ID   ACSL4_MOUSE             Reviewed;         711 AA.
AC   Q9QUJ7; Q5D071; Q9JHT4; Q9R0H3;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   24-JAN-2024, entry version 188.
DE   RecName: Full=Long-chain-fatty-acid--CoA ligase 4;
DE            EC=6.2.1.3 {ECO:0000250|UniProtKB:O35547};
DE   AltName: Full=Arachidonate--CoA ligase {ECO:0000250|UniProtKB:O35547};
DE            EC=6.2.1.15 {ECO:0000250|UniProtKB:O35547};
DE   AltName: Full=Long-chain acyl-CoA synthetase 4;
DE            Short=LACS 4;
DE            Short=mACS4;
GN   Name=Acsl4; Synonyms=Acs4, Facl4;
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] (ISOFORMS LONG AND SHORT).
RX   PubMed=10924347; DOI=10.1006/bbrc.2000.3207;
RA   Cho Y.-Y., Kang M.-J., Ogawa S., Yamashita Y., Fujino T., Yamamoto T.T.;
RT   "Regulation by adrenocorticotropic hormone and arachidonate of the
RT   expression of acyl-CoA synthetase 4, an arachidonate-preferring enzyme
RT   expressed in steroidogenic tissues.";
RL   Biochem. Biophys. Res. Commun. 274:741-745(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RC   TISSUE=Embryo;
RX   PubMed=10828604; DOI=10.1159/000015533;
RA   Vitelli F., Meloni I., Fineschi S., Favara F., Tiziana Storlazzi C.,
RA   Rocchi M., Renieri A.;
RT   "Identification and characterization of mouse orthologs of the AMMECR1 and
RT   FACL4 genes deleted in AMME syndrome: orthology of Xq22.3 and MmuXF1-F3.";
RL   Cytogenet. Cell Genet. 88:259-263(2000).
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] (ISOFORM LONG).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Spleen, and
RC   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).
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. Preferentially activates arachidonate
CC       and eicosapentaenoate as substrates. Preferentially activates 8,9-EET >
CC       14,15-EET > 5,6-EET > 11,12-EET. Modulates glucose-stimulated insulin
CC       secretion by regulating the levels of unesterified EETs (By
CC       similarity). Modulates prostaglandin E2 secretion (By similarity).
CC       {ECO:0000250|UniProtKB:O35547, ECO:0000250|UniProtKB:O60488}.
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:O35547};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC         Evidence={ECO:0000250|UniProtKB:O35547};
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:O35547};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714;
CC         Evidence={ECO:0000250|UniProtKB:O35547};
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:O35547};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52117;
CC         Evidence={ECO:0000250|UniProtKB:O35547};
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:O35547};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52113;
CC         Evidence={ECO:0000250|UniProtKB:O35547};
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:O35547};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52109;
CC         Evidence={ECO:0000250|UniProtKB:O35547};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5,6-epoxy-(8Z,11Z,14Z)-eicosatrienoate + ATP + CoA = 5,6-
CC         epoxy-(8Z,11Z,14Z)-eicosatrienoyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:52088, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:131992, ChEBI:CHEBI:136351,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:O35547};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52089;
CC         Evidence={ECO:0000250|UniProtKB:O35547};
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:O35547};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52017;
CC         Evidence={ECO:0000250|UniProtKB:O35547};
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:O35547};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52013;
CC         Evidence={ECO:0000250|UniProtKB:O35547};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=8,9-epoxy-(5Z,11Z,14Z)-eicosatrienoate + ATP + CoA = 8,9-
CC         epoxy-(5Z,11Z,14Z)-eicosatrienoyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:52008, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:84025, ChEBI:CHEBI:136107,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:O35547};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52009;
CC         Evidence={ECO:0000250|UniProtKB:O35547};
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:O60488};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC         Evidence={ECO:0000250|UniProtKB:O60488};
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:O60488};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36140;
CC         Evidence={ECO:0000250|UniProtKB:O60488};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Both triacsin C and rosiglitazone inhibit
CC       arachidonoyl-CoA ligase activity. {ECO:0000250|UniProtKB:O60488}.
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:O60488}; Single-pass type III membrane protein
CC       {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:O60488}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=Q9QUJ7-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=Q9QUJ7-2; Sequence=VSP_000239;
CC   -!- TISSUE SPECIFICITY: Abundant in steroidogenic tissues, also found in
CC       the kidney, brain and liver.
CC   -!- INDUCTION: Induced by adrenocorticotropic hormone (ACTH) and suppressed
CC       by glucocorticoid.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AB033887; BAA85931.1; -; mRNA.
DR   EMBL; AB033886; BAA85930.1; -; mRNA.
DR   EMBL; AB033885; BAA85929.1; -; mRNA.
DR   EMBL; AJ243502; CAB95965.1; -; mRNA.
DR   EMBL; AL731672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC058663; AAH58663.1; -; mRNA.
DR   CCDS; CCDS30448.1; -. [Q9QUJ7-1]
DR   CCDS; CCDS41156.1; -. [Q9QUJ7-2]
DR   RefSeq; NP_001028772.1; NM_001033600.1. [Q9QUJ7-2]
DR   RefSeq; NP_062350.3; NM_019477.3. [Q9QUJ7-2]
DR   RefSeq; NP_997508.1; NM_207625.2. [Q9QUJ7-1]
DR   RefSeq; XP_011246144.1; XM_011247842.2. [Q9QUJ7-2]
DR   RefSeq; XP_011246145.1; XM_011247843.2. [Q9QUJ7-2]
DR   AlphaFoldDB; Q9QUJ7; -.
DR   SMR; Q9QUJ7; -.
DR   BioGRID; 206122; 5.
DR   IntAct; Q9QUJ7; 1.
DR   STRING; 10090.ENSMUSP00000033634; -.
DR   iPTMnet; Q9QUJ7; -.
DR   PhosphoSitePlus; Q9QUJ7; -.
DR   SwissPalm; Q9QUJ7; -.
DR   EPD; Q9QUJ7; -.
DR   MaxQB; Q9QUJ7; -.
DR   PaxDb; 10090-ENSMUSP00000033634; -.
DR   ProteomicsDB; 285658; -. [Q9QUJ7-1]
DR   ProteomicsDB; 285659; -. [Q9QUJ7-2]
DR   Pumba; Q9QUJ7; -.
DR   Antibodypedia; 444; 409 antibodies from 37 providers.
DR   DNASU; 50790; -.
DR   Ensembl; ENSMUST00000033634.5; ENSMUSP00000033634.5; ENSMUSG00000031278.13. [Q9QUJ7-1]
DR   Ensembl; ENSMUST00000112903.8; ENSMUSP00000108524.2; ENSMUSG00000031278.13. [Q9QUJ7-2]
DR   Ensembl; ENSMUST00000112904.8; ENSMUSP00000108525.2; ENSMUSG00000031278.13. [Q9QUJ7-2]
DR   Ensembl; ENSMUST00000112907.8; ENSMUSP00000108528.2; ENSMUSG00000031278.13. [Q9QUJ7-1]
DR   GeneID; 50790; -.
DR   KEGG; mmu:50790; -.
DR   UCSC; uc009ulu.1; mouse. [Q9QUJ7-1]
DR   AGR; MGI:1354713; -.
DR   CTD; 2182; -.
DR   MGI; MGI:1354713; Acsl4.
DR   VEuPathDB; HostDB:ENSMUSG00000031278; -.
DR   eggNOG; KOG1180; Eukaryota.
DR   GeneTree; ENSGT00940000157427; -.
DR   HOGENOM; CLU_000022_45_2_1; -.
DR   InParanoid; Q9QUJ7; -.
DR   OMA; KIFQWAA; -.
DR   OrthoDB; 443463at2759; -.
DR   PhylomeDB; Q9QUJ7; -.
DR   TreeFam; TF314012; -.
DR   BRENDA; 6.2.1.3; 3474.
DR   Reactome; R-MMU-434313; Intracellular metabolism of fatty acids regulates insulin secretion.
DR   Reactome; R-MMU-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR   BioGRID-ORCS; 50790; 13 hits in 81 CRISPR screens.
DR   ChiTaRS; Acsl4; mouse.
DR   PRO; PR:Q9QUJ7; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q9QUJ7; Protein.
DR   Bgee; ENSMUSG00000031278; Expressed in adrenal gland and 291 other cell types or tissues.
DR   ExpressionAtlas; Q9QUJ7; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005811; C:lipid droplet; ISO:MGI.
DR   GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; ISO:MGI.
DR   GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005777; C:peroxisome; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
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; IDA:MGI.
DR   GO; GO:0031957; F:very long-chain fatty acid-CoA ligase activity; ISO:MGI.
DR   GO; GO:0060996; P:dendritic spine development; ISO:MGI.
DR   GO; GO:0060136; P:embryonic process involved in female pregnancy; IMP:MGI.
DR   GO; GO:0006631; P:fatty acid metabolic process; ISO:MGI.
DR   GO; GO:0015908; P:fatty acid transport; ISO:MGI.
DR   GO; GO:0008610; P:lipid biosynthetic process; ISO:MGI.
DR   GO; GO:0006629; P:lipid metabolic process; ISO:MGI.
DR   GO; GO:0001676; P:long-chain fatty acid metabolic process; ISS:UniProtKB.
DR   GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; ISO:MGI.
DR   GO; GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; IBA:GO_Central.
DR   GO; GO:0032307; P:negative regulation of prostaglandin secretion; ISO:MGI.
DR   GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR   GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR   GO; GO:0032024; P:positive regulation of insulin secretion; ISS:UniProtKB.
DR   GO; GO:0019217; P:regulation of fatty acid metabolic process; TAS:MGI.
DR   GO; GO:0019432; P:triglyceride biosynthetic process; ISO:MGI.
DR   CDD; cd17639; LC_FACS_euk1; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR43272; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR   PANTHER; PTHR43272:SF22; LONG-CHAIN-FATTY-ACID--COA LIGASE 4; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   Genevisible; Q9QUJ7; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell membrane; Endoplasmic reticulum;
KW   Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium; Membrane;
KW   Microsome; Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
KW   Peroxisome; Phosphoprotein; Reference proteome; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..711
FT                   /note="Long-chain-fatty-acid--CoA ligase 4"
FT                   /id="PRO_0000193110"
FT   TRANSMEM        8..28
FT                   /note="Helical; Signal-anchor for type III membrane
FT                   protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..711
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         447
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O60488"
FT   VAR_SEQ         1..41
FT                   /note="Missing (in isoform Short)"
FT                   /evidence="ECO:0000303|PubMed:10828604,
FT                   ECO:0000303|PubMed:10924347"
FT                   /id="VSP_000239"
FT   CONFLICT        288
FT                   /note="V -> L (in Ref. 1; BAA85929/BAA85930/BAA85931)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        293
FT                   /note="S -> T (in Ref. 1; BAA85929/BAA85930/BAA85931)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        430..432
FT                   /note="ALL -> DLV (in Ref. 1; BAA85929/BAA85930/BAA85931)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        441
FT                   /note="S -> Y (in Ref. 1; BAA85929/BAA85930/BAA85931)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        458
FT                   /note="F -> L (in Ref. 1; BAA85929/BAA85930/BAA85931)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        584
FT                   /note="S -> F (in Ref. 1; BAA85929/BAA85930/BAA85931)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        704
FT                   /note="I -> V (in Ref. 1; BAA85929/BAA85930/BAA85931)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   711 AA;  79077 MW;  84ACA29CADDD6A3A CRC64;
     MNLKLNVLTI ILLPVHLLIT IYSALIFIPW YFLTNAKKKN AMAKRIKAKP TSDKPGSPYR
     SVTHFDSLAV IDIPGADTLD KLFDHAVAKF GKKDSLGTRE ILSEENEMQP NGKVFKKLIL
     GNYKWINYLE VNCRVNNFGS GLTALGLKPK NTIAIFCETR AEWMIAAQTC FKYNFPLVTL
     YATLGREAVV HGLNESEASY LITSVELLES KLKAALVDIN CVKHIIYVDN KTINRAEYPE
     GLEIHSMQSV EELGAKPENL SVPPSRPTPS DMAIVMYTSG STGRPKGVMM HHSNLIAGMT
     GQCERIPGLG PKDTYIGYLP LAHVLELTAE ISCFTYGCRI GYSSPLTLSD QSSKIKKGSK
     GDCTVLKPTL MAAVPEIMDR IYKNVMSKVQ EMNYVQKTLF KIGYDYKLEQ IKKGYDAPLC
     NLILFKKVKA LLGGNVRMML SGGAPLSPQT HRFMNVCFCC PIGQGYGLTE SCGAGTVTEV
     TDYTTGRVGA PLICCEIKLK DWQEGGYTVH DKPNPRGEIV IGGQNISMGY FKNEEKTAED
     YCVDENGQRW FCTGDIGEFH PDGCLQIIDR KKDLVKLQAG EYVSLGKVEA ALKNCPLIDN
     ICAFAKSDQS YVISFVVPNQ KKLTLLAQQK GVEGSWVDIC NNPAMEAEIL KEIREAANAM
     KLERFEIPIK VRLSPEPWTP ETGLVTDAFK LKRKELKNHY LKDIERMYGG K
//