ABCD3_RAT
ID ABCD3_RAT Reviewed; 659 AA.
AC P16970;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=ATP-binding cassette sub-family D member 3;
DE EC=3.1.2.- {ECO:0000250|UniProtKB:P28288};
DE EC=7.6.2.- {ECO:0000250|UniProtKB:P28288};
DE AltName: Full=70 kDa peroxisomal membrane protein {ECO:0000303|PubMed:10207018, ECO:0000303|PubMed:1968461};
DE Short=PMP70;
GN Name=Abcd3; Synonyms=Pmp70, Pxmp1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=1968461; DOI=10.1016/s0021-9258(19)39595-x;
RA Kamijo K., Taketani S., Yokota S., Osumi T., Hashimoto T.;
RT "The 70-kDa peroxisomal membrane protein is a member of the Mdr (P-
RT glycoprotein)-related ATP-binding protein superfamily.";
RL J. Biol. Chem. 265:4534-4540(1990).
RN [2]
RP PROTEIN SEQUENCE OF 2-15 AND 283-296.
RC TISSUE=Liver;
RX PubMed=10527525; DOI=10.1006/abio.1999.4281;
RA Gouveia A.M.M., Reguenga C., Oliveira M.E.M., Eckerskorn C., Sa-Miranda C.,
RA Azevedo J.E.;
RT "Alkaline density gradient floatation of membranes: polypeptide composition
RT of the mammalian peroxisomal membrane.";
RL Anal. Biochem. 274:270-277(1999).
RN [3]
RP SUBCELLULAR LOCATION, FUNCTION, AND MUTAGENESIS OF 277-GLU-GLU-278 AND
RP LYS-479.
RX PubMed=10207018; DOI=10.1074/jbc.274.17.11968;
RA Imanaka T., Aihara K., Takano T., Yamashita A., Sato R., Suzuki Y.,
RA Yokota S., Osumi T.;
RT "Characterization of the 70-kDa peroxisomal membrane protein, an ATP
RT binding cassette transporter.";
RL J. Biol. Chem. 274:11968-11976(1999).
RN [4]
RP SUBUNIT, AND ATP BINDING.
RX PubMed=11883951; DOI=10.1006/bbrc.2002.6588;
RA Kashiwayama Y., Morita M., Kamijo K., Imanaka T.;
RT "Nucleotide-induced conformational changes of PMP70, an ATP binding
RT cassette transporter on rat liver peroxisomal membranes.";
RL Biochem. Biophys. Res. Commun. 291:1245-1251(2002).
CC -!- FUNCTION: Broad substrate specificity ATP-dependent transporter of the
CC ATP-binding cassette (ABC) family that catalyzes the transport of long-
CC chain fatty acids (LCFA)-CoA, dicarboxylic acids-CoA, long-branched-
CC chain fatty acids-CoA and bile acids from the cytosol to the peroxisome
CC lumen for beta-oxydation. Has fatty acyl-CoA thioesterase and ATPase
CC activities (By similarity). Probably hydrolyzes fatty acyl-CoAs into
CC free fatty acids prior to their ATP-dependent transport into
CC peroxisomes (By similarity). Thus, play a role in regulation of LCFAs
CC and energy metabolism namely, in the degradation and biosynthesis of
CC fatty acids by beta-oxidation (PubMed:10207018).
CC {ECO:0000250|UniProtKB:P28288, ECO:0000250|UniProtKB:P33897,
CC ECO:0000269|PubMed:10207018}.
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:P28288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67073;
CC Evidence={ECO:0000250|UniProtKB:P28288};
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:P28288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67081;
CC Evidence={ECO:0000250|UniProtKB:P28288};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acyl-CoA + H2O = a long-chain fatty acid +
CC CoA + H(+); Xref=Rhea:RHEA:67680, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:83139; Evidence={ECO:0000250|UniProtKB:P28288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67681;
CC Evidence={ECO:0000250|UniProtKB:P28288};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid(in) + ATP + H2O = a long-chain fatty
CC acid(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:67684,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57560, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P28288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67685;
CC Evidence={ECO:0000250|UniProtKB:P28288};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + pristanoyl-CoA = 2,6,10,14-tetramethylpentadecanoate +
CC CoA + H(+); Xref=Rhea:RHEA:40415, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:77250,
CC ChEBI:CHEBI:77268; Evidence={ECO:0000250|UniProtKB:P28288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40416;
CC Evidence={ECO:0000250|UniProtKB:P28288};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,6,10,14-tetramethylpentadecanoate(in) + ATP + H2O =
CC 2,6,10,14-tetramethylpentadecanoate(out) + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:67688, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:77268,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P28288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67689;
CC Evidence={ECO:0000250|UniProtKB:P28288};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanedioyl-CoA = CoA + H(+) + hexadecanedioate;
CC Xref=Rhea:RHEA:67696, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:76276, ChEBI:CHEBI:77085;
CC Evidence={ECO:0000250|UniProtKB:P28288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67697;
CC Evidence={ECO:0000250|UniProtKB:P28288};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + hexadecanedioate(in) = ADP + H(+) +
CC hexadecanedioate(out) + phosphate; Xref=Rhea:RHEA:67692,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:76276, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P28288};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + H2O =
CC (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + CoA + H(+);
CC Xref=Rhea:RHEA:67712, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:58562, ChEBI:CHEBI:73862;
CC Evidence={ECO:0000250|UniProtKB:P28288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67713;
CC Evidence={ECO:0000250|UniProtKB:P28288};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate(in) + ATP + H2O =
CC (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate(out) + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:67708, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58562,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P28288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67709;
CC Evidence={ECO:0000250|UniProtKB:P28288};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + H2O =
CC (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + CoA + H(+);
CC Xref=Rhea:RHEA:67700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:74298, ChEBI:CHEBI:77016;
CC Evidence={ECO:0000250|UniProtKB:P28288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67701;
CC Evidence={ECO:0000250|UniProtKB:P28288};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate(in) + ATP + H2O =
CC (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate(out) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:67704, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:77016, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P28288};
CC -!- SUBUNIT: Homodimers (PubMed:11883951). Can form heterodimers with ABCD1
CC and ABCD2. Dimerization is necessary to form an active transporter.
CC Interacts with PEX19; mediates the targeting of ABCD3 to peroxisomes
CC (By similarity). {ECO:0000250|UniProtKB:P28288,
CC ECO:0000269|PubMed:11883951}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000269|PubMed:10207018}; Multi-pass membrane protein
CC {ECO:0000255}.
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; D90038; BAA14086.1; -; mRNA.
DR PIR; A35723; A35723.
DR RefSeq; NP_036936.1; NM_012804.1.
DR AlphaFoldDB; P16970; -.
DR SMR; P16970; -.
DR BioGRID; 247310; 3.
DR IntAct; P16970; 1.
DR STRING; 10116.ENSRNOP00000016739; -.
DR GlyGen; P16970; 3 sites.
DR iPTMnet; P16970; -.
DR PhosphoSitePlus; P16970; -.
DR jPOST; P16970; -.
DR PaxDb; P16970; -.
DR PRIDE; P16970; -.
DR Ensembl; ENSRNOT00000016739; ENSRNOP00000016739; ENSRNOG00000011929.
DR GeneID; 25270; -.
DR KEGG; rno:25270; -.
DR UCSC; RGD:2007; rat.
DR CTD; 5825; -.
DR RGD; 2007; Abcd3.
DR eggNOG; KOG0060; Eukaryota.
DR GeneTree; ENSGT00950000182955; -.
DR HOGENOM; CLU_007587_5_1_1; -.
DR InParanoid; P16970; -.
DR OMA; FRYGLVH; -.
DR OrthoDB; 309052at2759; -.
DR PhylomeDB; P16970; -.
DR Reactome; R-RNO-1369062; ABC transporters in lipid homeostasis.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR Reactome; R-RNO-9603798; Class I peroxisomal membrane protein import.
DR PRO; PR:P16970; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000011929; Expressed in duodenum and 19 other tissues.
DR Genevisible; P16970; RN.
DR GO; GO:0016021; C:integral component of membrane; NAS:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005782; C:peroxisomal matrix; ISO:RGD.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:HGNC-UCL.
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; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:RGD.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISO:RGD.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0043621; F:protein self-association; IDA:RGD.
DR GO; GO:0015721; P:bile acid and bile salt transport; ISS:UniProtKB.
DR GO; GO:0006699; P:bile acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISO:RGD.
DR GO; GO:0006633; P:fatty acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006869; P:lipid transport; ISO:RGD.
DR GO; GO:0015910; P:long-chain fatty acid import into peroxisome; ISS:UniProtKB.
DR GO; GO:0007031; P:peroxisome organization; ISO:RGD.
DR GO; GO:1903512; P:phytanic acid metabolic process; ISS:UniProtKB.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0042760; P:very long-chain fatty acid catabolic process; ISO:RGD.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; ISO:RGD.
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; IPR005283; FA_transporter.
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 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 Acetylation; ATP-binding; Direct protein sequencing; Glycoprotein;
KW Hydrolase; Membrane; Nucleotide-binding; Peroxisome; Phosphoprotein;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10527525"
FT CHAIN 2..659
FT /note="ATP-binding cassette sub-family D member 3"
FT /id="PRO_0000093311"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 85..372
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 434..659
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 2..61
FT /note="Interaction with PEX19"
FT /evidence="ECO:0000250|UniProtKB:P28288"
FT BINDING 473..480
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 61
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P55096"
FT MOD_RES 260
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P28288"
FT MOD_RES 399
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P28288"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55096"
FT MOD_RES 533
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P55096"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55096"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 277..278
FT /note="EE->DD: Inhibition of palmitic acid beta-oxidation."
FT /evidence="ECO:0000269|PubMed:10207018"
FT MUTAGEN 479
FT /note="K->A: Inhibition of palmitic acid beta-oxidation."
FT /evidence="ECO:0000269|PubMed:10207018"
SQ SEQUENCE 659 AA; 75316 MW; CA567F3DBE80B169 CRC64;
MAAFSKYLTA RNSSLAGAAF LLFCLLHKRR RALGLHGKKS GKPPLQNNEK EGKKERAVVD
KVFLSRLSQI LKIMVPRTFC KETGYLILIA VMLVSRTYCD VWMIQNGTLI ESGIIGRSSK
DFKRYLFNFI AAMPLISLVN NFLKYGLNEL KLCFRVRLTR YLYEEYLQAF TYYKMGNLDN
RIANPDQLLT QDVEKFCNSV VDLYSNLSKP FLDIVLYIFK LTSAIGAQGP ASMMAYLLVS
GLFLTRLRRP IGKMTIMEQK YEGEYRFVNS RLITNSEEIA FYNGNKREKQ TIHSVFRKLV
EHLHNFIFFR FSMGFIDSII AKYIATVVGY LVVSRPFLDL AHPRHLHSTH SELLEDYYQS
GRMLLRMSQA LGRIVLAGRE MTRLAGFTAR ITELMQVLKD LNHGKYERTM VSQQDKGIEG
AQASPLIPGA GEIINADNII KFDHVPLATP NGDILIQDLS FEVRSGANVL ICGPNGCGKS
SLFRVLGELW PLFGGHLTKP ERGKLFYVPQ RPYMTLGTLR DQVIYPDGKE DQKKKGISDQ
VLKGYLDNVQ LGHILEREGG WDSVQDWMDV LSGGEKQRMA MARLFYHKPQ FAILDECTSA
VSVDVEDYIY SHCRKVGITL FTVSHRKSLW KHHEYYLHMD GRGNYEFKKI TEDTVEFGS
