
FT /note="Missing (in ALD; CALD-type)"
FT /evidence="ECO:0000269|PubMed:7717396"
FT /id="VAR_000073"
FT VARIANT 529
FT /note="G -> S (in ALD)"
FT /evidence="ECO:0000269|PubMed:10480364"
FT /id="VAR_009376"
FT VARIANT 534
FT /note="P -> L (in ALD; CALD-type)"
FT /id="VAR_000074"
FT VARIANT 540
FT /note="F -> C (in ALD)"
FT /evidence="ECO:0000269|PubMed:21700483"
FT /id="VAR_067243"
FT VARIANT 540
FT /note="F -> S (in ALD)"
FT /id="VAR_009377"
FT VARIANT 543
FT /note="P -> L (in ALD; dbSNP:rs1557054776)"
FT /evidence="ECO:0000269|PubMed:10737980,
FT ECO:0000269|PubMed:10980539"
FT /id="VAR_009378"
FT VARIANT 544
FT /note="Q -> R (in ALD)"
FT /id="VAR_009379"
FT VARIANT 552
FT /note="S -> P (in ALD)"
FT /id="VAR_009380"
FT VARIANT 554
FT /note="R -> H (in ALD; dbSNP:rs201568579)"
FT /evidence="ECO:0000269|PubMed:10737980,
FT ECO:0000269|PubMed:15643618"
FT /id="VAR_009381"
FT VARIANT 556
FT /note="Q -> R (in ALD; ACALD type)"
FT /evidence="ECO:0000269|PubMed:10980539"
FT /id="VAR_013352"
FT VARIANT 560
FT /note="P -> L (in ALD; CALD-type; dbSNP:rs398123105)"
FT /evidence="ECO:0000269|PubMed:21700483,
FT ECO:0000269|PubMed:21889498, ECO:0000269|PubMed:7717396"
FT /id="VAR_000075"
FT VARIANT 560
FT /note="P -> R (in ALD; AMN and ALMD-types)"
FT /id="VAR_000076"
FT VARIANT 560
FT /note="P -> S (in ALD)"
FT /id="VAR_013353"
FT VARIANT 566
FT /note="M -> K (in ALD)"
FT /id="VAR_000077"
FT VARIANT 591
FT /note="R -> P (in ALD)"
FT /id="VAR_013354"
FT VARIANT 591
FT /note="R -> Q (in ALD; AMN-type; significantly decreases
FT homodimerization and abolishes heterodimerization with
FT ABCD2 and ABCD3; dbSNP:rs1557054873)"
FT /evidence="ECO:0000269|PubMed:10551832"
FT /id="VAR_000078"
FT VARIANT 591
FT /note="R -> W (in ALD; dbSNP:rs398123106)"
FT /id="VAR_009382"
FT VARIANT 606
FT /note="S -> L (in ALD; decreased ATP-binding affinity;
FT dbSNP:rs128624225)"
FT /evidence="ECO:0000269|PubMed:11248239,
FT ECO:0000269|PubMed:8040304"
FT /id="VAR_000079"
FT VARIANT 606
FT /note="S -> P (in ALD; CALD, AMN and ALMD-types;
FT dbSNP:rs201774661)"
FT /evidence="ECO:0000269|PubMed:21700483,
FT ECO:0000269|PubMed:21889498"
FT /id="VAR_000080"
FT VARIANT 608
FT /note="G -> D (in ALD; CALD-type; dbSNP:rs78993751)"
FT /evidence="ECO:0000269|PubMed:11438993"
FT /id="VAR_013355"
FT VARIANT 609
FT /note="E -> G (in ALD; dbSNP:rs1557055260)"
FT /id="VAR_000081"
FT VARIANT 609
FT /note="E -> K (in ALD; AMN-type; dbSNP:rs150346282)"
FT /evidence="ECO:0000269|PubMed:8566952"
FT /id="VAR_000082"
FT VARIANT 616
FT /note="A -> V (in ALD)"
FT /evidence="ECO:0000269|PubMed:10737980"
FT /id="VAR_009383"
FT VARIANT 617
FT /note="R -> C (in ALD; ALD-type and asymptomatic;
FT dbSNP:rs4010613)"
FT /evidence="ECO:0000269|PubMed:8040304,
FT ECO:0000269|PubMed:8566952"
FT /id="VAR_000083"
FT VARIANT 617
FT /note="R -> G (in ALD; ADO and AMN-types with cerebral
FT involvement)"
FT /evidence="ECO:0000269|PubMed:8566952"
FT /id="VAR_000084"
FT VARIANT 617
FT /note="R -> H (in ALD; dbSNP:rs11146842)"
FT /evidence="ECO:0000269|PubMed:21700483,
FT ECO:0000269|PubMed:8040304"
FT /id="VAR_000085"
FT VARIANT 626
FT /note="A -> D (in ALD)"
FT /id="VAR_013356"
FT VARIANT 626
FT /note="A -> T (in ALD; CALD and AMN-types;
FT dbSNP:rs1557055316)"
FT /evidence="ECO:0000269|PubMed:21700483"
FT /id="VAR_000086"
FT VARIANT 629
FT /note="D -> H (in ALD)"
FT /id="VAR_000087"
FT VARIANT 630
FT /note="E -> G (in ALD)"
FT /id="VAR_009384"
FT VARIANT 631
FT /note="C -> Y (in ALD)"
FT /id="VAR_009385"
FT VARIANT 632
FT /note="T -> I (in ALD; dbSNP:rs1064793877)"
FT /id="VAR_013357"
FT VARIANT 632
FT /note="T -> P (in ALD)"
FT /evidence="ECO:0000269|PubMed:21700483"
FT /id="VAR_067244"
FT VARIANT 633
FT /note="S -> I (in ALD; asymptomatic)"
FT /evidence="ECO:0000269|PubMed:11438993"
FT /id="VAR_013358"
FT VARIANT 633
FT /note="S -> R (in ALD)"
FT /evidence="ECO:0000269|PubMed:10737980,
FT ECO:0000269|PubMed:21700483"
FT /id="VAR_009386"
FT VARIANT 635
FT /note="V -> M (in ALD; dbSNP:rs201427153)"
FT /id="VAR_013359"
FT VARIANT 636
FT /note="S -> I (in ALD)"
FT /id="VAR_009387"
FT VARIANT 638
FT /note="D -> Y (in ALD)"
FT /evidence="ECO:0000269|PubMed:10480364"
FT /id="VAR_009388"
FT VARIANT 640
FT /note="E -> K (in ALD)"
FT /evidence="ECO:0000269|PubMed:21700483"
FT /id="VAR_067245"
FT VARIANT 646
FT /note="A -> P (in ALD)"
FT /evidence="ECO:0000269|PubMed:10737980"
FT /id="VAR_009389"
FT VARIANT 654
FT /note="L -> P (in ALD)"
FT /id="VAR_009390"
FT VARIANT 657
FT /note="Missing (in ALD; CALD-type)"
FT /id="VAR_000088"
FT VARIANT 660
FT /note="R -> P (in ALD; CALD-type)"
FT /evidence="ECO:0000269|PubMed:11438993"
FT /id="VAR_013360"
FT VARIANT 660
FT /note="R -> Q (in ALD; dbSNP:rs1557055340)"
FT /evidence="ECO:0000269|PubMed:21889498"
FT /id="VAR_067329"
FT VARIANT 660
FT /note="R -> W (in ALD; CALD, ALMD and AS-types;
FT dbSNP:rs1569541203)"
FT /id="VAR_000089"
FT VARIANT 667
FT /note="H -> D (in ALD)"
FT /id="VAR_009391"
FT VARIANT 668
FT /note="T -> I (in ALD; dbSNP:rs1557055398)"
FT /id="VAR_009392"
FT VARIANT 677
FT /note="G -> D (in ALD)"
FT /evidence="ECO:0000269|PubMed:21700483"
FT /id="VAR_067246"
FT VARIANT 679
FT /note="W -> R (in ALD; AMN-type; dbSNP:rs1557055405)"
FT /evidence="ECO:0000269|PubMed:9452087"
FT /id="VAR_000090"
FT VARIANT 693
FT /note="T -> M (in ALD; dbSNP:rs782311214)"
FT /id="VAR_009393"
FT MUTAGEN 67
FT /note="M->P: Does not affect PEX19 interaction."
FT /evidence="ECO:0000269|PubMed:15781447"
FT MUTAGEN 68
FT /note="N->P: Does not affect PEX19 interaction."
FT /evidence="ECO:0000269|PubMed:15781447"
FT MUTAGEN 69
FT /note="R->P: Does not affect PEX19 interaction."
FT /evidence="ECO:0000269|PubMed:15781447"
FT MUTAGEN 70
FT /note="V->P: Does not affect PEX19 interaction."
FT /evidence="ECO:0000269|PubMed:15781447"
FT MUTAGEN 71
FT /note="F->P: Does not affect PEX19 interaction."
FT /evidence="ECO:0000269|PubMed:15781447"
FT MUTAGEN 72
FT /note="L->P: Does not affect PEX19 interaction."
FT /evidence="ECO:0000269|PubMed:15781447"
FT MUTAGEN 73
FT /note="Q->P: Does not affect PEX19 interaction."
FT /evidence="ECO:0000269|PubMed:15781447"
FT MUTAGEN 74
FT /note="R->P: Does not affect PEX19 interaction."
FT /evidence="ECO:0000269|PubMed:15781447"
FT MUTAGEN 75
FT /note="L->P: Impairs PEX19 interaction."
FT /evidence="ECO:0000269|PubMed:15781447"
FT MUTAGEN 76
FT /note="L->P: Impairs PEX19 interaction."
FT /evidence="ECO:0000269|PubMed:15781447"
FT MUTAGEN 77
FT /note="W->P: Does not affect PEX19 interaction."
FT /evidence="ECO:0000269|PubMed:15781447"
FT MUTAGEN 78
FT /note="L->P: Impairs PEX19 interaction."
FT /evidence="ECO:0000269|PubMed:15781447"
FT MUTAGEN 79
FT /note="L->P: Impairs PEX19 interaction."
FT /evidence="ECO:0000269|PubMed:15781447"
FT MUTAGEN 80
FT /note="R->P: Does not affect PEX19 interaction."
FT /evidence="ECO:0000269|PubMed:15781447"
FT MUTAGEN 81
FT /note="L->P: Does not affect PEX19 interaction."
FT /evidence="ECO:0000269|PubMed:15781447"
FT MUTAGEN 82
FT /note="L->P: Does not affect PEX19 interaction."
FT /evidence="ECO:0000269|PubMed:15781447"
FT MUTAGEN 83
FT /note="F->P: Does not affect PEX19 interaction."
FT /evidence="ECO:0000269|PubMed:15781447"
FT MUTAGEN 513
FT /note="K->A: Does not affect ACOT activity. Transport
FT activity of VLCFA is strongly reduced."
FT /evidence="ECO:0000269|PubMed:33500543"
FT CONFLICT 123
FT /note="V -> A (in Ref. 1; CAA79922/CAA83230)"
FT /evidence="ECO:0000305"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:7SHM"
FT HELIX 69..82
FT /evidence="ECO:0007829|PDB:7SHN"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:7SHN"
FT TURN 89..93
FT /evidence="ECO:0007829|PDB:7SHN"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:7SHN"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:7SHN"
FT HELIX 102..106
FT /evidence="ECO:0007829|PDB:7SHN"
FT HELIX 108..123
FT /evidence="ECO:0007829|PDB:7SHN"
FT HELIX 127..156
FT /evidence="ECO:0007829|PDB:7SHN"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:7SHN"
FT HELIX 163..174
FT /evidence="ECO:0007829|PDB:7SHN"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:7SHM"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:7SHN"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:7SHN"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:7SHN"
FT HELIX 193..196
FT /evidence="ECO:0007829|PDB:7SHN"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:7SHN"
FT HELIX 201..233
FT /evidence="ECO:0007829|PDB:7SHN"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:7SHN"
FT HELIX 242..252
FT /evidence="ECO:0007829|PDB:7SHN"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:7SHN"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:7SHN"
FT TURN 262..264
FT /evidence="ECO:0007829|PDB:7SHN"
FT HELIX 269..288
FT /evidence="ECO:0007829|PDB:7SHN"
FT HELIX 290..295
FT /evidence="ECO:0007829|PDB:7SHN"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:7SHN"
FT HELIX 299..335
FT /evidence="ECO:0007829|PDB:7SHN"
FT HELIX 338..352
FT /evidence="ECO:0007829|PDB:7SHN"
FT HELIX 374..378
FT /evidence="ECO:0007829|PDB:7SHN"
FT HELIX 380..394
FT /evidence="ECO:0007829|PDB:7SHN"
FT TURN 395..398
FT /evidence="ECO:0007829|PDB:7SHN"
FT HELIX 399..403
FT /evidence="ECO:0007829|PDB:7SHN"
FT HELIX 409..428
FT /evidence="ECO:0007829|PDB:7SHN"
FT HELIX 429..431
FT /evidence="ECO:0007829|PDB:7SHN"
FT STRAND 467..469
FT /evidence="ECO:0007829|PDB:7SHN"
FT STRAND 475..483
FT /evidence="ECO:0007829|PDB:7SHN"
FT TURN 484..486
FT /evidence="ECO:0007829|PDB:7SHN"
FT STRAND 487..493
FT /evidence="ECO:0007829|PDB:7SHN"
FT STRAND 494..496
FT /evidence="ECO:0007829|PDB:7RR9"
FT STRAND 503..506
FT /evidence="ECO:0007829|PDB:7SHN"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:7SHM"
FT HELIX 515..520
FT /evidence="ECO:0007829|PDB:7SHN"
FT STRAND 522..524
FT /evidence="ECO:0007829|PDB:7SHM"
FT STRAND 528..533
FT /evidence="ECO:0007829|PDB:7SHN"
FT HELIX 536..538
FT /evidence="ECO:0007829|PDB:7SHN"
FT STRAND 539..542
FT /evidence="ECO:0007829|PDB:7SHN"
FT STRAND 550..552
FT /evidence="ECO:0007829|PDB:7RR9"
FT HELIX 554..556
FT /evidence="ECO:0007829|PDB:7SHN"
FT HELIX 563..569
FT /evidence="ECO:0007829|PDB:7SHN"
FT HELIX 573..582
FT /evidence="ECO:0007829|PDB:7SHN"
FT HELIX 588..590
FT /evidence="ECO:0007829|PDB:7SHN"
FT TURN 591..593
FT /evidence="ECO:0007829|PDB:7SHN"
FT STRAND 595..597
FT /evidence="ECO:0007829|PDB:7RR9"
FT HELIX 601..604
FT /evidence="ECO:0007829|PDB:7SHN"
FT HELIX 607..620
FT /evidence="ECO:0007829|PDB:7SHN"
FT STRAND 624..630
FT /evidence="ECO:0007829|PDB:7SHN"
FT STRAND 633..635
FT /evidence="ECO:0007829|PDB:7SHN"
FT HELIX 637..650
FT /evidence="ECO:0007829|PDB:7SHN"
FT STRAND 654..657
FT /evidence="ECO:0007829|PDB:7SHN"
FT HELIX 664..666
FT /evidence="ECO:0007829|PDB:7SHN"
FT STRAND 671..673
FT /evidence="ECO:0007829|PDB:7SHN"
FT STRAND 675..677
FT /evidence="ECO:0007829|PDB:7SHN"
FT STRAND 679..681
FT /evidence="ECO:0007829|PDB:7SHN"
SQ SEQUENCE 745 AA; 82937 MW; 82F90905F71FFDC8 CRC64;
MPVLSRPRPW RGNTLKRTAV LLALAAYGAH KVYPLVRQCL APARGLQAPA GEPTQEASGV
AAAKAGMNRV FLQRLLWLLR LLFPRVLCRE TGLLALHSAA LVSRTFLSVY VARLDGRLAR
CIVRKDPRAF GWQLLQWLLI ALPATFVNSA IRYLEGQLAL SFRSRLVAHA YRLYFSQQTY
YRVSNMDGRL RNPDQSLTED VVAFAASVAH LYSNLTKPLL DVAVTSYTLL RAARSRGAGT
AWPSAIAGLV VFLTANVLRA FSPKFGELVA EEARRKGELR YMHSRVVANS EEIAFYGGHE
VELALLQRSY QDLASQINLI LLERLWYVML EQFLMKYVWS ASGLLMVAVP IITATGYSES
DAEAVKKAAL EKKEEELVSE RTEAFTIARN LLTAAADAIE RIMSSYKEVT ELAGYTARVH
EMFQVFEDVQ RCHFKRPREL EDAQAGSGTI GRSGVRVEGP LKIRGQVVDV EQGIICENIP
IVTPSGEVVV ASLNIRVEEG MHLLITGPNG CGKSSLFRIL GGLWPTYGGV LYKPPPQRMF
YIPQRPYMSV GSLRDQVIYP DSVEDMQRKG YSEQDLEAIL DVVHLHHILQ REGGWEAMCD
WKDVLSGGEK QRIGMARMFY HRPKYALLDE CTSAVSIDVE GKIFQAAKDA GIALLSITHR
PSLWKYHTHL LQFDGEGGWK FEKLDSAARL SLTEEKQRLE QQLAGIPKMQ RRLQELCQIL
GEAVAPAHVP APSPQGPGGL QGAST
