ABCD_DROME
ID ABCD_DROME Reviewed; 730 AA.
AC Q7JUN3;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=ATP-binding cassette sub-family D member {ECO:0000312|FlyBase:FBgn0039890};
DE EC=7.6.2.4 {ECO:0000250|UniProtKB:P33897};
GN Name=ABCD {ECO:0000312|FlyBase:FBgn0039890};
GN ORFNames=CG2316 {ECO:0000312|FlyBase:FBgn0039890};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAM52684.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM52684.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAM52684.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=29739804; DOI=10.1242/dmm.031286;
RA Gordon H.B., Valdez L., Letsou A.;
RT "Etiology and treatment of adrenoleukodystrophy: new insights from
RT Drosophila.";
RL Dis. Model. Mech. 11:0-0(2018).
CC -!- FUNCTION: Plays a role in the transport of free very-long-chain fatty
CC acids (VLCFAs) as well as their CoA-esters across the peroxisomal
CC membrane by acting as an ATP-specific binding subunit releasing ADP
CC after ATP hydrolysis. Thus, plays a role in regulation of VLCFAs and
CC energy metabolism namely, in the degradation and biosynthesis of fatty
CC acids by beta-oxidation, mitochondrial function and microsomal fatty
CC acid elongation. {ECO:0000250|UniProtKB:P33897}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA(out) + ATP + H2O = ADP + an acyl-CoA(in) + H(+) +
CC phosphate; Xref=Rhea:RHEA:15181, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:456216; EC=7.6.2.4;
CC Evidence={ECO:0000250|UniProtKB:P33897};
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000250|UniProtKB:P33897}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown survives to adulthood,
CC but suffer from neurodegeneration including age-dependent retinal
CC disorganization with retinal holes and pigment cell loss
CC (PubMed:29739804). RNAi-mediated knockdown in the neurons results in a
CC similar phenotype (PubMed:29739804). Effects are probably due to
CC elevated levels of very long chain fatty acids (VLCFAs)
CC (PubMed:29739804). In contrast, glial-specific RNAi-mediated knockdown
CC results in no defect (PubMed:29739804). {ECO:0000269|PubMed:29739804}.
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; AE014135; AAF59365.1; -; Genomic_DNA.
DR EMBL; AE014135; AAF59366.1; -; Genomic_DNA.
DR EMBL; AE014135; AAF59367.2; -; Genomic_DNA.
DR EMBL; AE014135; AAN06515.1; -; Genomic_DNA.
DR EMBL; AE014135; AAN06517.1; -; Genomic_DNA.
DR EMBL; AE014135; AFH06769.1; -; Genomic_DNA.
DR EMBL; AY122172; AAM52684.1; -; mRNA.
DR RefSeq; NP_001245409.1; NM_001258480.1.
DR RefSeq; NP_651906.1; NM_143649.3.
DR RefSeq; NP_726542.1; NM_166736.4.
DR RefSeq; NP_726543.1; NM_166737.3.
DR RefSeq; NP_726544.1; NM_166738.3.
DR RefSeq; NP_726546.1; NM_166740.2.
DR AlphaFoldDB; Q7JUN3; -.
DR SMR; Q7JUN3; -.
DR IntAct; Q7JUN3; 5.
DR STRING; 7227.FBpp0088213; -.
DR PaxDb; Q7JUN3; -.
DR PRIDE; Q7JUN3; -.
DR DNASU; 43772; -.
DR EnsemblMetazoa; FBtr0089146; FBpp0088213; FBgn0039890.
DR EnsemblMetazoa; FBtr0089147; FBpp0088214; FBgn0039890.
DR EnsemblMetazoa; FBtr0089148; FBpp0088215; FBgn0039890.
DR EnsemblMetazoa; FBtr0089149; FBpp0088216; FBgn0039890.
DR EnsemblMetazoa; FBtr0089150; FBpp0088217; FBgn0039890.
DR EnsemblMetazoa; FBtr0308247; FBpp0300567; FBgn0039890.
DR GeneID; 43772; -.
DR KEGG; dme:Dmel_CG2316; -.
DR UCSC; CG2316-RA; d. melanogaster.
DR CTD; 43772; -.
DR FlyBase; FBgn0039890; ABCD.
DR VEuPathDB; VectorBase:FBgn0039890; -.
DR eggNOG; KOG0064; Eukaryota.
DR GeneTree; ENSGT00950000182955; -.
DR HOGENOM; CLU_007587_1_1_1; -.
DR InParanoid; Q7JUN3; -.
DR OMA; IPRWNSK; -.
DR OrthoDB; 309052at2759; -.
DR PhylomeDB; Q7JUN3; -.
DR Reactome; R-DME-1369062; ABC transporters in lipid homeostasis.
DR Reactome; R-DME-2046105; Linoleic acid (LA) metabolism.
DR Reactome; R-DME-2046106; alpha-linolenic acid (ALA) metabolism.
DR Reactome; R-DME-390247; Beta-oxidation of very long chain fatty acids.
DR Reactome; R-DME-9603798; Class I peroxisomal membrane protein import.
DR SignaLink; Q7JUN3; -.
DR BioGRID-ORCS; 43772; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43772; -.
DR PRO; PR:Q7JUN3; -.
DR Proteomes; UP000000803; Chromosome 4.
DR Bgee; FBgn0039890; Expressed in midgut and 27 other tissues.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; ISS:FlyBase.
DR GO; GO:0005778; C:peroxisomal membrane; ISS:FlyBase.
DR GO; GO:0015607; F:ABC-type fatty-acyl-CoA transporter activity; ISS:FlyBase.
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:FlyBase.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR GO; GO:0015910; P:long-chain fatty acid import into peroxisome; ISS:FlyBase.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; IMP:UniProtKB.
DR GO; GO:0007031; P:peroxisome organization; IBA:GO_Central.
DR GO; GO:0042760; P:very long-chain fatty acid catabolic process; IBA:GO_Central.
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; IPR027417; P-loop_NTPase.
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; Membrane; Nucleotide-binding; Peroxisome; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..730
FT /note="ATP-binding cassette sub-family D member"
FT /evidence="ECO:0000305"
FT /id="PRO_0000447340"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 136..373
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 505..727
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 538..545
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 730 AA; 82639 MW; 0041926ED35C717C CRC64;
MSVLSKYVDR IAEKCEHNGF TKHAFSYALV TSAILALTIK VTIPYVKNVN TTSSVRTQKG
KTNGQLSPST RDSSEEDFKL AEAEKLLVAQ QLKKKATNNL VEPGLNKEFL KHLQMLAKIM
IPQAFCYETG LLSVHTFCLI SRTFLSIYVA ALEGALVKFI VRKDIKQFAL VLLKWFGIAI
PATFVNSMIR FLESKLSLAF RTRLVRHSYR LYFKNQNYYR VSNLDGRIEN ADHRLTEDIS
VFANSVAHLY SSLTKPCFDL MLIGLALMRS SKKMKANIIT GPALSIGVIA LTAHILRIVS
PKFGQLVSEE ANRYGYLRHI HSRIITNAEE IAFYGGHKVE MQQLRQAYNR LVNQMTTIFN
QKLWFIMLEQ FFMKYVWSGT GMIMVSLPIL TGSDVGLGTV PNTAISESRV SERTQYLTTA
RNLLISAADA IERLMSSYKE IVSLAGYTFR VAGMMDVFEE TALGVYCKTS VMESNQSNGI
IEFRNGKPIA KGRIIYSDDP KNMSISLRAV PVVTPNCDIV VPKLTLCIEP GVHLLITGPN
GCGKSSLFRI LSGLWPIYAG ELHIPRPVKD VPCMFYIPQR PYMSIGSLCD QIIYPDTRED
MKRKHITENE LRSILKMVSL EHIAQRDSFD VVRDWKDILS GGEKQRMAIA RLFYHRPRYA
LLDECTSAVS IDVESSIYEI AKGMGITLLT ITHRPTLWKY HTHILEFDGL GNWQFRKMNS
DEEQKGQFLS
