ID ACS2B_HUMAN Reviewed; 577 AA.
AC Q68CK6; Q86YT1;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 27-MAR-2024, entry version 145.
DE RecName: Full=Acyl-coenzyme A synthetase ACSM2B, mitochondrial;
DE EC=6.2.1.2 {ECO:0000269|PubMed:10434065};
DE AltName: Full=Acyl-CoA synthetase medium-chain family member 2B;
DE AltName: Full=Benzoate--CoA ligase;
DE EC=6.2.1.25 {ECO:0000269|PubMed:10434065, ECO:0000269|PubMed:12616642};
DE AltName: Full=Butyrate--CoA ligase 2B;
DE AltName: Full=Butyryl-coenzyme A synthetase 2B;
DE AltName: Full=Middle-chain acyl-CoA synthetase 2B;
DE AltName: Full=Xenobiotic/medium-chain fatty acid-CoA ligase HXM-A {ECO:0000303|PubMed:10434065};
DE Flags: Precursor;
GN Name=ACSM2B; Synonyms=ACSM2; ORFNames=HYST1046;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 152-163 AND 483-491,
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND CATALYTIC ACTIVITY.
RC TISSUE=Liver;
RX PubMed=12616642; DOI=10.1002/jbt.10056;
RA Vessey D.A., Lau E., Kelley M., Warren R.S.;
RT "Isolation, sequencing, and expression of a cDNA for the HXM-A form of
RT xenobiotic/medium-chain fatty acid:CoA ligase from human liver
RT mitochondria.";
RL J. Biochem. Mol. Toxicol. 17:1-6(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15221005; DOI=10.1038/sj.onc.1207782;
RA Yamada S., Ohira M., Horie H., Ando K., Takayasu H., Suzuki Y., Sugano S.,
RA Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y., Ando H., Suita S.,
RA Kaneko M., Sasaki F., Hashizume K., Ohnuma N., Nakagawara A.;
RT "Expression profiling and differential screening between hepatoblastomas
RT and the corresponding normal livers: identification of high expression of
RT the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas.";
RL Oncogene 23:5901-5911(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, COFACTOR, TISSUE
RP SPECIFICITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10434065; DOI=10.1016/s0304-4165(99)00088-4;
RA Vessey D.A., Kelley M., Warren R.S.;
RT "Characterization of the CoA ligases of human liver mitochondria catalyzing
RT the activation of short- and medium-chain fatty acids and xenobiotic
RT carboxylic acids.";
RL Biochim. Biophys. Acta 1428:455-462(1999).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19634011; DOI=10.1007/s10528-009-9273-z;
RA Boomgaarden I., Vock C., Klapper M., Doering F.;
RT "Comparative analyses of disease risk genes belonging to the acyl-CoA
RT synthetase medium-chain (ACSM) family in human liver and cell lines.";
RL Biochem. Genet. 47:739-748(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [7]
RP REVIEW.
RX PubMed=27351777; DOI=10.1080/17425255.2016.1206888;
RA van der Sluis R., Erasmus E.;
RT "Xenobiotic/medium chain fatty acid: CoA ligase - a critical review on its
RT role in fatty acid metabolism and the detoxification of benzoic acid and
RT aspirin.";
RL Expert Opin. Drug Metab. Toxicol. 12:1169-1179(2016).
CC -!- FUNCTION: Catalyzes the activation of fatty acids by CoA to produce an
CC acyl-CoA, the first step in fatty acid metabolism (PubMed:10434065,
CC PubMed:12616642). Capable of activating medium-chain fatty acids (e.g.
CC butyric (C4) to decanoic (C10) acids), and certain carboxylate-
CC containing xenobiotics, e.g. benzoate (PubMed:10434065,
CC PubMed:12616642). {ECO:0000269|PubMed:10434065,
CC ECO:0000269|PubMed:12616642}.
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:0000269|PubMed:10434065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48341;
CC Evidence={ECO:0000305|PubMed:10434065};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + benzoate + CoA = AMP + benzoyl-CoA + diphosphate;
CC Xref=Rhea:RHEA:10132, ChEBI:CHEBI:16150, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57369,
CC ChEBI:CHEBI:456215; EC=6.2.1.25;
CC Evidence={ECO:0000269|PubMed:10434065, ECO:0000269|PubMed:12616642};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10133;
CC Evidence={ECO:0000305|PubMed:10434065, ECO:0000305|PubMed:12616642};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + hexanoate = AMP + diphosphate + hexanoyl-CoA;
CC Xref=Rhea:RHEA:43740, ChEBI:CHEBI:17120, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:10434065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43741;
CC Evidence={ECO:0000305|PubMed:10434065};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + butanoate + CoA = AMP + butanoyl-CoA + diphosphate;
CC Xref=Rhea:RHEA:46172, ChEBI:CHEBI:17968, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:10434065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46173;
CC Evidence={ECO:0000305|PubMed:10434065};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + octanoate = AMP + diphosphate + octanoyl-CoA;
CC Xref=Rhea:RHEA:33631, ChEBI:CHEBI:25646, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:10434065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33632;
CC Evidence={ECO:0000305|PubMed:10434065};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + decanoate = AMP + decanoyl-CoA + diphosphate;
CC Xref=Rhea:RHEA:33627, ChEBI:CHEBI:27689, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:10434065};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33628;
CC Evidence={ECO:0000305|PubMed:10434065};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10434065};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:10434065};
CC -!- ACTIVITY REGULATION: Activated by monovalent cations, such as
CC potassium, rubidium or ammonium. {ECO:0000269|PubMed:10434065}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13 uM for benzoate {ECO:0000269|PubMed:10434065};
CC KM=800 uM for butyrate {ECO:0000269|PubMed:10434065};
CC KM=110 uM for decanoate {ECO:0000269|PubMed:10434065};
CC KM=74 uM for hexanoate {ECO:0000269|PubMed:10434065};
CC KM=60 uM for laurate {ECO:0000269|PubMed:10434065};
CC KM=160 uM for phenylacetate {ECO:0000269|PubMed:10434065};
CC KM=7.4 uM for salicylate {ECO:0000269|PubMed:10434065};
CC Vmax=103 nmol/min/mg enzyme for benzoate
CC {ECO:0000269|PubMed:10434065};
CC Vmax=27 nmol/min/mg enzyme for butyrate
CC {ECO:0000269|PubMed:10434065};
CC Vmax=15 nmol/min/mg enzyme for decanoate
CC {ECO:0000269|PubMed:10434065};
CC Vmax=88 nmol/min/mg enzyme for hexanoate
CC {ECO:0000269|PubMed:10434065};
CC Vmax=0.2 nmol/min/mg enzyme for laurate
CC {ECO:0000269|PubMed:10434065};
CC Vmax=29 nmol/min/mg enzyme for phenylacetate
CC {ECO:0000269|PubMed:10434065};
CC Vmax=0.7 nmol/min/mg enzyme for salicylate
CC {ECO:0000269|PubMed:10434065};
CC pH dependence:
CC Optimum pH is 8.8. {ECO:0000269|PubMed:10434065};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12616642}.
CC -!- INTERACTION:
CC Q68CK6; P43364: MAGEA11; NbExp=3; IntAct=EBI-2880280, EBI-739552;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10434065,
CC ECO:0000269|PubMed:12616642, ECO:0000269|PubMed:19634011}.
CC -!- TISSUE SPECIFICITY: Detected in liver. {ECO:0000269|PubMed:10434065,
CC ECO:0000269|PubMed:19634011}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AY160217; AAO17576.1; -; mRNA.
DR EMBL; AB073604; BAD38642.1; -; mRNA.
DR EMBL; AC141053; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC141273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS10586.1; -.
DR RefSeq; NP_001098539.1; NM_001105069.1.
DR RefSeq; NP_872423.3; NM_182617.3.
DR AlphaFoldDB; Q68CK6; -.
DR SMR; Q68CK6; -.
DR BioGRID; 131510; 5.
DR IntAct; Q68CK6; 2.
DR STRING; 9606.ENSP00000327453; -.
DR SwissLipids; SLP:000001827; -.
DR iPTMnet; Q68CK6; -.
DR PhosphoSitePlus; Q68CK6; -.
DR BioMuta; ACSM2B; -.
DR DMDM; 296434397; -.
DR EPD; Q68CK6; -.
DR MassIVE; Q68CK6; -.
DR MaxQB; Q68CK6; -.
DR PaxDb; 9606-ENSP00000327453; -.
DR PeptideAtlas; Q68CK6; -.
DR ProteomicsDB; 66005; -.
DR Antibodypedia; 55971; 5 antibodies from 4 providers.
DR DNASU; 348158; -.
DR Ensembl; ENST00000329697.10; ENSP00000327453.6; ENSG00000066813.14.
DR Ensembl; ENST00000414188.6; ENSP00000390378.3; ENSG00000066813.14.
DR Ensembl; ENST00000565232.5; ENSP00000454995.1; ENSG00000066813.14.
DR Ensembl; ENST00000567001.5; ENSP00000456378.1; ENSG00000066813.14.
DR GeneID; 348158; -.
DR KEGG; hsa:348158; -.
DR MANE-Select; ENST00000329697.10; ENSP00000327453.6; NM_001105069.2; NP_001098539.1.
DR UCSC; uc002dhj.5; human.
DR AGR; HGNC:30931; -.
DR CTD; 348158; -.
DR DisGeNET; 348158; -.
DR GeneCards; ACSM2B; -.
DR HGNC; HGNC:30931; ACSM2B.
DR HPA; ENSG00000066813; Group enriched (kidney, liver).
DR MIM; 614359; gene.
DR neXtProt; NX_Q68CK6; -.
DR OpenTargets; ENSG00000066813; -.
DR PharmGKB; PA162375437; -.
DR VEuPathDB; HostDB:ENSG00000066813; -.
DR eggNOG; KOG1175; Eukaryota.
DR GeneTree; ENSGT00940000164294; -.
DR InParanoid; Q68CK6; -.
DR OMA; GPVGCRY; -.
DR OrthoDB; 5474118at2759; -.
DR PhylomeDB; Q68CK6; -.
DR TreeFam; TF354264; -.
DR PathwayCommons; Q68CK6; -.
DR Reactome; R-HSA-177128; Conjugation of salicylate with glycine.
DR Reactome; R-HSA-177135; Conjugation of benzoate with glycine.
DR Reactome; R-HSA-177162; Conjugation of phenylacetate with glutamine.
DR Reactome; R-HSA-9749641; Aspirin ADME.
DR SABIO-RK; Q68CK6; -.
DR SignaLink; Q68CK6; -.
DR BioGRID-ORCS; 348158; 14 hits in 1147 CRISPR screens.
DR ChiTaRS; ACSM2B; human.
DR GeneWiki; ACSM2B; -.
DR GenomeRNAi; 348158; -.
DR Pharos; Q68CK6; Tdark.
DR PRO; PR:Q68CK6; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q68CK6; Protein.
DR Bgee; ENSG00000066813; Expressed in right lobe of liver and 104 other cell types or tissues.
DR ExpressionAtlas; Q68CK6; baseline and differential.
DR Genevisible; Q68CK6; HS.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0018858; F:benzoate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0047760; F:butyrate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0016405; F:CoA-ligase activity; TAS:Reactome.
DR GO; GO:0102391; F:decanoate-CoA ligase activity; IEA:RHEA.
DR GO; GO:0015645; F:fatty acid ligase activity; IBA:GO_Central.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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_com.
DR InterPro; IPR042099; ANL_N_sf.
DR PANTHER; PTHR43605; ACYL-COENZYME A SYNTHETASE; 1.
DR PANTHER; PTHR43605:SF3; ACYL-COENZYME A SYNTHETASE ACSM2B, MITOCHONDRIAL; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Fatty acid metabolism; Ligase;
KW Lipid metabolism; Magnesium; Metal-binding; Mitochondrion;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 47..577
FT /note="Acyl-coenzyme A synthetase ACSM2B, mitochondrial"
FT /id="PRO_0000306094"
FT BINDING 139
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 221..229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 359..364
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 446
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 461
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 469..471
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 472
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 501
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 532
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 540..542
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 557
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CONFLICT 46
FT /note="F -> L (in Ref. 1; AAO17576)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="I -> V (in Ref. 1; AAO17576 and 2; BAD38642)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="F -> I (in Ref. 1; AAO17576)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="G -> E (in Ref. 1; AAO17576)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="T -> A (in Ref. 1; AAO17576)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 577 AA; 64271 MW; 93A6F0581A47F222 CRC64;
MHWLRKVQGL CTLWGTQMSS RTLYINSRQL VSLQWGHQEV PAKFNFASDV LDHWADMEKA
GKRLPSPALW WVNGKGKELM WNFRELSENS QQAANILSGA CGLQRGDRVA VMLPRVPEWW
LVILGCIRAG LIFMPGTIQM KSTDILYRLQ MSKAKAIVAG DEVIQEVDTV ASECPSLRIK
LLVSEKSCDG WLNFKKLLNE ASTTHHCVET GSQEASAIYF TSGTSGLPKM AEHSYSSLGL
KAKMDAGWTG LQASDIMWTI SDTGWILNIL GSLLESWTLG ACTFVHLLPK FDPLVILKTL
SSYPIKSMMG APIVYRMLLQ QDLSSYKFPH LQNCLAGGES LLPETLENWR AQTGLDIREF
YGQTETGLTC MVSKTMKIKP GYMGTAASCY DVQVIDDKGN VLPPGTEGDI GIRVKPIRPI
GIFSGYVENP DKTAANIRGD FWLLGDRGIK DEDGYFQFMG RADDIINSSG YRIGPSEVEN
ALMKHPAVVE TAVISSPDPV RGEVVKAFVI LASQFLSHDP EQLTKELQQH VKSVTAPYKY
PRKIEFVLNL PKTVTGKIQR TKLRDKEWKM SGKARAQ
//
