LKHA4_MOUSE
ID LKHA4_MOUSE Reviewed; 611 AA.
AC P24527; Q3UY71; Q8VDR8;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Leukotriene A-4 hydrolase;
DE Short=LTA-4 hydrolase;
DE EC=3.3.2.6 {ECO:0000269|PubMed:1881903, ECO:0000269|PubMed:9287304};
DE AltName: Full=Leukotriene A(4) hydrolase;
DE AltName: Full=Tripeptide aminopeptidase LTA4H;
DE EC=3.4.11.4 {ECO:0000269|PubMed:1881903, ECO:0000269|PubMed:20813919};
GN Name=Lta4h;
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].
RC TISSUE=Spleen;
RX PubMed=1710117; DOI=10.1016/0006-291x(91)90459-k;
RA Medina J.F., Raadmark O., Funk C.D., Haeggstroem J.Z.;
RT "Molecular cloning and expression of mouse leukotriene A4 hydrolase cDNA.";
RL Biochem. Biophys. Res. Commun. 176:1516-1524(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-296; HIS-300 AND GLU-319, AND
RP FUNCTION.
RX PubMed=1881903; DOI=10.1073/pnas.88.17.7620;
RA Medina J.F., Wetterholm A., Raadmark O., Shapiro R., Haeggstroem J.Z.,
RA Vallee B.L., Samuelsson B.;
RT "Leukotriene A4 hydrolase: determination of the three zinc-binding ligands
RT by site-directed mutagenesis and zinc analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:7620-7624(1991).
RN [5]
RP MUTAGENESIS OF TYR-384, CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=9287304; DOI=10.1074/jbc.272.37.23057;
RA Andberg M.B., Hamberg M., Haeggstrom J.Z.;
RT "Mutation of tyrosine 383 in leukotriene A4 hydrolase allows conversion of
RT leukotriene A4 into 5S,6S-dihydroxy-7,9-trans-11,14-cis-eicosatetraenoic
RT acid. Implications for the epoxide hydrolase mechanism.";
RL J. Biol. Chem. 272:23057-23063(1997).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=10586081;
RA Byrum R.S., Goulet J.L., Snouwaert J.N., Griffiths R.J., Koller B.H.;
RT "Determination of the contribution of cysteinyl leukotrienes and
RT leukotriene B4 in acute inflammatory responses using 5-lipoxygenase- and
RT leukotriene A4 hydrolase-deficient mice.";
RL J. Immunol. 163:6810-6819(1999).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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).
RN [8]
RP CATALYTIC ACTIVITY, FUNCTION, DISRUPTION PHENOTYPE, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=20813919; DOI=10.1126/science.1190594;
RA Snelgrove R.J., Jackson P.L., Hardison M.T., Noerager B.D., Kinloch A.,
RA Gaggar A., Shastry S., Rowe S.M., Shim Y.M., Hussell T., Blalock J.E.;
RT "A critical role for LTA4H in limiting chronic pulmonary neutrophilic
RT inflammation.";
RL Science 330:90-94(2010).
CC -!- FUNCTION: Bifunctional zinc metalloenzyme that comprises both epoxide
CC hydrolase (EH) and aminopeptidase activities (By similarity). Acts as
CC an epoxide hydrolase to catalyze the conversion of LTA4 to the pro-
CC inflammatory mediator leukotriene B4 (LTB4) (PubMed:1881903,
CC PubMed:9287304). Has also aminopeptidase activity, with high affinity
CC for N-terminal arginines of various synthetic tripeptides (By
CC similarity). In addition to its pro-inflammatory EH activity, may also
CC counteract inflammation by its aminopeptidase activity, which
CC inactivates by cleavage another neutrophil attractant, the tripeptide
CC Pro-Gly-Pro (PGP), a bioactive fragment of collagen generated by the
CC action of matrix metalloproteinase-9 (MMP9) and prolylendopeptidase
CC (PREPL) (PubMed:20813919). Involved also in the biosynthesis of
CC resolvin E1 and 18S-resolvin E1 from eicosapentaenoic acid, two lipid
CC mediators that show potent anti-inflammatory and pro-resolving actions
CC (By similarity). {ECO:0000250|UniProtKB:P09960,
CC ECO:0000269|PubMed:1881903, ECO:0000269|PubMed:20813919,
CC ECO:0000269|PubMed:9287304}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + leukotriene A4 = leukotriene B4; Xref=Rhea:RHEA:22324,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:57461, ChEBI:CHEBI:57463; EC=3.3.2.6;
CC Evidence={ECO:0000269|PubMed:1881903, ECO:0000269|PubMed:9287304};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22325;
CC Evidence={ECO:0000269|PubMed:1881903, ECO:0000269|PubMed:9287304};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5S,6S)-epoxy-(18R)-hydroxy-(7E,9E,11Z,14Z,16E)-
CC eicosapentaenoate + H2O = resolvin E1; Xref=Rhea:RHEA:50272,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:91000, ChEBI:CHEBI:132219;
CC Evidence={ECO:0000250|UniProtKB:P09960};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50273;
CC Evidence={ECO:0000250|UniProtKB:P09960};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5S,6S)-epoxy-(18S)-hydroxy-(7E,9E,11Z,14Z,16E)-
CC eicosapentaenoate + H2O = 18S-resolvin E1; Xref=Rhea:RHEA:51988,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:134661, ChEBI:CHEBI:136057;
CC Evidence={ECO:0000250|UniProtKB:P09960};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51989;
CC Evidence={ECO:0000250|UniProtKB:P09960};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of the N-terminal residue from a tripeptide.;
CC EC=3.4.11.4; Evidence={ECO:0000269|PubMed:1881903,
CC ECO:0000269|PubMed:20813919};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P09960};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P09960};
CC -!- ACTIVITY REGULATION: Inhibited by bestatin (By similarity). The epoxide
CC hydrolase activity is restrained by suicide inactivation that involves
CC binding of LTA4 to Tyr-379 (PubMed:9287304). 4-(4-benzylphenyl)thiazol-
CC 2-amine (ARM1) selectively inhibits the epoxide hydrolase activity (By
CC similarity). {ECO:0000250|UniProtKB:P09960,
CC ECO:0000269|PubMed:9287304}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 uM for leukotriene A4 {ECO:0000269|PubMed:9287304};
CC KM=1.59 uM for Pro-Gly-Pro {ECO:0000269|PubMed:20813919};
CC Vmax=1030 nmol/min/mg enzyme for leukotriene A4
CC {ECO:0000269|PubMed:9287304};
CC -!- PATHWAY: Lipid metabolism; leukotriene B4 biosynthesis.
CC {ECO:0000269|PubMed:1881903, ECO:0000269|PubMed:9287304}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P09960}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P09960}.
CC -!- PTM: Phosphorylation at Ser-416 inhibits leukotriene-A4 hydrolase
CC activity. {ECO:0000250|UniProtKB:P09960}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice have normal phenotypes.
CC Inflammatory reactions are reduced as are some other immunological
CC responses. {ECO:0000269|PubMed:10586081, ECO:0000269|PubMed:20813919}.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR EMBL; M63848; AAB59675.1; -; mRNA.
DR EMBL; AK134931; BAE22342.1; -; mRNA.
DR EMBL; BC021417; AAH21417.1; -; mRNA.
DR CCDS; CCDS24125.1; -.
DR PIR; JN0066; JN0066.
DR RefSeq; NP_001300826.1; NM_001313897.1.
DR RefSeq; NP_032543.2; NM_008517.2.
DR AlphaFoldDB; P24527; -.
DR SMR; P24527; -.
DR BioGRID; 201217; 12.
DR IntAct; P24527; 1.
DR STRING; 10090.ENSMUSP00000016033; -.
DR BindingDB; P24527; -.
DR ChEMBL; CHEMBL3738; -.
DR MEROPS; M01.004; -.
DR iPTMnet; P24527; -.
DR PhosphoSitePlus; P24527; -.
DR SwissPalm; P24527; -.
DR EPD; P24527; -.
DR jPOST; P24527; -.
DR MaxQB; P24527; -.
DR PaxDb; P24527; -.
DR PeptideAtlas; P24527; -.
DR PRIDE; P24527; -.
DR ProteomicsDB; 292101; -.
DR Antibodypedia; 4453; 553 antibodies from 37 providers.
DR DNASU; 16993; -.
DR Ensembl; ENSMUST00000016033; ENSMUSP00000016033; ENSMUSG00000015889.
DR GeneID; 16993; -.
DR KEGG; mmu:16993; -.
DR UCSC; uc007gur.1; mouse.
DR CTD; 4048; -.
DR MGI; MGI:96836; Lta4h.
DR VEuPathDB; HostDB:ENSMUSG00000015889; -.
DR eggNOG; KOG1047; Eukaryota.
DR GeneTree; ENSGT00940000156375; -.
DR HOGENOM; CLU_014505_0_0_1; -.
DR InParanoid; P24527; -.
DR OMA; YHPICRQ; -.
DR OrthoDB; 775595at2759; -.
DR PhylomeDB; P24527; -.
DR TreeFam; TF300758; -.
DR BRENDA; 3.3.2.6; 3474.
DR Reactome; R-MMU-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-9018676; Biosynthesis of D-series resolvins.
DR Reactome; R-MMU-9018681; Biosynthesis of protectins.
DR Reactome; R-MMU-9018896; Biosynthesis of E-series 18(S)-resolvins.
DR Reactome; R-MMU-9020265; Biosynthesis of aspirin-triggered D-series resolvins.
DR Reactome; R-MMU-9023661; Biosynthesis of E-series 18(R)-resolvins.
DR SABIO-RK; P24527; -.
DR UniPathway; UPA00878; -.
DR BioGRID-ORCS; 16993; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Lta4h; mouse.
DR PRO; PR:P24527; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P24527; protein.
DR Bgee; ENSMUSG00000015889; Expressed in granulocyte and 266 other tissues.
DR Genevisible; P24527; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0004177; F:aminopeptidase activity; ISS:UniProtKB.
DR GO; GO:0004301; F:epoxide hydrolase activity; ISS:UniProtKB.
DR GO; GO:0004463; F:leukotriene-A4 hydrolase activity; ISS:UniProtKB.
DR GO; GO:0070006; F:metalloaminopeptidase activity; ISO:MGI.
DR GO; GO:0045148; F:tripeptide aminopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0019370; P:leukotriene biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006691; P:leukotriene metabolic process; ISO:MGI.
DR GO; GO:0043171; P:peptide catabolic process; ISS:UniProtKB.
DR GO; GO:0019538; P:protein metabolic process; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
DR GO; GO:0010043; P:response to zinc ion; IEA:Ensembl.
DR GO; GO:0060509; P:type I pneumocyte differentiation; IEA:Ensembl.
DR CDD; cd09599; M1_LTA4H; 1.
DR Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 1.25.40.320; -; 1.
DR Gene3D; 2.60.40.1730; -; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR012777; LTA4H.
DR InterPro; IPR038502; M1_LTA-4_hydro/amino_C_sf.
DR InterPro; IPR034015; M1_LTA4H.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR015211; Peptidase_M1_C.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR45726; PTHR45726; 1.
DR Pfam; PF09127; Leuk-A4-hydro_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SMART; SM01263; Leuk-A4-hydro_C; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF63737; SSF63737; 1.
DR TIGRFAMs; TIGR02411; leuko_A4_hydro; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Hydrolase; Leukotriene biosynthesis; Metal-binding;
KW Metalloprotease; Phosphoprotein; Protease; Reference proteome; Zinc.
FT CHAIN 1..611
FT /note="Leukotriene A-4 hydrolase"
FT /id="PRO_0000095125"
FT ACT_SITE 297
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P09960"
FT ACT_SITE 384
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P09960"
FT BINDING 135..137
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09960"
FT BINDING 267..272
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09960"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P09960"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P09960"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P09960"
FT BINDING 564..566
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P09960"
FT SITE 376
FT /note="Essential for epoxide hydrolase activity, but not
FT for aminopeptidase activity"
FT /evidence="ECO:0000250|UniProtKB:P09960"
FT SITE 379
FT /note="Covalently modified during suicide inhibition by
FT leukotrienes"
FT /evidence="ECO:0000250|UniProtKB:P09960"
FT MOD_RES 73
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09960"
FT MOD_RES 337
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09960"
FT MOD_RES 414
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09960"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09960"
FT MOD_RES 573
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09960"
FT MUTAGEN 296
FT /note="H->Y: Complete loss of LTA4 hydrolase and peptidase
FT enzyme activities."
FT /evidence="ECO:0000269|PubMed:1881903"
FT MUTAGEN 300
FT /note="H->Y: Complete loss of LTA4 hydrolase and peptidase
FT enzyme activities."
FT /evidence="ECO:0000269|PubMed:1881903"
FT MUTAGEN 319
FT /note="E->Q: Complete loss of LTA4 hydrolase and peptidase
FT enzyme activities."
FT /evidence="ECO:0000269|PubMed:1881903"
FT MUTAGEN 384
FT /note="Y->F,H,Q: Alters leukotriene hydrolase activity,
FT strongly enhancing the formation of a metabolite that is
FT normally produced in trace amounts."
FT /evidence="ECO:0000269|PubMed:9287304"
FT CONFLICT 447
FT /note="T -> A (in Ref. 1; AAB59675 and 3; AAH21417)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 611 AA; 69051 MW; CCF8D30F6FA9721E CRC64;
MPEVADTCSL ASPASVCRTQ HLHLRCSVDF ARRTLTGTAA LTVQSQEENL RSLTLDTKDL
TIEKVVINGQ EVKYTLGESQ GYKGSPMEIS LPIALSKNQE IVIEISFETS PKSSALQWLT
PEQTSGKQHP YLFSQCQAIH CRAILPCQDT PSVKLTYTAE VSVPKELVAL MSAIRDGEAP
DPEDPSRKIY RFNQRVPIPC YLIALVVGAL ESRQIGPRTL VWSEKEQVEK SANEFSETES
MLKIAEDLGG PYVWGQYDLL VLPPSFPYGG MENPCLTFVT PTLLAGDKSL SNVIAHEISH
SWTGNLVTNK TWDHFWLNEG HTVYLERHIC GRLFGEKFRH FHALGGWGEL QNTIKTFGES
HPFTKLVVDL KDVDPDVAYS SIPYEKGFAL LFYLEQLLGG PEVFLGFLKA YVKKFSYQSV
TTDDWKSFLY SHFKDKVDLL NQVDWNTWLY APGLPPVKPN YDVTLTNACI ALSQRWVTAK
EEDLSSFSIA DLKDLSSHQL NEFLAQVLQK APLPLGHIKR MQEVYNFNAI NNSEIRFRWL
RLCIQSKWEE AIPLALKMAT EQGRMKFTRP LFKDLAAFDK SHDQAVHTYQ EHKASMHPVT
AMLVGRDLKV D
