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   24-JAN-2024, entry version 184.
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   -!- PTM: Ubiquitinated by PEX2 during pexophagy in response to starvation,
CC       leading to its degradation. {ECO:0000250|UniProtKB:P28288}.
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   GlyCosmos; P16970; 3 sites, No reported glycans.
DR   GlyGen; P16970; 4 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; P16970; -.
DR   PhosphoSitePlus; P16970; -.
DR   jPOST; P16970; -.
DR   PaxDb; 10116-ENSRNOP00000016739; -.
DR   Ensembl; ENSRNOT00000016739.7; ENSRNOP00000016739.5; ENSRNOG00000011929.7.
DR   Ensembl; ENSRNOT00055046119; ENSRNOP00055037846; ENSRNOG00055026677.
DR   Ensembl; ENSRNOT00060004454; ENSRNOP00060003148; ENSRNOG00060002776.
DR   Ensembl; ENSRNOT00065039403; ENSRNOP00065032029; ENSRNOG00065023022.
DR   GeneID; 25270; -.
DR   KEGG; rno:25270; -.
DR   UCSC; RGD:2007; rat.
DR   AGR; RGD:2007; -.
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   OrthoDB; 7698at2759; -.
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 cell types or tissues.
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   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; IPR005283; FA_transporter.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00954; 3a01203; 1.
DR   PANTHER; PTHR11384:SF62; ATP-BINDING CASSETTE SUB-FAMILY D MEMBER 3; 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; P16970; RN.
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; Ubl conjugation.
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
//