ID ABCD2_HUMAN Reviewed; 740 AA. AC Q9UBJ2; B2RAM3; Q13210; Q2M3H9; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 24-JAN-2024, entry version 191. DE RecName: Full=ATP-binding cassette sub-family D member 2; DE EC=3.1.2.- {ECO:0000269|PubMed:29397936}; DE EC=7.6.2.- {ECO:0000269|PubMed:29397936, ECO:0000305|PubMed:16946495}; DE AltName: Full=Adrenoleukodystrophy-like 1; DE AltName: Full=Adrenoleukodystrophy-related protein; DE Short=hALDR; GN Name=ABCD2 {ECO:0000312|HGNC:HGNC:66}; GN Synonyms=ALD1, ALDL1, ALDR {ECO:0000303|PubMed:10777694}, ALDRP GN {ECO:0000303|PubMed:10329405, ECO:0000303|PubMed:16946495}; 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]. RX PubMed=8577752; DOI=10.1073/pnas.93.3.1265; RA Lombard-Platet G., Savary S., Sarde C.-O., Mandel J.-L., Chimini G.; RT "A close relative of the adrenoleukodystrophy (ALD) gene codes for a RT peroxisomal protein with a specific expression pattern."; RL Proc. Natl. Acad. Sci. U.S.A. 93:1265-1269(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX PubMed=9345306; DOI=10.1006/bbrc.1997.7391; RA Holzinger A., Kammerer S., Berger J., Roscher A.A.; RT "cDNA cloning and mRNA expression of the human adrenoleukodystrophy related RT protein (ALDRP), a peroxisomal ABC transporter."; RL Biochem. Biophys. Res. Commun. 239:261-264(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND SUBCELLULAR LOCATION. RX PubMed=10329405; DOI=10.1006/bbrc.1999.0535; RA Holzinger A., Mayerhofer P., Berger J., Lichtner P., Kammerer S., RA Roscher A.A.; RT "Full length cDNA cloning, promoter sequence, and genomic organization of RT the human adrenoleukodystrophy related (ALDR) gene functionally redundant RT to the gene responsible for X-linked adrenoleukodystrophy."; RL Biochem. Biophys. Res. Commun. 258:436-442(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; 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 [7] RP SUBUNIT, AND INTERACTION WITH ABCD3. 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 [8] RP INTERACTION WITH PEX19. 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 [9] 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 [10] RP FUNCTION, AND CATALYTIC ACTIVITY. 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 [11] RP INTERACTION WITH ABCD1, AND SUBUNIT. 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 [12] RP SUBCELLULAR LOCATION, 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 [13] 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 [14] RP VARIANT [LARGE SCALE ANALYSIS] LYS-244. RX PubMed=18772397; DOI=10.1126/science.1164368; RA Jones S., Zhang X., Parsons D.W., Lin J.C., Leary R.J., Angenendt P., RA Mankoo P., Carter H., Kamiyama H., Jimeno A., Hong S.M., Fu B., Lin M.T., RA Calhoun E.S., Kamiyama M., Walter K., Nikolskaya T., Nikolsky Y., RA Hartigan J., Smith D.R., Hidalgo M., Leach S.D., Klein A.P., Jaffee E.M., RA Goggins M., Maitra A., Iacobuzio-Donahue C., Eshleman J.R., Kern S.E., RA Hruban R.H., Karchin R., Papadopoulos N., Parmigiani G., Vogelstein B., RA Velculescu V.E., Kinzler K.W.; RT "Core signaling pathways in human pancreatic cancers revealed by global RT genomic analyses."; RL Science 321:1801-1806(2008). 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:21145416, CC PubMed:29397936). Like ABCD1 seems to have fatty acyl-CoA thioesterase CC (ACOT) and ATPase activities, according to this model, VLCFA-CoA as CC free VLCFA is transpoted in an ATP-dependent manner into peroxisomes CC after the hydrolysis of VLCFA-CoA mediated by the ACOT activity of CC ABCD2 (Probable) (PubMed:29397936). Shows overlapping substrate CC specificities with ABCD1 toward saturated fatty acids (FA) and CC monounsaturated FA (MUFA) but has a distinct substrate preference for CC shorter VLCFA (C22:0) and polyunsaturated fatty acid (PUFA) such as CC C22:6-CoA and C24:6-CoA (in vitro) (PubMed:21145416). Thus, may play a CC role in regulation of VLCFAs and energy metabolism namely, in the CC degradation and biosynthesis of fatty acids by beta-oxidation CC (PubMed:21145416). {ECO:0000269|PubMed:21145416, CC ECO:0000269|PubMed:29397936, ECO:0000305|PubMed:16946495}. 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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67073; CC Evidence={ECO:0000305|PubMed:29397936}; 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:29397936, ECO:0000305|PubMed:16946495}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67081; CC Evidence={ECO:0000305|PubMed:29397936}; CC -!- SUBUNIT: Homodimers (By similarity). Homotetramers (By similarity). The CC minimal functional unit is a homodimer but the major oligomeric form in CC peroxisomal membrane is a homotetramer (By similarity). Forms CC heterodimers with ABCD1 (PubMed:17609205). Forms heterodimers with CC ABCD3 (PubMed:10551832). In addition to tetramers, some larger CC molecular assemblies are also found but represented only a minor CC fraction (By similarity). Interacts with PEX19; facilitates ABCD2 CC insertion into the peroxisome membrane (PubMed:10777694, CC PubMed:10704444). {ECO:0000250|UniProtKB:Q9QY44, CC ECO:0000269|PubMed:10551832, ECO:0000269|PubMed:10704444, CC ECO:0000269|PubMed:10777694, ECO:0000269|PubMed:17609205}. CC -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:10329405, CC ECO:0000269|PubMed:21145416, ECO:0000269|PubMed:29397936}; Multi-pass CC membrane protein {ECO:0000255}. CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain and heart. CC {ECO:0000269|PubMed:9345306}. 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=ABCMdb; Note=Database for mutations in ABC proteins; CC URL="http://abcm2.hegelab.org/search"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U28150; AAB00541.1; -; Genomic_DNA. DR EMBL; AJ000327; CAA03994.1; -; mRNA. DR EMBL; AF119831; AAD30439.1; -; Genomic_DNA. DR EMBL; AF119822; AAD30439.1; JOINED; Genomic_DNA. DR EMBL; AF119823; AAD30439.1; JOINED; Genomic_DNA. DR EMBL; AF119824; AAD30439.1; JOINED; Genomic_DNA. DR EMBL; AF119826; AAD30439.1; JOINED; Genomic_DNA. DR EMBL; AF119825; AAD30439.1; JOINED; Genomic_DNA. DR EMBL; AF119827; AAD30439.1; JOINED; Genomic_DNA. DR EMBL; AF119828; AAD30439.1; JOINED; Genomic_DNA. DR EMBL; AF119829; AAD30439.1; JOINED; Genomic_DNA. DR EMBL; AF119830; AAD30439.1; JOINED; Genomic_DNA. DR EMBL; AK314254; BAG36920.1; -; mRNA. DR EMBL; CH471111; EAW57807.1; -; Genomic_DNA. DR EMBL; BC104901; AAI04902.1; -; mRNA. DR EMBL; BC104903; AAI04904.1; -; mRNA. DR CCDS; CCDS8734.1; -. DR PIR; JC5712; JC5712. DR RefSeq; NP_005155.1; NM_005164.3. DR RefSeq; XP_011536329.1; XM_011538027.2. DR AlphaFoldDB; Q9UBJ2; -. DR SMR; Q9UBJ2; -. DR BioGRID; 106727; 5. DR IntAct; Q9UBJ2; 3. DR STRING; 9606.ENSP00000310688; -. DR TCDB; 3.A.1.203.7; the atp-binding cassette (abc) superfamily. DR GlyCosmos; Q9UBJ2; 2 sites, No reported glycans. DR GlyGen; Q9UBJ2; 2 sites. DR iPTMnet; Q9UBJ2; -. DR PhosphoSitePlus; Q9UBJ2; -. DR BioMuta; ABCD2; -. DR DMDM; 12643305; -. DR jPOST; Q9UBJ2; -. DR MassIVE; Q9UBJ2; -. DR MaxQB; Q9UBJ2; -. DR PaxDb; 9606-ENSP00000310688; -. DR PeptideAtlas; Q9UBJ2; -. DR ProteomicsDB; 83977; -. DR Antibodypedia; 42512; 300 antibodies from 31 providers. DR DNASU; 225; -. DR Ensembl; ENST00000308666.4; ENSP00000310688.3; ENSG00000173208.4. DR GeneID; 225; -. DR KEGG; hsa:225; -. DR MANE-Select; ENST00000308666.4; ENSP00000310688.3; NM_005164.4; NP_005155.1. DR UCSC; uc001rmb.3; human. DR AGR; HGNC:66; -. DR CTD; 225; -. DR DisGeNET; 225; -. DR GeneCards; ABCD2; -. DR HGNC; HGNC:66; ABCD2. DR HPA; ENSG00000173208; Tissue enhanced (adipose). DR MIM; 601081; gene. DR neXtProt; NX_Q9UBJ2; -. DR OpenTargets; ENSG00000173208; -. DR PharmGKB; PA24401; -. DR VEuPathDB; HostDB:ENSG00000173208; -. DR eggNOG; KOG0064; Eukaryota. DR GeneTree; ENSGT00950000182955; -. DR HOGENOM; CLU_007587_1_1_1; -. DR InParanoid; Q9UBJ2; -. DR OMA; DIQAGHF; -. DR OrthoDB; 7698at2759; -. DR PhylomeDB; Q9UBJ2; -. DR TreeFam; TF105205; -. DR BRENDA; 7.6.2.4; 2681. DR PathwayCommons; Q9UBJ2; -. DR Reactome; R-HSA-1369062; ABC transporters in lipid homeostasis. DR Reactome; R-HSA-9603798; Class I peroxisomal membrane protein import. DR SignaLink; Q9UBJ2; -. DR BioGRID-ORCS; 225; 14 hits in 1151 CRISPR screens. DR ChiTaRS; ABCD2; human. DR GeneWiki; ABCD2; -. DR GenomeRNAi; 225; -. DR Pharos; Q9UBJ2; Tbio. DR PRO; PR:Q9UBJ2; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q9UBJ2; Protein. DR Bgee; ENSG00000173208; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 101 other cell types or tissues. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central. DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB. DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro. DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IBA:GO_Central. 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:0005324; F:long-chain fatty acid transporter activity; IBA:GO_Central. DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0006635; P:fatty acid beta-oxidation; IGI:UniProtKB. DR GO; GO:0015910; P:long-chain fatty acid import into peroxisome; IBA:GO_Central. 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:0007031; P:peroxisome organization; IBA:GO_Central. DR GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; IDA:UniProtKB. DR GO; GO:2001280; P:positive regulation of unsaturated fatty acid biosynthetic process; ISS:UniProtKB. DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl. DR GO; GO:0042760; P:very long-chain fatty acid catabolic process; IGI:UniProtKB. DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IDA:UniProtKB. DR CDD; cd03223; ABCD_peroxisomal_ALDP; 1. DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR11384:SF24; ATP-BINDING CASSETTE SUB-FAMILY D MEMBER 2; 1. DR PANTHER; PTHR11384; ATP-BINDING CASSETTE, SUB-FAMILY D MEMBER; 1. DR Pfam; PF06472; ABC_membrane_2; 1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF90123; ABC transporter transmembrane region; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR Genevisible; Q9UBJ2; HS. PE 1: Evidence at protein level; KW ATP-binding; Glycoprotein; Hydrolase; Membrane; Nucleotide-binding; KW Peroxisome; Reference proteome; Translocase; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..740 FT /note="ATP-binding cassette sub-family D member 2" FT /id="PRO_0000093306" FT TRANSMEM 107..127 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 144..164 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 251..271 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT TRANSMEM 351..371 FT /note="Helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT DOMAIN 107..399 FT /note="ABC transmembrane type-1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441" FT DOMAIN 478..704 FT /note="ABC transporter" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT REGION 1..218 FT /note="Interaction with PEX19" FT /evidence="ECO:0000269|PubMed:10777694" FT BINDING 511..518 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT CARBOHYD 190 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 227 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VARIANT 244 FT /note="Q -> K (in a pancreatic ductal adenocarcinoma FT sample; somatic mutation)" FT /evidence="ECO:0000269|PubMed:18772397" FT /id="VAR_062664" FT CONFLICT 18 FT /note="S -> G (in Ref. 1; AAB00541)" FT /evidence="ECO:0000305" SQ SEQUENCE 740 AA; 83233 MW; 9F3C8DBB8AB156E3 CRC64; MTHMLNAAAD RVKWTRSSAA KRAACLVAAA YALKTLYPII GKRLKQSGHG KKKAAAYPAA ENTEILHCTE TICEKPSPGV NADFFKQLLE LRKILFPKLV TTETGWLCLH SVALISRTFL SIYVAGLDGK IVKSIVEKKP RTFIIKLIKW LMIAIPATFV NSAIRYLECK LALAFRTRLV DHAYETYFTN QTYYKVINMD GRLANPDQSL TEDIMMFSQS VAHLYSNLTK PILDVMLTSY TLIQTATSRG ASPIGPTLLA GLVVYATAKV LKACSPKFGK LVAEEAHRKG YLRYVHSRII ANVEEIAFYR GHKVEMKQLQ KSYKALADQM NLILSKRLWY IMIEQFLMKY VWSSSGLIMV AIPIITATGF ADGEDGQKQV MVSERTEAFT TARNLLASGA DAIERIMSSY KEVTELAGYT ARVYNMFWVF DEVKRGIYKR TAVIQESESH SKNGAKVELP LSDTLAIKGK VIDVDHGIIC ENVPIITPAG EVVASRLNFK VEEGMHLLIT GPNGCGKSSL FRILSGLWPV YEGVLYKPPP QHMFYIPQRP YMSLGSLRDQ VIYPDSVDDM HDKGYTDQDL ERILHNVHLY HIVQREGGWD AVMDWKDVLS GGEKQRMGMA RMFYHKPKYA LLDECTSAVS IDVEGKIFQA AKGAGISLLS ITHRPSLWKY HTHLLQFDGE GGWRFEQLDT AIRLTLSEEK QKLESQLAGI PKMQQRLNEL CKILGEDSVL KTIKNEDETS //