S27A5_MOUSE
ID S27A5_MOUSE Reviewed; 689 AA.
AC Q4LDG0; A6H6C1; O88694; Q91VD5;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Long-chain fatty acid transport protein 5 {ECO:0000305};
DE Short=FATP-5 {ECO:0000303|PubMed:16618416, ECO:0000303|PubMed:16618417};
DE Short=Fatty acid transport protein 5 {ECO:0000303|PubMed:16618416, ECO:0000303|PubMed:16618417};
DE AltName: Full=Bile acid-CoA ligase {ECO:0000303|PubMed:16618417};
DE Short=BA-CoA ligase {ECO:0000303|PubMed:16618417};
DE Short=BAL {ECO:0000303|PubMed:16618417};
DE AltName: Full=Bile acyl-CoA synthetase {ECO:0000250|UniProtKB:Q9Y2P5};
DE Short=BACS {ECO:0000250|UniProtKB:Q9Y2P5};
DE EC=6.2.1.7 {ECO:0000269|PubMed:16618417};
DE AltName: Full=Cholate--CoA ligase {ECO:0000303|PubMed:16618417};
DE AltName: Full=Long-chain-fatty-acid--CoA ligase;
DE EC=6.2.1.3 {ECO:0000250|UniProtKB:Q9Y2P5};
DE AltName: Full=Solute carrier family 27 member 5;
DE AltName: Full=Very long-chain acyl-CoA synthetase-related protein {ECO:0000303|PubMed:9642112};
DE Short=VLACS-related {ECO:0000303|PubMed:9642112};
DE Short=VLACSR {ECO:0000303|PubMed:9642112};
DE EC=6.2.1.- {ECO:0000250|UniProtKB:Q9Y2P5};
GN Name=Slc27a5; Synonyms=Acsb, Acsvl6, Fatp5, Vlacsr;
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], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=9642112; DOI=10.1006/bbrc.1998.8770;
RA Berger J., Truppe C., Neumann H., Forss-Petter S.;
RT "A novel relative of the very-long-chain acyl-CoA synthetase and fatty acid
RT transporter protein genes with a distinct expression pattern.";
RL Biochem. Biophys. Res. Commun. 247:255-260(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Brain, and Salivary gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 28-689.
RX PubMed=9671728; DOI=10.1073/pnas.95.15.8625;
RA Hirsch D., Stahl A., Lodish H.F.;
RT "A family of fatty acid transporters conserved from mycobacterium to man.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8625-8629(1998).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=11980911; DOI=10.1074/jbc.m203295200;
RA Mihalik S.J., Steinberg S.J., Pei Z., Park J., Kim do G., Heinzer A.K.,
RA Dacremont G., Wanders R.J., Cuebas D.A., Smith K.D., Watkins P.A.;
RT "Participation of two members of the very long-chain acyl-CoA synthetase
RT family in bile acid synthesis and recycling.";
RL J. Biol. Chem. 277:24771-24779(2002).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [6]
RP FUNCTION, TRANSPORT ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=16618416; DOI=10.1053/j.gastro.2006.02.006;
RA Doege H., Baillie R.A., Ortegon A.M., Tsang B., Wu Q., Punreddy S.,
RA Hirsch D., Watson N., Gimeno R.E., Stahl A.;
RT "Targeted deletion of FATP5 reveals multiple functions in liver metabolism:
RT alterations in hepatic lipid homeostasis.";
RL Gastroenterology 130:1245-1258(2006).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16618417; DOI=10.1053/j.gastro.2006.02.012;
RA Hubbard B., Doege H., Punreddy S., Wu H., Huang X., Kaushik V.K.,
RA Mozell R.L., Byrnes J.J., Stricker-Krongrad A., Chou C.J., Tartaglia L.A.,
RA Lodish H.F., Stahl A., Gimeno R.E.;
RT "Mice deleted for fatty acid transport protein 5 have defective bile acid
RT conjugation and are protected from obesity.";
RL Gastroenterology 130:1259-1269(2006).
CC -!- FUNCTION: Mediates the import of long-chain fatty acids (LCFA) by
CC facilitating their transport across cell membranes (PubMed:16618416).
CC Also catalyzes the ATP-dependent formation of fatty acyl-CoA using LCFA
CC and very-long-chain fatty acids (VLCFA) as substrates (By similarity).
CC Mainly functions as a bile acyl-CoA synthetase catalyzing the
CC activation of bile acids via ATP-dependent formation of bile acid CoA
CC thioesters which is necessary for their subsequent conjugation with
CC glycine or taurine (PubMed:16618417). Both primary bile acids (cholic
CC acid and chenodeoxycholic acid) and secondary bile acids (deoxycholic
CC acid and lithocholic acid) are the principal substrates (By
CC similarity). In vitro, activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-
CC beta-cholestanate ((25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-
CC cholestan-26-oate or THCA), the C27 precursor of cholic acid deriving
CC from the de novo synthesis from cholesterol (By similarity). Plays an
CC important role in hepatic fatty acid uptake and bile acid reconjugation
CC and recycling but not in de novo synthesis of bile acids
CC (PubMed:16618416, PubMed:16618417). {ECO:0000250|UniProtKB:Q9Y2P5,
CC ECO:0000269|PubMed:16618416, ECO:0000269|PubMed:16618417}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acid(in) = a fatty acid(out); Xref=Rhea:RHEA:38879,
CC ChEBI:CHEBI:28868; Evidence={ECO:0000269|PubMed:16618416};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cholate + CoA = AMP + choloyl-CoA + diphosphate;
CC Xref=Rhea:RHEA:23532, ChEBI:CHEBI:29747, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57373,
CC ChEBI:CHEBI:456215; EC=6.2.1.7;
CC Evidence={ECO:0000269|PubMed:16618417};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23533;
CC Evidence={ECO:0000305|PubMed:16618417};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate
CC + ATP + CoA = (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-
CC 26-oyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:22976,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58677, ChEBI:CHEBI:58734, ChEBI:CHEBI:456215; EC=6.2.1.7;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2P5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22977;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2P5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + chenodeoxycholate + CoA = AMP + chenodeoxycholoyl-CoA +
CC diphosphate; Xref=Rhea:RHEA:43764, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:36234, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:62989, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2P5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43765;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2P5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + deoxycholate = AMP + deoxycholoyl-CoA +
CC diphosphate; Xref=Rhea:RHEA:47128, ChEBI:CHEBI:23614,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58810, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2P5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47129;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2P5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + lithocholate = AMP + diphosphate + lithocholoyl-
CC CoA; Xref=Rhea:RHEA:47136, ChEBI:CHEBI:29744, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:87438,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q9Y2P5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47137;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2P5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very long-chain fatty acid + ATP + CoA = a very long-chain
CC fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:54536,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58950, ChEBI:CHEBI:138261, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2P5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54537;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2P5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + tetracosanoate = AMP + diphosphate +
CC tetracosanoyl-CoA; Xref=Rhea:RHEA:33639, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:31014, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:65052, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2P5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33640;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2P5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + hexacosanoate = AMP + diphosphate + hexacosanoyl-
CC CoA; Xref=Rhea:RHEA:43748, ChEBI:CHEBI:30616, ChEBI:CHEBI:31013,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:64868,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q9Y2P5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43749;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2P5};
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:Q9Y2P5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2P5};
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:Q9Y2P5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33616;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2P5};
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:Q9Y2P5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46209;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2P5};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9Y2P5}; Multi-pass membrane protein
CC {ECO:0000255}. Microsome {ECO:0000250|UniProtKB:Q9ES38}. Cell membrane
CC {ECO:0000269|PubMed:16618416}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Liver-specific (at protein level) (PubMed:16618416,
CC PubMed:9642112). In liver expressed in a periportal distribution
CC (PubMed:11980911). {ECO:0000269|PubMed:11980911,
CC ECO:0000269|PubMed:16618416, ECO:0000269|PubMed:9642112}.
CC -!- DISRUPTION PHENOTYPE: Mice exhibit a severe bile acid conjugation
CC defect (PubMed:16618417). Display a significant reduction in both liver
CC lipid uptake and content and show a redistribution of lipids away from
CC the liver to other tissues (PubMed:16618416). Hepatocytes show
CC significantly reduced long-chain fatty acids (LCFA) uptake
CC (PubMed:16618416). {ECO:0000269|PubMed:16618416,
CC ECO:0000269|PubMed:16618417}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AJ223959; CAA11688.1; -; mRNA.
DR EMBL; BC013335; AAH13335.1; -; mRNA.
DR EMBL; BC013272; AAH13272.1; -; mRNA.
DR EMBL; BC145823; AAI45824.1; -; mRNA.
DR EMBL; BC145825; AAI45826.1; -; mRNA.
DR EMBL; AF072760; AAC40189.1; -; mRNA.
DR CCDS; CCDS20821.1; -.
DR PIR; JW0107; JW0107.
DR RefSeq; NP_033538.2; NM_009512.2.
DR AlphaFoldDB; Q4LDG0; -.
DR SMR; Q4LDG0; -.
DR STRING; 10090.ENSMUSP00000032539; -.
DR TCDB; 4.C.1.1.8; the fatty acid group translocation (fat) family.
DR iPTMnet; Q4LDG0; -.
DR PhosphoSitePlus; Q4LDG0; -.
DR SwissPalm; Q4LDG0; -.
DR jPOST; Q4LDG0; -.
DR MaxQB; Q4LDG0; -.
DR PaxDb; Q4LDG0; -.
DR PeptideAtlas; Q4LDG0; -.
DR PRIDE; Q4LDG0; -.
DR ProteomicsDB; 260900; -.
DR Antibodypedia; 1943; 310 antibodies from 26 providers.
DR DNASU; 26459; -.
DR Ensembl; ENSMUST00000032539; ENSMUSP00000032539; ENSMUSG00000030382.
DR GeneID; 26459; -.
DR KEGG; mmu:26459; -.
DR UCSC; uc009fey.3; mouse.
DR CTD; 10998; -.
DR MGI; MGI:1347100; Slc27a5.
DR VEuPathDB; HostDB:ENSMUSG00000030382; -.
DR eggNOG; KOG1179; Eukaryota.
DR GeneTree; ENSGT00940000157947; -.
DR HOGENOM; CLU_000022_46_2_1; -.
DR InParanoid; Q4LDG0; -.
DR OMA; GATFFTY; -.
DR OrthoDB; 298283at2759; -.
DR PhylomeDB; Q4LDG0; -.
DR TreeFam; TF313430; -.
DR Reactome; R-MMU-159418; Recycling of bile acids and salts.
DR Reactome; R-MMU-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-MMU-193775; Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
DR BioGRID-ORCS; 26459; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Slc27a5; mouse.
DR PRO; PR:Q4LDG0; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q4LDG0; protein.
DR Bgee; ENSMUSG00000030382; Expressed in left lobe of liver and 34 other tissues.
DR ExpressionAtlas; Q4LDG0; baseline and differential.
DR Genevisible; Q4LDG0; MM.
DR GO; GO:0009925; C:basal plasma membrane; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047747; F:cholate-CoA ligase activity; IMP:UniProtKB.
DR GO; GO:0015245; F:fatty acid transmembrane transporter activity; IDA:MGI.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; ISO:MGI.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0031957; F:very long-chain fatty acid-CoA ligase activity; ISO:MGI.
DR GO; GO:0006699; P:bile acid biosynthetic process; ISO:MGI.
DR GO; GO:0008206; P:bile acid metabolic process; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0015908; P:fatty acid transport; IDA:MGI.
DR GO; GO:0046951; P:ketone body biosynthetic process; IMP:MGI.
DR GO; GO:0015911; P:long-chain fatty acid import across plasma membrane; IMP:MGI.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; TAS:MGI.
DR GO; GO:0006642; P:triglyceride mobilization; IMP:MGI.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; ISO:MGI.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
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 InterPro; IPR030302; FATP5.
DR PANTHER; PTHR43107:SF4; PTHR43107:SF4; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Endoplasmic reticulum; Fatty acid metabolism;
KW Ligase; Lipid metabolism; Lipid transport; Membrane; Microsome;
KW Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..689
FT /note="Long-chain fatty acid transport protein 5"
FT /id="PRO_0000193214"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2P5"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..689
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2P5"
FT BINDING 292..303
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255"
FT CONFLICT 88
FT /note="K -> I (in Ref. 1; CAA11688)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="N -> T (in Ref. 3; AAC40189)"
FT /evidence="ECO:0000305"
FT CONFLICT 568
FT /note="C -> S (in Ref. 1; CAA11688)"
FT /evidence="ECO:0000305"
FT CONFLICT 688
FT /note="N -> K (in Ref. 1; CAA11688)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 689 AA; 76203 MW; 1642BBC2CF04FAA3 CRC64;
MGIWKKLTLL LLLLLLVGLG QPPWPAAMAL ALRWFLGDPT CLVLLGLALL GRPWISSWMP
HWLSLVGAAL TLFLLPLQPP PGLRWLHKDV AFTFKMLFYG LKFRRRLNKH PPETFVDALE
RQALAWPDRV ALVCTGSEGS SITNSQLDAR SCQAAWVLKA KLKDAVIQNT RDAAAILVLP
SKTISALSVF LGLAKLGCPV AWINPHSRGM PLLHSVRSSG ASVLIVDPDL QENLEEVLPK
LLAENIHCFY LGHSSPTPGV EALGASLDAA PSDPVPASLR ATIKWKSPAI FIFTSGTTGL
PKPAILSHER VIQVSNVLSF CGCRADDVVY DVLPLYHTIG LVLGFLGCLQ VGATCVLAPK
FSASRFWAEC RQHGVTVILY VGEILRYLCN VPEQPEDKIH TVRLAMGNGL RANVWKNFQQ
RFGPIRIWEF YGSTEGNVGL MNYVGHCGAV GRTSCILRML TPFELVQFDI ETAEPLRDKQ
GFCIPVEPGK PGLLLTKVRK NQPFLGYRGS QAESNRKLVA NVRRVGDLYF NTGDVLTLDQ
EGFFYFQDRL GDTFRWKGEN VSTGEVECVL SSLDFLEEVN VYGVPVPGCE GKVGMAAVKL
APGKTFDGQK LYQHVRSWLP AYATPHFIRI QDSLEITNTY KLVKSRLVRE GFDVGIIADP
LYILDNKAQT FRSLMPDVYQ AVCEGTWNL
