ABCD2_HUMAN
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 03-AUG-2022, entry version 183.
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},
GN ALDRP {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";
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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 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; Q9UBJ2; -.
DR PeptideAtlas; Q9UBJ2; -.
DR PRIDE; Q9UBJ2; -.
DR ProteomicsDB; 83977; -.
DR Antibodypedia; 42512; 272 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 CTD; 225; -.
DR DisGeNET; 225; -.
DR GeneCards; ABCD2; -.
DR HGNC; HGNC:66; ABCD2.
DR HPA; ENSG00000173208; Tissue enhanced (adipose tissue, brain).
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; IPEMQNR; -.
DR OrthoDB; 309052at2759; -.
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 1071 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 cortical plate and 101 other tissues.
DR Genevisible; Q9UBJ2; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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; 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 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; IPR031239; ABCD2.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11384:SF24; PTHR11384:SF24; 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 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
