ID   ACSL6_RAT               Reviewed;         697 AA.
AC   P33124; Q63835; Q6IU14;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   24-JAN-2024, entry version 163.
DE   RecName: Full=Long-chain-fatty-acid--CoA ligase 6 {ECO:0000305};
DE            EC=6.2.1.3 {ECO:0000269|PubMed:28209804};
DE   AltName: Full=Arachidonate--CoA ligase {ECO:0000305};
DE            EC=6.2.1.15 {ECO:0000269|PubMed:28209804};
DE   AltName: Full=Long-chain acyl-CoA synthetase 6;
DE            Short=LACS 6;
DE   AltName: Full=Long-chain-fatty-acid--CoA ligase, brain isozyme;
GN   Name=Acsl6 {ECO:0000312|RGD:69403}; Synonyms=Acs2, Facl6;
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] (ISOFORM 1).
RC   STRAIN=Wistar; TISSUE=Brain;
RX   PubMed=1569043; DOI=10.1093/oxfordjournals.jbchem.a123737;
RA   Fujino T., Yamamoto T.;
RT   "Cloning and functional expression of a novel long-chain acyl-CoA
RT   synthetase expressed in brain.";
RL   J. Biochem. 111:197-203(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, TISSUE
RP   SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   TISSUE=Brain;
RX   PubMed=15683247; DOI=10.1021/bi047721l;
RA   Van Horn C.G., Caviglia J.M., Li L.O., Wang S., Granger D.A., Coleman R.A.;
RT   "Characterization of recombinant long-chain rat acyl-CoA synthetase
RT   isoforms 3 and 6: identification of a novel variant of isoform 6.";
RL   Biochemistry 44:1635-1642(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-160 (ISOFORM 1).
RC   TISSUE=Spinal ganglion;
RG   Amgen EST program;
RT   "Amgen rat EST program.";
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   RETRACTED PAPER.
RC   TISSUE=Brain;
RX   PubMed=1654331; DOI=10.1016/s0021-9258(19)47411-5;
RA   Yamakawa A., Nishizawa M., Fujiwara K.T., Kawai S., Kawasaki H., Suzuki K.,
RA   Takenawa T.;
RT   "Molecular cloning and sequencing of cDNA encoding the phosphatidylinositol
RT   kinase from rat brain.";
RL   J. Biol. Chem. 266:17580-17583(1991).
RN   [5]
RP   RETRACTION NOTICE OF PUBMED:1654331.
RX   PubMed=1460058; DOI=10.1016/s0021-9258(19)74086-1;
RA   Yamakawa A., Nishizawa M., Fujiwara K.T., Kawai S., Kawasaki H., Suzuki K.,
RA   Takenawa T.;
RL   J. Biol. Chem. 267:25620-25620(1992).
RN   [6]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=8973631; DOI=10.1111/j.1432-1033.1996.0186r.x;
RA   Iijima H., Fujino T., Minekura H., Suzuki H., Kang M.-J., Yamamoto T.T.;
RT   "Biochemical studies of two rat acyl-CoA synthetases, ACS1 and ACS2.";
RL   Eur. J. Biochem. 242:186-190(1996).
RN   [7]
RP   CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=28209804; DOI=10.1194/jlr.m072512;
RA   Klett E.L., Chen S., Yechoor A., Lih F.B., Coleman R.A.;
RT   "Long-chain acyl-CoA synthetase isoforms differ in preferences for
RT   eicosanoid species and long-chain fatty acids.";
RL   J. Lipid Res. 58:884-894(2017).
RN   [8]
RP   ERRATUM OF PUBMED:28209804.
RX   PubMed=29196521; DOI=10.1194/jlr.m072512err;
RA   Klett E.L., Chen S., Yechoor A., Lih F.B., Coleman R.A.;
RL   J. Lipid Res. 58:2365-2365(2017).
CC   -!- FUNCTION: Catalyzes the conversion of long-chain fatty acids to their
CC       active form acyl-CoA for both synthesis of cellular lipids, and
CC       degradation via beta-oxidation (PubMed:28209804). Plays an important
CC       role in fatty acid metabolism in brain and the acyl-CoAs produced may
CC       be utilized exclusively for the synthesis of the brain lipid.
CC       {ECO:0000269|PubMed:28209804}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC         CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC         ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC         Evidence={ECO:0000269|PubMed:28209804};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC         Evidence={ECO:0000305|PubMed:28209804};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA =
CC         (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:19713, ChEBI:CHEBI:30616, ChEBI:CHEBI:32395,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC         ChEBI:CHEBI:456215; EC=6.2.1.15;
CC         Evidence={ECO:0000269|PubMed:28209804};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714;
CC         Evidence={ECO:0000305|PubMed:28209804};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=15-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + ATP + CoA = 15-
CC         hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:52116, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:78832, ChEBI:CHEBI:136409,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:28209804};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52117;
CC         Evidence={ECO:0000305|PubMed:28209804};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=12-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + ATP + CoA = 12-
CC         hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:52112, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:90718, ChEBI:CHEBI:136408,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:28209804};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52113;
CC         Evidence={ECO:0000305|PubMed:28209804};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA = 5-
CC         hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:52108, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:65341, ChEBI:CHEBI:136407,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:28209804};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52109;
CC         Evidence={ECO:0000305|PubMed:28209804};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-
CC         CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q9UKU0};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC         Evidence={ECO:0000250|UniProtKB:Q9UKU0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-hexadec-2-enoate + ATP + CoA = (2E)-hexadecenoyl-CoA + AMP
CC         + diphosphate; Xref=Rhea:RHEA:36139, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61526,
CC         ChEBI:CHEBI:72745, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000250|UniProtKB:Q9UKU0};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36140;
CC         Evidence={ECO:0000250|UniProtKB:Q9UKU0};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=12210 uM for ATP (Isoform 1) {ECO:0000269|PubMed:15683247};
CC         KM=4.7 uM for CoA (Isoform 1) {ECO:0000269|PubMed:15683247};
CC         KM=6 uM for palmitate (Isoform 1) {ECO:0000269|PubMed:15683247};
CC         KM=3 uM for oleate (Isoform 1) {ECO:0000269|PubMed:15683247};
CC         KM=9.7 uM for arachidonate (Isoform 1) {ECO:0000269|PubMed:15683247};
CC         KM=1480 uM for ATP (Isoform 2) {ECO:0000269|PubMed:15683247};
CC         KM=2.4 uM for CoA (Isoform 2) {ECO:0000269|PubMed:15683247};
CC         KM=3.6 uM for palmitate (Isoform 2) {ECO:0000269|PubMed:15683247};
CC         KM=5.3 uM for oleate (Isoform 2) {ECO:0000269|PubMed:15683247};
CC         KM=6.5 uM for arachidonate (Isoform 2) {ECO:0000269|PubMed:15683247};
CC         KM=3 uM for palmitate (when expreesed in bacteria)
CC         {ECO:0000269|PubMed:28209804};
CC         KM=4.4 uM for stearate (when expreesed in bacteria)
CC         {ECO:0000269|PubMed:28209804};
CC         KM=4.4 uM for oleate (when expreesed in bacteria)
CC         {ECO:0000269|PubMed:28209804};
CC         KM=6 uM for linoleate (when expreesed in bacteria)
CC         {ECO:0000269|PubMed:28209804};
CC         KM=2.9 uM for arachidonate (when expreesed in bacteria)
CC         {ECO:0000269|PubMed:28209804};
CC         Vmax=208 nmol/min/mg enzyme with palmitate as substrate (Isoform 1)
CC         {ECO:0000269|PubMed:15683247};
CC         Vmax=153 nmol/min/mg enzyme with oleate as substrate (Isoform 1)
CC         {ECO:0000269|PubMed:15683247};
CC         Vmax=139 nmol/min/mg enzyme with arachidonate as substrate (Isoform
CC         1) {ECO:0000269|PubMed:15683247};
CC         Vmax=739 nmol/min/mg enzyme with palmitate as substrate (Isoform 2)
CC         {ECO:0000269|PubMed:15683247};
CC         Vmax=1088 nmol/min/mg enzyme with oleate as substrate (Isoform 2)
CC         {ECO:0000269|PubMed:15683247};
CC         Vmax=1212 nmol/min/mg enzyme with arachidonate as substrate (Isoform
CC         2) {ECO:0000269|PubMed:15683247};
CC         Vmax=3993 nmol/min/mg enzyme with palmitate as substrate (when
CC         expreesed in bacteria) {ECO:0000269|PubMed:28209804};
CC         Vmax=1727 nmol/min/mg enzyme with stearate as substrate (when
CC         expreesed in bacteria) {ECO:0000269|PubMed:28209804};
CC         Vmax=2238 nmol/min/mg enzyme with oleate as substrate (when expreesed
CC         in bacteria) {ECO:0000269|PubMed:28209804};
CC         Vmax=1763 nmol/min/mg enzyme with linoleate as substrate (when
CC         expreesed in bacteria) {ECO:0000269|PubMed:28209804};
CC         Vmax=1682 nmol/min/mg enzyme with arachidonate as substrate (when
CC         expreesed in bacteria) {ECO:0000269|PubMed:28209804};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC       Single-pass type III membrane protein {ECO:0000250}. Peroxisome
CC       membrane {ECO:0000250}; Single-pass type III membrane protein
CC       {ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass type III
CC       membrane protein {ECO:0000250}. Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9UKU0}; Single-pass type III membrane protein
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=ACSL6_vs1;
CC         IsoId=P33124-1; Sequence=Displayed;
CC       Name=2; Synonyms=ACSL6_vs2;
CC         IsoId=P33124-2; Sequence=VSP_057107, VSP_057108;
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in brain and, to a much
CC       lesser extent, in heart and adrenal.
CC   -!- DEVELOPMENTAL STAGE: Isoform 1 is detected 10 days after birth, and
CC       increased in a coordinate fashion during the development of brain, and
CC       the amount did not decrease when myelination was completed.
CC       {ECO:0000269|PubMed:8973631}.
CC   -!- MISCELLANEOUS: 5 rat isozymes encoded by different genes have been
CC       described. ACSL6 corresponds to isozyme 2 (ACS2).
CC       {ECO:0000303|PubMed:15683247}.
CC   -!- MISCELLANEOUS: [Isoform 1]: Contains exon 14.
CC   -!- MISCELLANEOUS: [Isoform 2]: Contains exon 13. No differences in the
CC       affinity for fatty acids and CoA. Decreased affinity for ATP. Could
CC       play an important role at lower ATP levels. Expressed at lower level in
CC       the brain compared to isoform 1. {ECO:0000269|PubMed:15683247}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; S56508; AAB19809.2; -; mRNA.
DR   EMBL; D10041; BAA00932.1; -; mRNA.
DR   EMBL; CB582512; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AY625254; AAT41589.1; -; mRNA.
DR   PIR; JX0205; JX0205.
DR   RefSeq; NP_570095.1; NM_130739.1. [P33124-1]
DR   RefSeq; XP_006246285.1; XM_006246223.3. [P33124-2]
DR   RefSeq; XP_006246286.1; XM_006246224.3. [P33124-2]
DR   AlphaFoldDB; P33124; -.
DR   SMR; P33124; -.
DR   STRING; 10116.ENSRNOP00000055608; -.
DR   SwissLipids; SLP:000001686; -.
DR   iPTMnet; P33124; -.
DR   PhosphoSitePlus; P33124; -.
DR   SwissPalm; P33124; -.
DR   jPOST; P33124; -.
DR   PaxDb; 10116-ENSRNOP00000055608; -.
DR   Ensembl; ENSRNOT00000030760.5; ENSRNOP00000033248.5; ENSRNOG00000026745.8. [P33124-2]
DR   GeneID; 117243; -.
DR   KEGG; rno:117243; -.
DR   UCSC; RGD:69403; rat. [P33124-1]
DR   AGR; RGD:69403; -.
DR   CTD; 23305; -.
DR   RGD; 69403; Acsl6.
DR   VEuPathDB; HostDB:ENSRNOG00000026745; -.
DR   eggNOG; KOG1256; Eukaryota.
DR   GeneTree; ENSGT00940000162308; -.
DR   InParanoid; P33124; -.
DR   OrthoDB; 443463at2759; -.
DR   PhylomeDB; P33124; -.
DR   BRENDA; 6.2.1.3; 5301.
DR   Reactome; R-RNO-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR   SABIO-RK; P33124; -.
DR   PRO; PR:P33124; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000026745; Expressed in frontal cortex and 12 other cell types or tissues.
DR   ExpressionAtlas; P33124; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0047676; F:arachidonate-CoA ligase activity; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR   GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
DR   GO; GO:0015908; P:fatty acid transport; IGI:RGD.
DR   GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:UniProtKB.
DR   GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; IGI:RGD.
DR   GO; GO:0007405; P:neuroblast proliferation; ISO:RGD.
DR   GO; GO:0048666; P:neuron development; IEP:RGD.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IMP:RGD.
DR   GO; GO:0010747; P:positive regulation of long-chain fatty acid import across plasma membrane; IMP:RGD.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
DR   GO; GO:0009629; P:response to gravity; IEP:RGD.
DR   GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR   GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR   GO; GO:0048545; P:response to steroid hormone; IEP:RGD.
DR   GO; GO:0019432; P:triglyceride biosynthetic process; IGI:RGD.
DR   GO; GO:0000038; P:very long-chain fatty acid metabolic process; IBA:GO_Central.
DR   CDD; cd05927; LC-FACS_euk; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR045311; LC-FACS_euk.
DR   PANTHER; PTHR43272; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR   PANTHER; PTHR43272:SF54; LONG-CHAIN-FATTY-ACID--COA LIGASE 6; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   Genevisible; P33124; RN.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Endoplasmic reticulum;
KW   Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium; Membrane;
KW   Microsome; Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
KW   Peroxisome; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..697
FT                   /note="Long-chain-fatty-acid--CoA ligase 6"
FT                   /id="PRO_0000193117"
FT   TRANSMEM        25..45
FT                   /note="Helical; Signal-anchor for type III membrane
FT                   protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        46..697
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         306..319
FT                   /note="SQWAPTCADVHFSY -> KVIFPRQDDVLISF (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15683247"
FT                   /id="VSP_057107"
FT   VAR_SEQ         329..330
FT                   /note="MV -> VI (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15683247"
FT                   /id="VSP_057108"
SQ   SEQUENCE   697 AA;  78180 MW;  0B0CA7EFD653E2BE CRC64;
     MQTQEILRIL RLPELSDLGQ FFRSLSATTL VSMGALAAIL AYWLTHRPKA LQPPCNLLMQ
     SEEVEDSGGA RRSVIGDCTQ LLTHYYDDAR TMYQVFRRGL SISGNGPCLG FRKPEQPYQW
     LSYQEVAKRA EFLGSGLLQH DCKVGTEQFI GVFAQNRPEW IIAELACYTY SMVVVPLYDT
     LGPGSIRYII NTADICTVIV DKPHKAILLL EHVERKETPG LKLVILMEPF DDALRERGKK
     CGVDIKSMQA IEDSGQENHR VPVPPRPDDL SIVCFTSGTT GNPKGAMLTH GNVVADFSGF
     LKVTESQWAP TCADVHFSYL PLAHMFERMV QSVVYCHGGR VGFFQGDIRL LSDDMKALRP
     TIFPVVPRLL NRMYDKIFHQ ADTSLKRWLL EFAAKRKQAE VRSGIIRNNS IWDELFFNKI
     QASLGGHVRM IVTGAAPASP TVLGFLRAAL GCQVYEGYGQ TECTAGCTFT TPGDWTSGHV
     GAPLPCNHIK LVDAEELNYW TSKGEGEICV KGPNVFKGYL KDEDRTKEAL DSDGWLHTGD
     IGKWLPEGTL KIIDRKKHIF KLAQGEYVAP EKIENIYIRS EPVAQIYVHG DSLKAFLVGI
     VVPDPEVMPC WAQKKGIEGN YQELCKSKEL KKAILDDMVM LGKESGLHSF EQVKAIYIHC
     DMFSVQNGLL TPTLKAKRPE LREYFKKQIE ELYSISM
//