ABCD1_MOUSE
ID ABCD1_MOUSE Reviewed; 736 AA.
AC P48410; Q9QY41; Q9QZ32;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=ATP-binding cassette sub-family D member 1 {ECO:0000305};
DE EC=3.1.2.- {ECO:0000250|UniProtKB:P33897};
DE EC=7.6.2.- {ECO:0000250|UniProtKB:P33897};
DE AltName: Full=Adrenoleukodystrophy protein {ECO:0000250|UniProtKB:P33897};
DE Short=ALDP {ECO:0000250|UniProtKB:P33897};
GN Name=Abcd1 {ECO:0000312|MGI:MGI:1349215};
GN Synonyms=Ald {ECO:0000303|PubMed:10504404},
GN Aldgh {ECO:0000303|PubMed:7894167};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fibrotic liver;
RX PubMed=7894167; DOI=10.1007/bf00292021;
RA Sarde C.-O., Thomas J., Sadoulet H., Garnier J.-M., Mandel J.-L.;
RT "cDNA sequence of Aldgh, the mouse homolog of the X-linked
RT adrenoleukodystrophy gene.";
RL Mamm. Genome 5:810-813(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary gland;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RC STRAIN=129/SvJ;
RX PubMed=10504404; DOI=10.1046/j.1432-1327.1999.00772.x;
RA Berger J., Albet S., Bentejac M., Netik A., Holzinger A., Roscher A.,
RA Bugaut M., Forss-Petter S.;
RT "The four murine peroxisomal ABC-transporter genes differ in constitutive,
RT inducible and developmental expression.";
RL Eur. J. Biochem. 265:719-727(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 362-736.
RA Platzer M., Brenner V., Reichwald K., Wiehe T., Oksche A., Rosenthal A.;
RT "Comparative sequence analysis of the mouse L1cam locus and the
RT corresponding region of human Xq28.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=9126326; DOI=10.1006/bbrc.1997.6340;
RA Kobayashi T., Shinnoh N., Kondo A., Yamada T.;
RT "Adrenoleukodystrophy protein-deficient mice represent abnormality of very
RT long chain fatty acid metabolism.";
RL Biochem. Biophys. Res. Commun. 232:631-636(1997).
RN [8]
RP DISRUPTION PHENOTYPE, FUNCTION, AND MISCELLANEOUS.
RX PubMed=9418970;
RX DOI=10.1002/(sici)1097-4547(19971201)50:5<829::aid-jnr19>3.0.co;2-w;
RA Forss-Petter S., Werner H., Berger J., Lassmann H., Molzer B., Schwab M.H.,
RA Bernheimer H., Zimmermann F., Nave K.A.;
RT "Targeted inactivation of the X-linked adrenoleukodystrophy gene in mice.";
RL J. Neurosci. Res. 50:829-843(1997).
RN [9]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=9256488; DOI=10.1073/pnas.94.17.9366;
RA Lu J.F., Lawler A.M., Watkins P.A., Powers J.M., Moser A.B., Moser H.W.,
RA Smith K.D.;
RT "A mouse model for X-linked adrenoleukodystrophy.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:9366-9371(1997).
RN [10]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=11875044; DOI=10.1093/hmg/11.5.499;
RA Pujol A., Hindelang C., Callizot N., Bartsch U., Schachner M., Mandel J.L.;
RT "Late onset neurological phenotype of the X-ALD gene inactivation in mice:
RT a mouse model for adrenomyeloneuropathy.";
RL Hum. Mol. Genet. 11:499-505(2002).
RN [11]
RP SUBUNIT.
RX PubMed=15276650; DOI=10.1016/j.bbadis.2004.04.001;
RA Guimaraes C.P., Domingues P., Aubourg P., Fouquet F., Pujol A.,
RA Jimenez-Sanchez G., Sa-Miranda C., Azevedo J.E.;
RT "Mouse liver PMP70 and ALDP: homomeric interactions prevail in vivo.";
RL Biochim. Biophys. Acta 1689:235-243(2004).
RN [12]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=15489218; DOI=10.1093/hmg/ddh323;
RA Pujol A., Ferrer I., Camps C., Metzger E., Hindelang C., Callizot N.,
RA Ruiz M., Pampols T., Giros M., Mandel J.L.;
RT "Functional overlap between ABCD1 (ALD) and ABCD2 (ALDR) transporters: a
RT therapeutic target for X-adrenoleukodystrophy.";
RL Hum. Mol. Genet. 13:2997-3006(2004).
RN [13]
RP FUNCTION.
RX PubMed=18344354; DOI=10.1093/hmg/ddn085;
RA Fourcade S., Lopez-Erauskin J., Galino J., Duval C., Naudi A., Jove M.,
RA Kemp S., Villarroya F., Ferrer I., Pamplona R., Portero-Otin M., Pujol A.;
RT "Early oxidative damage underlying neurodegeneration in X-
RT adrenoleukodystrophy.";
RL Hum. Mol. Genet. 17:1762-1773(2008).
RN [14]
RP FUNCTION.
RX PubMed=18723473; DOI=10.1194/jlr.m800321-jlr200;
RA Singh J., Khan M., Singh I.;
RT "Silencing of Abcd1 and Abcd2 genes sensitizes astrocytes for inflammation:
RT implication for X-adrenoleukodystrophy.";
RL J. Lipid Res. 50:135-147(2009).
RN [15]
RP FUNCTION.
RX PubMed=18854420; DOI=10.1152/ajpendo.90736.2008;
RA Fourcade S., Ruiz M., Camps C., Schlueter A., Houten S.M., Mooyer P.A.,
RA Pampols T., Dacremont G., Wanders R.J., Giros M., Pujol A.;
RT "A key role for the peroxisomal ABCD2 transporter in fatty acid
RT homeostasis.";
RL Am. J. Physiol. 296:E211-E221(2009).
RN [16]
RP FUNCTION.
RX PubMed=23123468; DOI=10.1248/bpb.b12-00411;
RA Morita M., Shinbo S., Asahi A., Imanaka T.;
RT "Very long chain fatty acid beta-oxidation in astrocytes: contribution of
RT the ABCD1-dependent and -independent pathways.";
RL Biol. Pharm. Bull. 35:1972-1979(2012).
RN [17]
RP FUNCTION.
RX PubMed=22521832; DOI=10.1016/j.neuroscience.2012.03.058;
RA Baarine M., Andreoletti P., Athias A., Nury T., Zarrouk A., Ragot K.,
RA Vejux A., Riedinger J.M., Kattan Z., Bessede G., Trompier D., Savary S.,
RA Cherkaoui-Malki M., Lizard G.;
RT "Evidence of oxidative stress in very long chain fatty acid--treated
RT oligodendrocytes and potentialization of ROS production using RNA
RT interference-directed knockdown of ABCD1 and ACOX1 peroxisomal proteins.";
RL Neuroscience 213:1-18(2012).
RN [18]
RP FUNCTION.
RX PubMed=23604518; DOI=10.1093/hmg/ddt186;
RA Lopez-Erauskin J., Galino J., Ruiz M., Cuezva J.M., Fabregat I.,
RA Cacabelos D., Boada J., Martinez J., Ferrer I., Pamplona R., Villarroya F.,
RA Portero-Otin M., Fourcade S., Pujol A.;
RT "Impaired mitochondrial oxidative phosphorylation in the peroxisomal
RT disease X-linked adrenoleukodystrophy.";
RL Hum. Mol. Genet. 22:3296-3305(2013).
RN [19]
RP FUNCTION.
RX PubMed=25255441; DOI=10.1371/journal.pone.0108655;
RA Muneer Z., Wiesinger C., Voigtlaender T., Werner H.B., Berger J.,
RA Forss-Petter S.;
RT "Abcd2 is a strong modifier of the metabolic impairments in peritoneal
RT macrophages of ABCD1-deficient mice.";
RL PLoS ONE 9:E108655-E108655(2014).
RN [20]
RP FUNCTION.
RX PubMed=25583114; DOI=10.1016/j.bbadis.2015.01.005;
RA Kruska N., Schoenfeld P., Pujol A., Reiser G.;
RT "Astrocytes and mitochondria from adrenoleukodystrophy protein (ABCD1)-
RT deficient mice reveal that the adrenoleukodystrophy-associated very long-
RT chain fatty acids target several cellular energy-dependent functions.";
RL Biochim. Biophys. Acta 1852:925-936(2015).
RN [21]
RP FUNCTION.
RX PubMed=26108493; DOI=10.1007/s11011-015-9701-1;
RA Morita M., Kawamichi M., Shimura Y., Kawaguchi K., Watanabe S., Imanaka T.;
RT "Brain microsomal fatty acid elongation is increased in abcd1-deficient
RT mouse during active myelination phase.";
RL Metab. Brain Dis. 30:1359-1367(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. Has fatty acyl-CoA
CC thioesterase (ACOT) and ATPase activities. Coupled to the ATP-dependent
CC transporter activity has also a fatty acyl-CoA thioesterase activity
CC (ACOT) and hydrolyzes VLCFA-CoA into VLCFA prior their ATP-dependent
CC transport into peroxisomes, the ACOT activity is essential during this
CC transport process (By similarity). Thus, plays a role in regulation of
CC VLCFAs and energy metabolism namely, in the degradation and
CC biosynthesis of fatty acids by beta-oxidation, mitochondrial function
CC and microsomal fatty acid elongation (PubMed:9126326, PubMed:9418970,
CC PubMed:9256488, PubMed:18854420, PubMed:23123468, PubMed:23604518,
CC PubMed:25255441, PubMed:25583114, PubMed:26108493). Involved in several
CC processes; namely, controls the active myelination phase by negatively
CC regulating the microsomal fatty acid elongation activity and may also
CC play a role in axon and myelin maintenance (PubMed:11875044,
CC PubMed:15489218, PubMed:26108493). Controls also the cellular response
CC to oxidative stress by regulating mitochondrial functions such as
CC mitochondrial oxidative phosphorylation and depolarization
CC (PubMed:18344354, PubMed:22521832, PubMed:23604518, PubMed:25583114).
CC And finally controls the inflammatory response by positively regulating
CC peroxisomal beta-oxidation of VLCFAs (PubMed:18723473).
CC {ECO:0000250|UniProtKB:P33897, ECO:0000269|PubMed:11875044,
CC ECO:0000269|PubMed:15489218, ECO:0000269|PubMed:18344354,
CC ECO:0000269|PubMed:18723473, ECO:0000269|PubMed:18854420,
CC ECO:0000269|PubMed:22521832, ECO:0000269|PubMed:23123468,
CC ECO:0000269|PubMed:23604518, ECO:0000269|PubMed:25255441,
CC ECO:0000269|PubMed:25583114, ECO:0000269|PubMed:26108493,
CC ECO:0000269|PubMed:9126326, ECO:0000269|PubMed:9256488,
CC ECO:0000269|PubMed:9418970}.
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:0000250|UniProtKB:P33897};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67073;
CC Evidence={ECO:0000250|UniProtKB:P33897};
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:0000250|UniProtKB:P33897};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67081;
CC Evidence={ECO:0000250|UniProtKB:P33897};
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:0000250|UniProtKB:P33897};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40788;
CC Evidence={ECO:0000250|UniProtKB:P33897};
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:0000250|UniProtKB:P33897};
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:0000250|UniProtKB:P33897};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40792;
CC Evidence={ECO:0000250|UniProtKB:P33897};
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:0000250|UniProtKB:P33897};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67085;
CC Evidence={ECO:0000250|UniProtKB:P33897};
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:0000250|UniProtKB:P33897};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40784;
CC Evidence={ECO:0000250|UniProtKB:P33897};
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:0000250|UniProtKB:P33897};
CC -!- SUBUNIT: Can form homodimers and heterodimers with ABCD2 and ABCD3
CC (PubMed:15276650). Dimerization is necessary to form an active
CC transporter (By similarity). The minimal functional unit is a homodimer
CC but the major oligomeric form in peroxisomal membrane is a
CC homotetramer. Forms heterotramers with ABCD2 (By similarity). Interacts
CC with PEX19; facilitates ABCD1 insertion into the peroxisome membrane
CC (By similarity). {ECO:0000250|UniProtKB:D3ZHR2,
CC ECO:0000250|UniProtKB:P33897, ECO:0000269|PubMed:15276650}.
CC -!- INTERACTION:
CC P48410; P33897: ABCD1; Xeno; NbExp=2; IntAct=EBI-81118, EBI-81045;
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000250|UniProtKB:P33897}; Multi-pass membrane protein
CC {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:P33897};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P33897}. Lysosome
CC membrane {ECO:0000250|UniProtKB:P33897}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P33897}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P33897}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P33897}.
CC -!- TISSUE SPECIFICITY: Widely expressed at low levels with higher levels
CC in heart, lung, intestine and spleen than in skeletal muscle, brain,
CC liver and kidney. {ECO:0000269|PubMed:10504404}.
CC -!- DEVELOPMENTAL STAGE: Most abundant in embryo. Gradually decreases
CC during maturation. {ECO:0000269|PubMed:10504404}.
CC -!- INDUCTION: By dietary fenofibrate. {ECO:0000269|PubMed:10504404}.
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:0000250|UniProtKB:P33897}.
CC -!- PTM: Tyrosine-phosphorylated. {ECO:0000250|UniProtKB:D3ZHR2}.
CC -!- DISRUPTION PHENOTYPE: Abcd1 hemizygous males are viable and apparently
CC healthy and they show no detectable motor defect for at least 4-month-
CC old. Inbreeding homozygous and hemizygous Abcd1-deficient mice show a
CC reduction of fertility. Moreover, among several 6-month-old mice, there
CC is at least one apparently infertile mutant of each sex. The infertile
CC hemizygous male show additionally a severe testicular atrophy
CC (PubMed:9418970). Abcd1 hemizygous mutant male and homozygous mutant
CC mice grow normally, are fer- tile, and appear normal at least up to one
CC year of age (PubMed:9126326). Abcd1 hemizygous mutant male and
CC homozygous mutant mice grow normally, are fer- tile, and appear normal
CC at least up to 6 months of age (PubMed:9256488). At 20 months of age,
CC Abcd1 homozygous mice present an impairment of their locomotor
CC coordination and exploratory abilities (PubMed:11875044,
CC PubMed:15489218). Double Abcd1 and Abcd2 knockout mice exhibit severe
CC impairment of their locomotor coordination and exploratory abilities
CC already at 15 months of age (PubMed:15489218).
CC {ECO:0000269|PubMed:11875044, ECO:0000269|PubMed:15489218,
CC ECO:0000269|PubMed:9126326, ECO:0000269|PubMed:9256488,
CC ECO:0000269|PubMed:9418970}.
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}.
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DR EMBL; Z33637; CAA83917.1; -; mRNA.
DR EMBL; AK088792; BAC40574.1; -; mRNA.
DR EMBL; BC011273; AAH11273.1; -; mRNA.
DR EMBL; BC079840; AAH79840.1; -; mRNA.
DR EMBL; AJ009991; CAA08935.1; -; Genomic_DNA.
DR EMBL; AF133093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS30210.1; -.
DR PIR; S47044; S47044.
DR RefSeq; NP_031461.1; NM_007435.2.
DR AlphaFoldDB; P48410; -.
DR SMR; P48410; -.
DR BioGRID; 198062; 2.
DR IntAct; P48410; 1.
DR STRING; 10090.ENSMUSP00000002084; -.
DR GlyGen; P48410; 1 site.
DR iPTMnet; P48410; -.
DR PhosphoSitePlus; P48410; -.
DR EPD; P48410; -.
DR MaxQB; P48410; -.
DR PaxDb; P48410; -.
DR PeptideAtlas; P48410; -.
DR PRIDE; P48410; -.
DR ProteomicsDB; 285955; -.
DR Antibodypedia; 30940; 439 antibodies from 35 providers.
DR DNASU; 11666; -.
DR Ensembl; ENSMUST00000002084; ENSMUSP00000002084; ENSMUSG00000031378.
DR GeneID; 11666; -.
DR KEGG; mmu:11666; -.
DR UCSC; uc009tml.1; mouse.
DR CTD; 215; -.
DR MGI; MGI:1349215; Abcd1.
DR VEuPathDB; HostDB:ENSMUSG00000031378; -.
DR eggNOG; KOG0064; Eukaryota.
DR GeneTree; ENSGT00950000182955; -.
DR HOGENOM; CLU_007587_1_1_1; -.
DR InParanoid; P48410; -.
DR OMA; IPRWNSK; -.
DR OrthoDB; 309052at2759; -.
DR PhylomeDB; P48410; -.
DR TreeFam; TF105205; -.
DR BRENDA; 7.6.2.4; 3474.
DR Reactome; R-MMU-1369062; ABC transporters in lipid homeostasis.
DR Reactome; R-MMU-2046105; Linoleic acid (LA) metabolism.
DR Reactome; R-MMU-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-MMU-390247; Beta-oxidation of very long chain fatty acids.
DR Reactome; R-MMU-9603798; Class I peroxisomal membrane protein import.
DR BioGRID-ORCS; 11666; 1 hit in 61 CRISPR screens.
DR ChiTaRS; Abcd1; mouse.
DR PRO; PR:P48410; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P48410; protein.
DR Bgee; ENSMUSG00000031378; Expressed in small intestine Peyer's patch and 252 other tissues.
DR ExpressionAtlas; P48410; baseline and differential.
DR Genevisible; P48410; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; ISO:MGI.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:HGNC-UCL.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
DR GO; GO:0015607; F:ABC-type fatty-acyl-CoA transporter activity; ISS:UniProtKB.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; ISS:UniProtKB.
DR GO; GO:0043531; F:ADP binding; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IMP:UniProtKB.
DR GO; GO:0030497; P:fatty acid elongation; IMP:UniProtKB.
DR GO; GO:0055089; P:fatty acid homeostasis; IMP:UniProtKB.
DR GO; GO:0042758; P:long-chain fatty acid catabolic process; ISS:UniProtKB.
DR GO; GO:0015910; P:long-chain fatty acid import into peroxisome; ISS:UniProtKB.
DR GO; GO:0043217; P:myelin maintenance; IMP:UniProtKB.
DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IMP:UniProtKB.
DR GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; IMP:UniProtKB.
DR GO; GO:1990535; P:neuron projection maintenance; IMP:UniProtKB.
DR GO; GO:0007031; P:peroxisome organization; ISO:MGI.
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; IMP:UniProtKB.
DR GO; GO:1900407; P:regulation of cellular response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0031998; P:regulation of fatty acid beta-oxidation; IMP:UniProtKB.
DR GO; GO:0051900; P:regulation of mitochondrial depolarization; IMP:UniProtKB.
DR GO; GO:0002082; P:regulation of oxidative phosphorylation; IMP:UniProtKB.
DR GO; GO:0055092; P:sterol homeostasis; IMP:UniProtKB.
DR GO; GO:0042760; P:very long-chain fatty acid catabolic process; IMP:UniProtKB.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IMP:UniProtKB.
DR GO; GO:0036113; P:very long-chain fatty-acyl-CoA catabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
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 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 ATP-binding; Endoplasmic reticulum; Glycoprotein; Hydrolase; Lysosome;
KW Membrane; Mitochondrion; Nucleotide-binding; Peroxisome;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..736
FT /note="ATP-binding cassette sub-family D member 1"
FT /id="PRO_0000093305"
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 338..358
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..729
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 67..186
FT /note="Interaction with PEX19"
FT /evidence="ECO:0000250|UniProtKB:P33897"
FT REGION 67..84
FT /note="PEX19 binding site and required for peroxisomal
FT targeting"
FT /evidence="ECO:0000250|UniProtKB:P33897"
FT REGION 658..736
FT /note="Required for homodimerization"
FT /evidence="ECO:0000250|UniProtKB:P33897"
FT BINDING 507..514
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 736 AA; 81859 MW; 20B1B191DFC599E9 CRC64;
MPVLSTPRPS RVTTLKRTAV VLALTAYGVH KIYPLVRQCL TPARGPQVPA GEPTQEASGA
TATKAGMNRV FLQRLLALLR LLFPRVLCRE TGLLALHSAA LVSRTFLSVY VARLDGRLAR
CIVRKDPRAF SWQLLQWLLI ALPATFINSA IRYLEGQLAL SFRSRLVAHA YGLYFSQQTY
YRVSNMDGRL RNPDQSLTED VVAFAASVAH LYSNLTKPLL DVAVTSYTLL RAARSRGAGT
AWPSAIAGLV VFLTANVLRA FSPKFGELVA EEARRKGELR YMHSRVVANS EEIAFYGGHE
VELALLQHSY QDLASQINLI LLERLWYVML EQFLMKYVWS ASGLLMVAVP IITATGYAES
DSEAMKKAAL EMKEEELVSE RTEAFTIARN LLTAAADATE RIMSSYKEVT ELAGYTARVY
EMFQVFEDVK HCRFKRTGDL EEAQAGPGVM VQSGVHVEGP LKIQGQVVDV EQGIICENIP
IITPTGEVVV ASLNIRVEEG MHLLITGPNG CGKSSLFRIL GGLWPTYSGV LYKPPPQRMF
YIPQRPYMSV GSLRDQVIYP DSAEDMRRKG CSEQQLEAIL GIVHLRHILQ REGGWEAVCD
WKDVLSGGEK QRIGMARMFY HRPKYALLDE CTSAVSIDVE GKIFQAAKDA GIALLSITHR
PSLWKYHTHL LQFDGEGGWK FEKLDSAARL SLTEEKQRLE QQLAGIPKMQ GRLQELRQIL
GEAAAPVQPL VPGVPT
