ABCD3_MOUSE
ID ABCD3_MOUSE Reviewed; 659 AA.
AC P55096;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 180.
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=68 kDa peroxisomal membrane protein;
DE Short=PMP68;
DE AltName: Full=70 kDa peroxisomal membrane protein;
DE Short=PMP70;
GN Name=Abcd3; Synonyms=Pmp70, Pxmp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Swiss Webster; TISSUE=Liver;
RX PubMed=7551822; DOI=10.1006/bmme.1995.1027;
RA Bryant D.D., Wilson G.N.;
RT "Differential evolution and expression of murine peroxisomal membrane
RT protein genes.";
RL Biochem. Mol. Med. 55:22-30(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 271-647.
RC TISSUE=Liver;
RX PubMed=7544098; DOI=10.1006/abbi.1995.1426;
RA Chen N., Lu Z., Land M., Ayres R., Crane D.I.;
RT "Peroxisomal membrane protein PMP68 of mouse liver: cloning of a cDNA
RT encompassing the nucleotide binding fold and epitope mapping of monoclonal
RT antibodies to the expressed protein.";
RL Arch. Biochem. Biophys. 321:526-530(1995).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT MS/MS/MS.";
RL Mol. Cell. Proteomics 6:669-676(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-659, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-61; LYS-260; LYS-399 AND LYS-533,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [8]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=25168382; DOI=10.1093/hmg/ddu448;
RA Ferdinandusse S., Jimenez-Sanchez G., Koster J., Denis S.,
RA Van Roermund C.W., Silva-Zolezzi I., Moser A.B., Visser W.F., Gulluoglu M.,
RA Durmaz O., Demirkol M., Waterham H.R., Goekcay G., Wanders R.J., Valle D.;
RT "A novel bile acid biosynthesis defect due to a deficiency of peroxisomal
RT ABCD3.";
RL Hum. Mol. Genet. 24:361-370(2015).
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:25168382).
CC {ECO:0000250|UniProtKB:P28288, ECO:0000250|UniProtKB:P33897,
CC ECO:0000269|PubMed:25168382}.
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. Can form heterodimers with ABCD1 and ABCD2.
CC Dimerization is necessary to form an active transporter. Interacts with
CC PEX19; mediates the targeting of ABCD3 to peroxisomes.
CC {ECO:0000250|UniProtKB:P28288}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000250|UniProtKB:P28288}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Animals show normal activity and have no obvious
CC malformations. However, necroscopy show increased liver size compared
CC to controls, and fibroblasts show reduced numbers of enlarged
CC peroxisomes. They show however a defect in bile acid biosynthesis and
CC they have impaired beta-oxidation of the branched-chain pristanic and
CC phytanic fatty acids on a phytol-loaded diet.
CC {ECO:0000269|PubMed:25168382}.
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 ---------------------------------------------------------------------------
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; L28836; AAA39958.1; -; Genomic_DNA.
DR EMBL; AC129311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X89569; CAA61748.1; -; mRNA.
DR CCDS; CCDS17806.1; -.
DR PIR; I48716; S58009.
DR RefSeq; NP_033017.2; NM_008991.2.
DR AlphaFoldDB; P55096; -.
DR SMR; P55096; -.
DR BioGRID; 202521; 11.
DR IntAct; P55096; 3.
DR STRING; 10090.ENSMUSP00000029770; -.
DR GlyGen; P55096; 3 sites.
DR iPTMnet; P55096; -.
DR PhosphoSitePlus; P55096; -.
DR SwissPalm; P55096; -.
DR EPD; P55096; -.
DR jPOST; P55096; -.
DR MaxQB; P55096; -.
DR PaxDb; P55096; -.
DR PeptideAtlas; P55096; -.
DR PRIDE; P55096; -.
DR ProteomicsDB; 297499; -.
DR Antibodypedia; 33667; 219 antibodies from 35 providers.
DR DNASU; 19299; -.
DR Ensembl; ENSMUST00000029770; ENSMUSP00000029770; ENSMUSG00000028127.
DR GeneID; 19299; -.
DR KEGG; mmu:19299; -.
DR UCSC; uc008reg.1; mouse.
DR CTD; 5825; -.
DR MGI; MGI:1349216; Abcd3.
DR VEuPathDB; HostDB:ENSMUSG00000028127; -.
DR eggNOG; KOG0060; Eukaryota.
DR GeneTree; ENSGT00950000182955; -.
DR InParanoid; P55096; -.
DR OMA; FRYGLVH; -.
DR OrthoDB; 309052at2759; -.
DR PhylomeDB; P55096; -.
DR TreeFam; TF105205; -.
DR Reactome; R-MMU-1369062; ABC transporters in lipid homeostasis.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9603798; Class I peroxisomal membrane protein import.
DR BioGRID-ORCS; 19299; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Abcd3; mouse.
DR PRO; PR:P55096; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P55096; protein.
DR Bgee; ENSMUSG00000028127; Expressed in epithelium of stomach and 253 other tissues.
DR ExpressionAtlas; P55096; baseline and differential.
DR Genevisible; P55096; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005782; C:peroxisomal matrix; ISO:MGI.
DR GO; GO:0005778; C:peroxisomal membrane; IDA:MGI.
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; ISS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISO:MGI.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0043621; F:protein self-association; ISO:MGI.
DR GO; GO:0015721; P:bile acid and bile salt transport; IMP:UniProtKB.
DR GO; GO:0006699; P:bile acid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISO:MGI.
DR GO; GO:0006633; P:fatty acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006869; P:lipid transport; IMP:UniProtKB.
DR GO; GO:0015910; P:long-chain fatty acid import into peroxisome; ISS:UniProtKB.
DR GO; GO:0007031; P:peroxisome organization; ISO:MGI.
DR GO; GO:1903512; P:phytanic acid metabolic process; IMP:UniProtKB.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0042760; P:very long-chain fatty acid catabolic process; ISO:MGI.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; ISO:MGI.
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; Glycoprotein; Hydrolase; Membrane;
KW Nucleotide-binding; Peroxisome; Phosphoprotein; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..659
FT /note="ATP-binding cassette sub-family D member 3"
FT /id="PRO_0000093310"
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 1..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:0007744|PubMed:23576753"
FT MOD_RES 260
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 399
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17208939"
FT MOD_RES 533
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
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 CONFLICT 415
FT /note="E -> G (in Ref. 1; AAA39958)"
FT /evidence="ECO:0000305"
FT CONFLICT 467..468
FT /note="AN -> NH (in Ref. 1; AAA39958)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="C -> R (in Ref. 1; AAA39958)"
FT /evidence="ECO:0000305"
FT CONFLICT 626
FT /note="R -> T (in Ref. 1; AAA39958)"
FT /evidence="ECO:0000305"
FT CONFLICT 628
FT /note="S -> C (in Ref. 1; AAA39958)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 659 AA; 75475 MW; 6DF924D91B481DC4 CRC64;
MAAFSKYLTA RNTSLAGAAF LLLCLLHKRR RALGLHGKKS GKPPLQNNEK EGKKERAVVD
KVFLSRLSQI LKIMVPRTFC KETGYLLLIA VMLVSRTYCD VWMIQNGTLI ESGIIGRSSK
DFKRYLFNFI AAMPLISLVN NFLKYGLNEL KLCFRVRLTR YLYEEYLQAF TYYKMGNLDN
RIANPDQLLT QDVEKFCNSV VDLYSNLSKP FLDIVLYIFK LTSAIGAQGP ASMMAYLLVS
GLFLTRLRRP IGKMTIMEQK YEGEYRYVNS RLITNSEEIA FYNGNKREKQ TIHSVFRKLV
EHLHNFIFFR FSMGFIDSII AKYVATVVGY LVVSRPFLDL AHPRHLHSTH SELLEDYYQS
GRMLLRMSQA LGRIVLAGRE MTRLAGFTAR ITELMQVLKD LNHGRYERTM VSQQEKGIEG
AQASPLVPGA GEIINTDNII KFDHVPLATP NGDILIQDLS FEVRSGANVL ICGPNGCGKS
SLFRVLGELW PLFGGRLTKP ERGKLFYVPQ RPYMTLGTLR DQVIYPDGKE DQKKRGISDQ
VLKEYLDNVQ LGHILEREGG WDSVQDWMDV LSGGEKQRMA MARLFYHKPQ FAILDECTSA
VSVDVEDYIY SHCRKVGITL FTVSHRKSLW KHHEYYLHMD GRGNYEFKKI TEDTVEFGS
