ABCD1_DANRE
ID ABCD1_DANRE Reviewed; 766 AA.
AC F1RBC8;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 78.
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|ZFIN:ZDB-GENE-050517-27}; ORFNames=si:ch211-169p10;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=28911205; DOI=10.1093/hmg/ddx249;
RA Strachan L.R., Stevenson T.J., Freshner B., Keefe M.D., Miranda Bowles D.,
RA Bonkowsky J.L.;
RT "A zebrafish model of X-linked adrenoleukodystrophy recapitulates key
RT disease features and demonstrates a developmental requirement for abcd1 in
RT oligodendrocyte patterning and myelination.";
RL Hum. Mol. Genet. 26:3600-3614(2017).
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. 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. 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 (By similarity). Involved in
CC oligodendrocyte patterning and myelination (PubMed:28911205).
CC {ECO:0000250|UniProtKB:P33897, ECO:0000269|PubMed:28911205}.
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 -!- 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 -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000250|UniProtKB:P33897}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Expressed from 48 hpf in the nervous system, floor
CC plate, and pronephros/interrenal gland. By 72 hpf and persisting
CC through 96 hpf expression is present in the central nervous system
CC (CNS), floorplate, interrenal glands/pronephros, and gut. At 72 hpf
CC expressed in the brain and spinal cord. {ECO:0000269|PubMed:28911205}.
CC -!- DISRUPTION PHENOTYPE: abcd1 deficient zebrafish appear normal. By day
CC of life five abcd1 mutants demonstrate impaired motor function, and
CC overall survival to adulthood of heterozygous and homozygous mutants is
CC decreased. {ECO:0000269|PubMed:28911205}.
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; BX005406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005166771.1; XM_005166714.3.
DR AlphaFoldDB; F1RBC8; -.
DR SMR; F1RBC8; -.
DR STRING; 7955.ENSDARP00000101144; -.
DR TCDB; 3.A.1.203.15; the atp-binding cassette (abc) superfamily.
DR PaxDb; F1RBC8; -.
DR Ensembl; ENSDART00000111392; ENSDARP00000101144; ENSDARG00000074876.
DR GeneID; 566367; -.
DR CTD; 215; -.
DR ZFIN; ZDB-GENE-050517-27; abcd1.
DR eggNOG; KOG0064; Eukaryota.
DR GeneTree; ENSGT00950000182955; -.
DR HOGENOM; CLU_007587_1_1_1; -.
DR InParanoid; F1RBC8; -.
DR OrthoDB; 309052at2759; -.
DR PhylomeDB; F1RBC8; -.
DR TreeFam; TF105205; -.
DR Reactome; R-DRE-1369062; ABC transporters in lipid homeostasis.
DR Reactome; R-DRE-2046105; Linoleic acid (LA) metabolism.
DR Reactome; R-DRE-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-DRE-390247; Beta-oxidation of very long chain fatty acids.
DR Reactome; R-DRE-9603798; Class I peroxisomal membrane protein import.
DR PRO; PR:F1RBC8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 8.
DR Bgee; ENSDARG00000074876; Expressed in mature ovarian follicle and 19 other tissues.
DR ExpressionAtlas; F1RBC8; baseline.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR GO; GO:0015607; F:ABC-type fatty-acyl-CoA transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; ISS:UniProtKB.
DR GO; GO:0030325; P:adrenal gland development; IMP:UniProtKB.
DR GO; GO:0030301; P:cholesterol transport; IMP:ZFIN.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISS:UniProtKB.
DR GO; GO:0015910; P:long-chain fatty acid import into peroxisome; ISS:UniProtKB.
DR GO; GO:0061744; P:motor behavior; IMP:UniProtKB.
DR GO; GO:0014003; P:oligodendrocyte development; IMP:UniProtKB.
DR GO; GO:0007031; P:peroxisome organization; IBA:GO_Central.
DR GO; GO:0031643; P:positive regulation of myelination; IMP:UniProtKB.
DR GO; GO:0036269; P:swimming behavior; IMP:UniProtKB.
DR GO; GO:0042760; P:very long-chain fatty acid catabolic process; IBA:GO_Central.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IMP:UniProtKB.
DR Gene3D; 1.20.1560.10; -; 1.
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; 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 PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Hydrolase; Membrane; Nucleotide-binding; Peroxisome;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..766
FT /note="ATP-binding cassette sub-family D member 1"
FT /id="PRO_0000445227"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 101..393
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 482..708
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 728..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..750
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..766
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 515..522
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 766 AA; 86594 MW; 690B1502F0619D2C CRC64;
MSVYSKLPSQ LKKPLVKKAV VLLIALYGVK KLSPYFFGKL KGRTSKQVKG ADPLTSNGEP
LVEAARKRKR SPAVNREFFD RLIRLLKILF PRLFCKELGL LGFHSLALIS RTFLSIYVAN
LDGQIVKTIV KKDPRAFVVE LTKWLLIAIP ATFVNSAIRY LEGQLTLAFR TRLVTHAYML
YFSDQTYYRV SNMDGRLANP DQSLTEDVVM FAASVAHLYS NLTKPILDVV VTCYTLIKTA
ESKGANTTWP SVIAGIVVAL TAKVLRAFSP RFGKLVAEEA RRKGDLRYMH SRIIANSEEI
AFYGGHKIEM LQLQRSYNSL SRQINLILFK RLWYVMLEQF LMKYLWSASG LVMVAVPIIT
ATGYSKYDSE DVKQAALDMK EEDLVSERTQ AFTTARSLLN AAADAVERIM VSYKEVTELA
GYTARVYEMF EVFEDVRDGV YRRSATEVKP EETGAPQNVT HGMRVEGPLQ IRGQVIDVEQ
GIKCENLPII TPTGDVVVSS LNMQVDEGMH LLITGPNGCG KSSLFRILSG LWPVYSGVLY
KPSPDHMFYI PQRPYMSVGT LRDQVIYPHS VQEMQEKGIT DRQLEEILQT VSLRYILERE
GGWDAVSDWK DVLSGGEKQR MGMARMFYHK PQYALLDECT SAVSIDVEGK IFEAAKDAGI
SLLSITHRPS LWKYHSHLLQ FDGEGGWRFE KLDASTRISL QDEKIRLETQ LSGIPKMQQR
LTELCRILGE DSSLPTPGDE EEDEEEDEKQ TERDVQSAGK EKDLME
