ID   ABCD2_MOUSE             Reviewed;         741 AA.
AC   Q61285; A0A0R4J0U5; Q8BQ63; Q8C4B6;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-SEP-2021, sequence version 2.
DT   24-JAN-2024, entry version 175.
DE   RecName: Full=ATP-binding cassette sub-family D member 2;
DE            EC=3.1.2.- {ECO:0000250|UniProtKB:Q9UBJ2};
DE            EC=7.6.2.- {ECO:0000250|UniProtKB:Q9UBJ2};
DE   AltName: Full=Adrenoleukodystrophy-related protein;
GN   Name=Abcd2; Synonyms=Aldr {ECO:0000303|PubMed:8577752};
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 [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC   STRAIN=DBA/2J;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, 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   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, and Liver;
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   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=16223892; DOI=10.1093/hmg/ddi384;
RA   Ferrer I., Kapfhammer J.P., Hindelang C., Kemp S., Troffer-Charlier N.,
RA   Broccoli V., Callyzot N., Mooyer P., Selhorst J., Vreken P., Wanders R.J.,
RA   Mandel J.L., Pujol A.;
RT   "Inactivation of the peroxisomal ABCD2 transporter in the mouse leads to
RT   late-onset ataxia involving mitochondria, Golgi and endoplasmic reticulum
RT   damage.";
RL   Hum. Mol. Genet. 14:3565-3577(2005).
RN   [8]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=18854420; DOI=10.1152/ajpendo.90736.2008;
RA   Fourcade S., Ruiz M., Camps C., Schlueter A., Houten S.M., Mooyer P.A.,
RA   Pampols T., Dacremont G., Wanders R.J., Giros M., Pujol A.;
RT   "A key role for the peroxisomal ABCD2 transporter in fatty acid
RT   homeostasis.";
RL   Am. J. Physiol. 296:E211-E221(2009).
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 (By similarity). Like
CC       ABCD1 seems to have fatty acyl-CoA thioesterase (ACOT) and ATPase
CC       activities, according to this model, VLCFA-CoA as free VLCFA is
CC       transpoted in an ATP-dependent manner into peroxisomes after the
CC       hydrolysis of VLCFA-CoA mediated by the ACOT activity of ABCD2 (By
CC       similarity). Shows overlapping substrate specificities with ABCD1
CC       toward saturated fatty acids (FA) and monounsaturated FA (MUFA) but has
CC       a distinct substrate preference for shorter VLCFA (C22:0) and
CC       polyunsaturated fatty acid (PUFA) such as C22:6-CoA and C24:6-CoA (in
CC       vitro) (By similarity). Thus, may play a role in regulation of VLCFAs
CC       and energy metabolism namely, in the degradation and biosynthesis of
CC       fatty acids by beta-oxidation (PubMed:18854420, PubMed:16223892).
CC       {ECO:0000250|UniProtKB:P33897, ECO:0000250|UniProtKB:Q9UBJ2,
CC       ECO:0000269|PubMed:16223892, ECO:0000269|PubMed:18854420}.
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:Q9UBJ2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67073;
CC         Evidence={ECO:0000250|UniProtKB:Q9UBJ2};
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:Q9UBJ2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67081;
CC         Evidence={ECO:0000250|UniProtKB:Q9UBJ2};
CC   -!- SUBUNIT: Homodimers. Homotetramers. The minimal functional unit is a
CC       homodimer but the major oligomeric form in peroxisomal membrane is a
CC       homotetramer. Forms heterotramers with ABCD1. Forms heterodimers with
CC       ABCD3. In addition to tetramers, some larger molecular assemblies are
CC       also found but represented only a minor fraction. Interacts with PEX19.
CC       {ECO:0000250|UniProtKB:Q9UBJ2}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:8577752};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in brain and adrenals, and
CC       weakly expressed in liver. {ECO:0000269|PubMed:8577752}.
CC   -!- DISRUPTION PHENOTYPE: Deficient mice exhibit a late-onset cerebellar
CC       and sensory ataxia, loss of Purkinje cells, dorsal root ganglia cell
CC       degeneration, axonal degeneration in the spinal cord, and an
CC       accumulation of very long chain fatty acids (C26:0 and C24:0) in dorsal
CC       root ganglia cells, and reduced levels of C22:6omega3 in primary
CC       neurons. {ECO:0000269|PubMed:16223892, ECO:0000269|PubMed:18854420}.
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; Z48670; CAA88589.1; -; mRNA.
DR   EMBL; AK051445; BAC34641.1; -; mRNA.
DR   EMBL; AK082588; BAC38542.1; -; mRNA.
DR   EMBL; AC113102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC019187; AAH19187.1; -; mRNA.
DR   CCDS; CCDS27760.1; -.
DR   RefSeq; NP_036124.2; NM_011994.2.
DR   AlphaFoldDB; Q61285; -.
DR   SMR; Q61285; -.
DR   BioGRID; 205032; 3.
DR   IntAct; Q61285; 4.
DR   STRING; 10090.ENSMUSP00000068940; -.
DR   GlyCosmos; Q61285; 2 sites, No reported glycans.
DR   GlyGen; Q61285; 2 sites.
DR   iPTMnet; Q61285; -.
DR   PhosphoSitePlus; Q61285; -.
DR   SwissPalm; Q61285; -.
DR   MaxQB; Q61285; -.
DR   PaxDb; 10090-ENSMUSP00000068940; -.
DR   ProteomicsDB; 297498; -.
DR   ProteomicsDB; 338909; -.
DR   Pumba; Q61285; -.
DR   Antibodypedia; 42512; 300 antibodies from 31 providers.
DR   DNASU; 26874; -.
DR   Ensembl; ENSMUST00000069511.8; ENSMUSP00000068940.7; ENSMUSG00000055782.10.
DR   GeneID; 26874; -.
DR   KEGG; mmu:26874; -.
DR   UCSC; uc007xhx.1; mouse.
DR   AGR; MGI:1349467; -.
DR   CTD; 225; -.
DR   MGI; MGI:1349467; Abcd2.
DR   VEuPathDB; HostDB:ENSMUSG00000055782; -.
DR   eggNOG; KOG0064; Eukaryota.
DR   GeneTree; ENSGT00950000182955; -.
DR   InParanoid; Q61285; -.
DR   OMA; DIQAGHF; -.
DR   OrthoDB; 7698at2759; -.
DR   PhylomeDB; Q61285; -.
DR   TreeFam; TF105205; -.
DR   BRENDA; 7.6.2.4; 3474.
DR   Reactome; R-MMU-1369062; ABC transporters in lipid homeostasis.
DR   Reactome; R-MMU-9603798; Class I peroxisomal membrane protein import.
DR   BioGRID-ORCS; 26874; 3 hits in 77 CRISPR screens.
DR   ChiTaRS; Abcd2; mouse.
DR   PRO; PR:Q61285; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q61285; Protein.
DR   Bgee; ENSMUSG00000055782; Expressed in white adipose tissue and 195 other cell types or tissues.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0005778; C:peroxisomal membrane; ISO: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; IBA:GO_Central.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISS: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; ISS:UniProtKB.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IMP:UniProtKB.
DR   GO; GO:0015910; P:long-chain fatty acid import into peroxisome; IBA:GO_Central.
DR   GO; GO:0043217; P:myelin maintenance; IMP:UniProtKB.
DR   GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IMP:UniProtKB.
DR   GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; IMP:UniProtKB.
DR   GO; GO:1990535; P:neuron projection maintenance; IMP:UniProtKB.
DR   GO; GO:0007031; P:peroxisome organization; IBA:GO_Central.
DR   GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; IMP:UniProtKB.
DR   GO; GO:2001280; P:positive regulation of unsaturated fatty acid biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR   GO; GO:0042760; P:very long-chain fatty acid catabolic process; IMP:UniProtKB.
DR   GO; GO:0000038; P:very long-chain fatty acid metabolic process; ISS: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.
PE   1: Evidence at protein level;
KW   ATP-binding; Glycoprotein; Hydrolase; Lipid metabolism; Membrane;
KW   Nucleotide-binding; Peroxisome; Phosphoprotein; Reference proteome;
KW   Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..741
FT                   /note="ATP-binding cassette sub-family D member 2"
FT                   /id="PRO_0000093307"
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          479..705
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          1..218
FT                   /note="Interaction with PEX19"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBJ2"
FT   BINDING         512..519
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   MOD_RES         58
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17208939"
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   CONFLICT        296
FT                   /note="H -> R (in Ref. 2; BAC38542)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        737
FT                   /note="A -> P (in Ref. 1; CAA88589 and 4; AAH19187)"
SQ   SEQUENCE   741 AA;  83457 MW;  24B9952F61AB49D9 CRC64;
     MIHMLNAAAY RVKWTRSGAA KRAACLVAAA YALKTLYPII GKRLKQPGHR KAKAEAYSPA
     ENREILHCTE IICKKPAPGL NAAFFKQLLE LRKILFPKLV TTETGWLCLH SVALISRTFL
     SIYVAGLDGK IVKSIVEKKP RTFIIKLIKW LMIAIPATFV NSAIRYLECK LALAFRTRLV
     DHAYETYFAN QTYYKVINMD GRLANPDQSL TEDIMMFSQS VAHLYSNLTK PILDVILTSY
     TLIRTATSRG ASPIGPTLLA GLVVYATAKV LKACSPKFGS LVAEEAHRKG YLRYVHSRII
     ANVEEIAFYR GHKVEMKQLQ KCYKALAYQM NLILSKRLWY IMIEQFLMKY VWSSCGLIMV
     AIPIITATGF ADGDLEDGPK QAMVSDRTEA FTTARNLLAS GADAIERIMS SYKEITELAG
     YTARVYNMFW VFDEVKRGIY KRTVTQEPEN HSKRGGNLEL PLSDTLAIKG TVIDVDHGII
     CENVPIITPA GEVVASRLNF KVEEGMHLLI TGPNGCGKSS LFRILSGLWP VYEGVLYKPP
     PQHMFYIPQR PYMSLGSLRD QVIYPDSADD MREKGYTDQD LERILHSVHL YHIVQREGGW
     DAVMDWKDVL SGGEKQRMGM ARMFYHKPKY ALLDECTSAV SIDVEGKIFQ AAIGAGISLL
     SITHRPSLWK YHTHLLQFDG EGGWRFEQLD TAIRLTLSEE KQKLESQLAG IPKMQQRLNE
     LCKILGEDSV LKTIQTAEKT S
//