ACOT3_MOUSE
ID ACOT3_MOUSE Reviewed; 432 AA.
AC Q9QYR7; Q6Q2Z7;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Acyl-coenzyme A thioesterase 3;
DE Short=Acyl-CoA thioesterase 3;
DE EC=3.1.2.2 {ECO:0000269|PubMed:15007068};
DE AltName: Full=PTE-Ia;
DE AltName: Full=Peroxisomal acyl-coenzyme A thioester hydrolase 2a;
DE AltName: Full=Peroxisomal long-chain acyl-CoA thioesterase 2;
GN Name=Acot3; Synonyms=Pte1a, Pte2, Pte2a;
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 [GENOMIC DNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=10567408; DOI=10.1074/jbc.274.48.34317;
RA Hunt M.C., Nousiainen S.E.B., Huttunen M.K., Orii K.E., Svensson L.T.,
RA Alexson S.E.H.;
RT "Peroxisome proliferator-induced long chain acyl-CoA thioesterases comprise
RT a highly conserved novel multi-gene family involved in lipid metabolism.";
RL J. Biol. Chem. 274:34317-34326(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=129/Sv;
RX PubMed=15007068; DOI=10.1074/jbc.m313863200;
RA Westin M.A.K., Alexson S.E.H., Hunt M.C.;
RT "Molecular cloning and characterization of two mouse peroxisome
RT proliferator-activated receptor alpha (PPARalpha)-regulated peroxisomal
RT acyl-CoA thioesterases.";
RL J. Biol. Chem. 279:21841-21848(2004).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=16940157; DOI=10.1096/fj.06-6042com;
RA Hunt M.C., Rautanen A., Westin M.A.K., Svensson L.T., Alexson S.E.H.;
RT "Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters
RT shows that convergent, functional evolution results in a reduced number of
RT human peroxisomal ACOTs.";
RL FASEB J. 20:1855-1864(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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 hydrolysis of acyl-CoAs into free fatty acids
CC and coenzyme A (CoASH), regulating their respective intracellular
CC levels (PubMed:15007068, PubMed:16940157). Mainly active on long-chain
CC acyl-CoAs (PubMed:15007068, PubMed:16940157). May have a function in
CC termination of beta-oxidation of fatty acids (PubMed:16940157).
CC {ECO:0000269|PubMed:15007068, ECO:0000269|PubMed:16940157}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2;
CC Evidence={ECO:0000269|PubMed:15007068};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC Evidence={ECO:0000305|PubMed:15007068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanoyl-CoA + H2O = CoA + decanoate + H(+);
CC Xref=Rhea:RHEA:40059, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:27689, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430;
CC Evidence={ECO:0000269|PubMed:15007068, ECO:0000269|PubMed:16940157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060;
CC Evidence={ECO:0000305|PubMed:15007068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+);
CC Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375;
CC Evidence={ECO:0000269|PubMed:15007068, ECO:0000269|PubMed:16940157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136;
CC Evidence={ECO:0000305|PubMed:15007068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate;
CC Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385;
CC Evidence={ECO:0000269|PubMed:15007068, ECO:0000269|PubMed:16940157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120;
CC Evidence={ECO:0000305|PubMed:15007068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate;
CC Xref=Rhea:RHEA:30139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:25629, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394;
CC Evidence={ECO:0000269|PubMed:15007068, ECO:0000269|PubMed:16940157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140;
CC Evidence={ECO:0000305|PubMed:15007068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=eicosanoyl-CoA + H2O = CoA + eicosanoate + H(+);
CC Xref=Rhea:RHEA:40147, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32360, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380;
CC Evidence={ECO:0000269|PubMed:15007068, ECO:0000269|PubMed:16940157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40148;
CC Evidence={ECO:0000305|PubMed:15007068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA + H(+);
CC Xref=Rhea:RHEA:40139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387;
CC Evidence={ECO:0000269|PubMed:15007068, ECO:0000269|PubMed:16940157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140;
CC Evidence={ECO:0000305|PubMed:15007068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + H2O = (9Z,12Z)-octadecadienoate
CC + CoA + H(+); Xref=Rhea:RHEA:40143, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57383; Evidence={ECO:0000269|PubMed:15007068,
CC ECO:0000269|PubMed:16940157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40144;
CC Evidence={ECO:0000305|PubMed:15007068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H2O = (5Z,8Z,11Z,14Z)-
CC eicosatetraenoate + CoA + H(+); Xref=Rhea:RHEA:40151,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368;
CC Evidence={ECO:0000269|PubMed:15007068, ECO:0000269|PubMed:16940157};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40152;
CC Evidence={ECO:0000305|PubMed:15007068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + tetracosanoyl-CoA = CoA + H(+) + tetracosanoate;
CC Xref=Rhea:RHEA:40787, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:31014, ChEBI:CHEBI:57287, ChEBI:CHEBI:65052;
CC Evidence={ECO:0000269|PubMed:15007068};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40788;
CC Evidence={ECO:0000305|PubMed:15007068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexacosanoyl-CoA = CoA + H(+) + hexacosanoate;
CC Xref=Rhea:RHEA:40791, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:31013, ChEBI:CHEBI:57287, ChEBI:CHEBI:64868;
CC Evidence={ECO:0000269|PubMed:15007068};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40792;
CC Evidence={ECO:0000305|PubMed:15007068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=docosanoyl-CoA + H2O = CoA + docosanoate + H(+);
CC Xref=Rhea:RHEA:40783, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:23858, ChEBI:CHEBI:57287, ChEBI:CHEBI:65059;
CC Evidence={ECO:0000269|PubMed:15007068};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40784;
CC Evidence={ECO:0000305|PubMed:15007068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + H2O = (9Z)-hexadecenoate + CoA + H(+);
CC Xref=Rhea:RHEA:40131, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32372, ChEBI:CHEBI:57287, ChEBI:CHEBI:61540;
CC Evidence={ECO:0000269|PubMed:15007068};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40132;
CC Evidence={ECO:0000305|PubMed:15007068};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.9 uM for hexanoyl-coA {ECO:0000269|PubMed:15007068};
CC KM=46.2 uM for octanoyl-coA {ECO:0000269|PubMed:15007068};
CC KM=7.7 uM for decanoyl-coA {ECO:0000269|PubMed:15007068};
CC KM=7.6 uM for dodecanoyl-coA {ECO:0000269|PubMed:15007068};
CC KM=3.8 uM for tetradecanoyl-coA {ECO:0000269|PubMed:15007068};
CC KM=4.0 uM for hexadecanoyl-coA {ECO:0000269|PubMed:15007068};
CC KM=2.8 uM for (9Z)-hexadecenoyl-coA {ECO:0000269|PubMed:15007068};
CC KM=4.2 uM for octadecanoyl-coA {ECO:0000269|PubMed:15007068};
CC KM=4.6 uM for (9Z)-octadecenoyl-coA {ECO:0000269|PubMed:15007068};
CC KM=2.6 uM for (9Z,12Z)-octadecadienoyl-coA
CC {ECO:0000269|PubMed:15007068};
CC KM=2.2 uM for eicosanoyl-coA {ECO:0000269|PubMed:15007068};
CC KM=7.2 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoyl-coA
CC {ECO:0000269|PubMed:15007068};
CC KM=2.3 uM for docosanoyl-coA {ECO:0000269|PubMed:15007068};
CC KM=6.3 uM for tetracosanoyl-coA {ECO:0000269|PubMed:15007068};
CC KM=4.5 uM for hexacosanoyl-coA {ECO:0000269|PubMed:15007068};
CC Vmax=0.02 umol/min/mg enzyme with hexanoyl-coA as substrate
CC {ECO:0000269|PubMed:15007068};
CC Vmax=0.23 umol/min/mg enzyme with octanoyl-coA as substrate
CC {ECO:0000269|PubMed:15007068};
CC Vmax=0.87 umol/min/mg enzyme with decanoyl-coA as substrate
CC {ECO:0000269|PubMed:15007068};
CC Vmax=1.40 umol/min/mg enzyme with dodecanoyl-coA as substrate
CC {ECO:0000269|PubMed:15007068};
CC Vmax=1.60 umol/min/mg enzyme with tetradecanoyl-coA as substrate
CC {ECO:0000269|PubMed:15007068};
CC Vmax=1.85 umol/min/mg enzyme with hexadecanoyl-coA as substrate
CC {ECO:0000269|PubMed:15007068};
CC Vmax=0.93 umol/min/mg enzyme with (9Z)-hexadecenoyl-coA as substrate
CC {ECO:0000269|PubMed:15007068};
CC Vmax=1.43 umol/min/mg enzyme with octadecanoyl-coA as substrate
CC {ECO:0000269|PubMed:15007068};
CC Vmax=0.85 umol/min/mg enzyme with (9Z)-octadecenoyl-coA as substrate
CC {ECO:0000269|PubMed:15007068};
CC Vmax=0.63 umol/min/mg enzyme with (9Z,12Z)-octadecadienoyl-coA as
CC substrate {ECO:0000269|PubMed:15007068};
CC Vmax=0.71 umol/min/mg enzyme with eicosanoyl-coA as substrate
CC {ECO:0000269|PubMed:15007068};
CC Vmax=0.70 umol/min/mg enzyme with (5Z,8Z,11Z,14Z)-eicosatetraenoyl-
CC coA as substrate {ECO:0000269|PubMed:15007068};
CC Vmax=0.37 umol/min/mg enzyme with docosanoyl-coA as substrate
CC {ECO:0000269|PubMed:15007068};
CC Vmax=0.20 umol/min/mg enzyme with tetracosanoyl-coA as substrate
CC {ECO:0000269|PubMed:15007068};
CC Vmax=0.22 umol/min/mg enzyme with hexacosanoyl-coA as substrate
CC {ECO:0000269|PubMed:15007068};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000305|PubMed:15007068, ECO:0000305|PubMed:16940157}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:15007068}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=PTE-Ia 5':1;
CC IsoId=Q9QYR7-1; Sequence=Displayed;
CC Name=2; Synonyms=PTE-Ia 5':2;
CC IsoId=Q9QYR7-2; Sequence=VSP_010994;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in the kidney,
CC expressed at low level in the liver. Isoform 2 is expressed in the
CC kidney, but not in the liver. Isoform 1 is liver-specific
CC (PubMed:10567408). Highly expressed in kidney (at protein level)
CC (PubMed:15007068). {ECO:0000269|PubMed:10567408,
CC ECO:0000269|PubMed:15007068}.
CC -!- INDUCTION: In the liver and kidney, by peroxisome proliferator (such as
CC Clofibrate) treatment, via the peroxisome proliferator-activated
CC receptors (PPARs) or fasting for 24 hours.
CC -!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
CC {ECO:0000305}.
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DR EMBL; AF180804; AAF13873.1; -; Genomic_DNA.
DR EMBL; AF180802; AAF13873.1; JOINED; Genomic_DNA.
DR EMBL; AF180803; AAF13873.1; JOINED; Genomic_DNA.
DR EMBL; AY563098; AAS75456.1; -; mRNA.
DR CCDS; CCDS26036.1; -. [Q9QYR7-1]
DR CCDS; CCDS83985.1; -. [Q9QYR7-2]
DR RefSeq; NP_001333630.1; NM_001346701.1. [Q9QYR7-2]
DR RefSeq; NP_599007.1; NM_134246.3. [Q9QYR7-1]
DR AlphaFoldDB; Q9QYR7; -.
DR SMR; Q9QYR7; -.
DR STRING; 10090.ENSMUSP00000021653; -.
DR SwissLipids; SLP:000000530; -.
DR ESTHER; mouse-acot3; Acyl-CoA_Thioesterase.
DR MEROPS; S09.A51; -.
DR iPTMnet; Q9QYR7; -.
DR PhosphoSitePlus; Q9QYR7; -.
DR jPOST; Q9QYR7; -.
DR MaxQB; Q9QYR7; -.
DR PaxDb; Q9QYR7; -.
DR PRIDE; Q9QYR7; -.
DR ProteomicsDB; 285649; -. [Q9QYR7-1]
DR ProteomicsDB; 285650; -. [Q9QYR7-2]
DR DNASU; 171281; -.
DR Ensembl; ENSMUST00000021653; ENSMUSP00000021653; ENSMUSG00000021228. [Q9QYR7-1]
DR Ensembl; ENSMUST00000120927; ENSMUSP00000112678; ENSMUSG00000021228. [Q9QYR7-2]
DR GeneID; 171281; -.
DR KEGG; mmu:171281; -.
DR UCSC; uc007oef.1; mouse. [Q9QYR7-1]
DR CTD; 171281; -.
DR MGI; MGI:2159619; Acot3.
DR VEuPathDB; HostDB:ENSMUSG00000021228; -.
DR eggNOG; ENOG502QQ8Z; Eukaryota.
DR GeneTree; ENSGT01010000222336; -.
DR HOGENOM; CLU_029849_4_0_1; -.
DR InParanoid; Q9QYR7; -.
DR OMA; IVFPYVP; -.
DR PhylomeDB; Q9QYR7; -.
DR TreeFam; TF314911; -.
DR Reactome; R-MMU-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR SABIO-RK; Q9QYR7; -.
DR UniPathway; UPA00199; -.
DR BioGRID-ORCS; 171281; 3 hits in 61 CRISPR screens.
DR PRO; PR:Q9QYR7; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q9QYR7; protein.
DR Bgee; ENSMUSG00000021228; Expressed in animal zygote and 50 other tissues.
DR ExpressionAtlas; Q9QYR7; baseline and differential.
DR Genevisible; Q9QYR7; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0047617; F:acyl-CoA hydrolase activity; IDA:HGNC-UCL.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IDA:HGNC-UCL.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:HGNC-UCL.
DR GO; GO:0032788; P:saturated monocarboxylic acid metabolic process; IDA:HGNC-UCL.
DR GO; GO:0032789; P:unsaturated monocarboxylic acid metabolic process; IDA:HGNC-UCL.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IDA:HGNC-UCL.
DR Gene3D; 2.60.40.2240; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR016662; Acyl-CoA_thioEstase_long-chain.
DR InterPro; IPR014940; BAAT_C.
DR InterPro; IPR006862; Thio_Ohase/aa_AcTrfase.
DR InterPro; IPR042490; Thio_Ohase/BAAT_N.
DR Pfam; PF08840; BAAT_C; 1.
DR Pfam; PF04775; Bile_Hydr_Trans; 1.
DR PIRSF; PIRSF016521; Acyl-CoA_hydro; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Fatty acid metabolism; Hydrolase; Lipid metabolism;
KW Peroxisome; Reference proteome; Serine esterase.
FT CHAIN 1..432
FT /note="Acyl-coenzyme A thioesterase 3"
FT /id="PRO_0000202148"
FT MOTIF 430..432
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 243
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 337
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 371
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..11
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15007068"
FT /id="VSP_010994"
SQ SEQUENCE 432 AA; 47490 MW; BF5888C59C015359 CRC64;
MHAFTTQNPN RMAPTVILEP AGGCLCDQPV HIAVRGLAPE QPVTLRSVLR DEKGALFRAH
ARYRADSHGE LDLARTPALG GSFSGLEPMG LLWAMEPDRP FWRLIKRDVQ TPFVVELEVL
DGHEPDGGQR LARAVHERHF MAPGVRRVPV REGRVRATLF LPPGTGPFPG IIDLFGIGSG
LLEYRASLLA GKGFAVMALA YNNYEDLPKD MDIIHLEYFE EAVTYLLSHP QVTGSGVGVL
GISKGGELGF AMASFLKNIT AAVIINGSIS NIGGNLQYKD ETVPSVGINT KRVKRTKDGL
KDIVDLLNNP LEGPDQKSLI PVERSDTAFL FLVGQDDHNW KSEFYAREAS KRLQAHGKEK
PQIICYPETG HHIEPPYFPL CKASLNSLVG GPVIWGGEPR AHAMAQVDAW QQLQTFFHNH
LDGKKKTIPA KL
