ID   ACSL3_PONAB             Reviewed;         720 AA.
AC   Q5R668; Q5R4L4; Q5R9P0;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 2.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=Fatty acid CoA ligase Acsl3 {ECO:0000250|UniProtKB:Q63151};
DE   AltName: Full=Arachidonate--CoA ligase {ECO:0000250|UniProtKB:Q63151};
DE            EC=6.2.1.15 {ECO:0000250|UniProtKB:Q63151};
DE   AltName: Full=Long-chain acyl-CoA synthetase 3;
DE            Short=LACS 3;
DE   AltName: Full=Long-chain-fatty-acid--CoA ligase 3 {ECO:0000250|UniProtKB:O95573};
DE            EC=6.2.1.3 {ECO:0000250|UniProtKB:O95573};
DE   AltName: Full=Medium-chain acyl-CoA ligase Acsl3 {ECO:0000250|UniProtKB:Q63151};
DE            EC=6.2.1.2 {ECO:0000250|UniProtKB:Q63151};
GN   Name=ACSL3 {ECO:0000250|UniProtKB:O95573};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acyl-CoA synthetases (ACSL) activates long-chain fatty acids
CC       for both synthesis of cellular lipids, and degradation via beta-
CC       oxidation (By similarity). ACSL3 is required for the incorporation of
CC       fatty acids into phosphatidylcholine, the major phospholipid located on
CC       the surface of VLDL (very low density lipoproteins) (By similarity).
CC       Has mainly an anabolic role in energy metabolism. Mediates hepatic
CC       lipogenesis. Preferentially uses myristate, laurate, arachidonate and
CC       eicosapentaenoate as substrates. Both isoforms exhibit the same level
CC       of activity (By similarity). {ECO:0000250,
CC       ECO:0000250|UniProtKB:O95573, ECO:0000250|UniProtKB:Q63151}.
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:0000250|UniProtKB:Q63151};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC         Evidence={ECO:0000250|UniProtKB:Q63151};
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:O95573};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36140;
CC         Evidence={ECO:0000250|UniProtKB:O95573};
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:0000250|UniProtKB:Q63151};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714;
CC         Evidence={ECO:0000250|UniProtKB:Q63151};
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:0000250|UniProtKB:Q63151};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52117;
CC         Evidence={ECO:0000250|UniProtKB:Q63151};
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:0000250|UniProtKB:Q63151};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52113;
CC         Evidence={ECO:0000250|UniProtKB:Q63151};
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:0000250|UniProtKB:Q63151};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52109;
CC         Evidence={ECO:0000250|UniProtKB:Q63151};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoate + ATP + CoA = 14,15-
CC         epoxy-(5Z,8Z,11Z)-eicosatrienoyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:52016, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:84024, ChEBI:CHEBI:136117,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52017;
CC         Evidence={ECO:0000250|UniProtKB:Q63151};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=11,12-epoxy-(5Z,8Z,14Z)-eicosatrienoate + ATP + CoA = 11,12-
CC         epoxy-(5Z,8Z,14Z)-eicosatrienoyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:52012, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:76625, ChEBI:CHEBI:136115,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52013;
CC         Evidence={ECO:0000250|UniProtKB:Q63151};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty
CC         acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2;
CC         Evidence={ECO:0000250|UniProtKB:Q63151};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48341;
CC         Evidence={ECO:0000250|UniProtKB:Q63151};
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:Q63151};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC         Evidence={ECO:0000250|UniProtKB:Q63151};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + tetradecanoate = AMP + diphosphate +
CC         tetradecanoyl-CoA; Xref=Rhea:RHEA:33619, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:30807, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57385, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000250|UniProtKB:Q63151};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33620;
CC         Evidence={ECO:0000250|UniProtKB:Q63151};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + dodecanoate = AMP + diphosphate + dodecanoyl-CoA;
CC         Xref=Rhea:RHEA:33623, ChEBI:CHEBI:18262, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33624;
CC         Evidence={ECO:0000250|UniProtKB:Q63151};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + octadecanoate = AMP + diphosphate + octadecanoyl-
CC         CoA; Xref=Rhea:RHEA:33615, ChEBI:CHEBI:25629, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33616;
CC         Evidence={ECO:0000250|UniProtKB:Q63151};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + eicosanoate = AMP + diphosphate + eicosanoyl-CoA;
CC         Xref=Rhea:RHEA:46208, ChEBI:CHEBI:30616, ChEBI:CHEBI:32360,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46209;
CC         Evidence={ECO:0000250|UniProtKB:Q63151};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoate + ATP + CoA = (9Z)-octadecenoyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:33607, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:30823, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57387, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000250|UniProtKB:Q63151};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608;
CC         Evidence={ECO:0000250|UniProtKB:Q63151};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-hexadecenoate + ATP + CoA = (9Z)-hexadecenoyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:33647, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:32372, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:61540, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000250|UniProtKB:Q63151};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33648;
CC         Evidence={ECO:0000250|UniProtKB:Q63151};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z)-octadecadienoate + ATP + CoA = (9Z,12Z)-
CC         octadecadienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:33651,
CC         ChEBI:CHEBI:30245, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000250|UniProtKB:Q63151};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z,15Z)-octadecatrienoate + ATP + CoA = (9Z,12Z,15Z)-
CC         octadecatrienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:44936,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:32387, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:74034, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000250|UniProtKB:Q63151};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44937;
CC         Evidence={ECO:0000250|UniProtKB:Q63151};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + ATP + CoA =
CC         (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:44932, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:74298, ChEBI:CHEBI:77016,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44933;
CC         Evidence={ECO:0000250|UniProtKB:Q63151};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + ATP + CoA =
CC         (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:67848, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:58562, ChEBI:CHEBI:73862,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67849;
CC         Evidence={ECO:0000250|UniProtKB:Q63151};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acid + ATP + CoA = a fatty acyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:38883, ChEBI:CHEBI:28868,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:77636, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000250|UniProtKB:Q63151};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38884;
CC         Evidence={ECO:0000250|UniProtKB:Q63151};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
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}; Single-pass type III membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; CR859345; CAH91520.1; -; mRNA.
DR   EMBL; CR860628; CAH92748.1; -; mRNA.
DR   EMBL; CR861232; CAH93302.1; -; mRNA.
DR   RefSeq; NP_001127581.1; NM_001134109.1.
DR   RefSeq; NP_001128901.1; NM_001135429.1.
DR   AlphaFoldDB; Q5R668; -.
DR   SMR; Q5R668; -.
DR   STRING; 9601.ENSPPYP00000024216; -.
DR   GeneID; 100174659; -.
DR   GeneID; 100189843; -.
DR   KEGG; pon:100174659; -.
DR   CTD; 2181; -.
DR   eggNOG; KOG1180; Eukaryota.
DR   InParanoid; Q5R668; -.
DR   OrthoDB; 443463at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; ISS:UniProtKB.
DR   GO; GO:0031956; F:medium-chain fatty acid-CoA ligase activity; IEA:RHEA.
DR   GO; GO:0001676; P:long-chain fatty acid metabolic process; ISS:UniProtKB.
DR   CDD; cd17639; LC_FACS_euk1; 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   PANTHER; PTHR43272:SF13; FATTY ACID COA LIGASE ACSL3; 1.
DR   PANTHER; PTHR43272; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Endoplasmic reticulum; Fatty acid metabolism; Ligase;
KW   Lipid metabolism; Magnesium; Membrane; Microsome; Mitochondrion;
KW   Mitochondrion outer membrane; Nucleotide-binding; Peroxisome;
KW   Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..720
FT                   /note="Fatty acid CoA ligase Acsl3"
FT                   /id="PRO_0000240276"
FT   TRANSMEM        21..41
FT                   /note="Helical; Signal-anchor for type III membrane
FT                   protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        42..720
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         683
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O95573"
FT   CONFLICT        104
FT                   /note="L -> P (in Ref. 1; CAH91520)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        112
FT                   /note="N -> S (in Ref. 1; CAH93302)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        117
FT                   /note="V -> I (in Ref. 1; CAH93302)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        210
FT                   /note="I -> T (in Ref. 1; CAH91520)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        270
FT                   /note="N -> D (in Ref. 1; CAH93302)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        386
FT                   /note="I -> T (in Ref. 1; CAH92748)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   720 AA;  80445 MW;  C5E83CFBD6904101 CRC64;
     MNNHVSSKPS TMKLKHTINP ILLYFIHFLI SLYTILTYIP FYFFSESRQE KSNRIKAKPV
     NSKPDSAYRS VNSLDGLASV LYPGCDTLDK VFTYAKNKFK NKRLLGTREV LNEEDEVQPN
     GKIFKKVILG QYNWLSYEDV FVRAFNFGNG LQMLGQKPKT NIAIFCETRA EWMIAAQACF
     MYNFQLVTLY ATLGGPAIVH ALNETEVTNI ITSKELLQTK LKDIVSLVPR LRHIITVDGK
     PPTWSEFPKG IIVHTMAAVE ALGAKASMEN QPHSKPLPSD IAVIMYTSGS TGLPKGVMIS
     HSNIIAGITG MAERIPELGE EDVYIGYLPL AHVLELSAEL VCLSHGCRIG YSSPQTLADQ
     SSKIKKGSKG DTSMLKPTLM AAVPEIMDRI YKNVMNKVSE MSSFQRNLFI LAYNYKMEQI
     SKGRNTPLCN SFVFRKVRSL LGGNIRLLLC GGAPLSATTQ RFMNICFCCP VGQGYGLTES
     AGAGTISEVW DYNTGRVGAP LVCCEIKLKN WEEGGYFNTD KPHPRGEILI GGQIVTMGYY
     KNEAKTKADF FEDENGQRWL CTGDIGEFEP DGCLKIIDRK KDLVKLQAGE YVSLGKVEAA
     LKNLPLVDNI CAYANSYHSY VIGFVVPNQK ELTELARKKG LKGTWEELCN SCEMENEVLK
     VLSEAAISAS LEKFEIPVKI RLSPEPWTPE TGLVTDAFKL KRKELKTHYQ ADIERMYGRK
//