ACSL4_MOUSE
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 03-AUG-2022, entry version 180.
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; Q9QUJ7; -.
DR PRIDE; Q9QUJ7; -.
DR ProteomicsDB; 285658; -. [Q9QUJ7-1]
DR ProteomicsDB; 285659; -. [Q9QUJ7-2]
DR Antibodypedia; 444; 358 antibodies from 37 providers.
DR DNASU; 50790; -.
DR Ensembl; ENSMUST00000033634; ENSMUSP00000033634; ENSMUSG00000031278. [Q9QUJ7-1]
DR Ensembl; ENSMUST00000112903; ENSMUSP00000108524; ENSMUSG00000031278. [Q9QUJ7-2]
DR Ensembl; ENSMUST00000112904; ENSMUSP00000108525; ENSMUSG00000031278. [Q9QUJ7-2]
DR Ensembl; ENSMUST00000112907; ENSMUSP00000108528; ENSMUSG00000031278. [Q9QUJ7-1]
DR GeneID; 50790; -.
DR KEGG; mmu:50790; -.
DR UCSC; uc009ulu.1; mouse. [Q9QUJ7-1]
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; 293865at2759; -.
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; 12 hits in 76 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 288 other tissues.
DR ExpressionAtlas; Q9QUJ7; baseline and differential.
DR Genevisible; Q9QUJ7; MM.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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 Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
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
