LOX3_SOYBN
ID LOX3_SOYBN Reviewed; 857 AA.
AC P09186; Q39838;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Seed linoleate 9S-lipoxygenase-3;
DE EC=1.13.11.58;
DE AltName: Full=Lipoxygenase-3;
DE Short=L-3;
GN Name=LOX1.3; Synonyms=LOX3;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RA Yenofsky R.L., Fine M., Liu C.;
RT "Isolation and characterization of a soybean (Glycine max) lipoxygenase-3
RT gene.";
RL Mol. Gen. Genet. 211:215-222(1988).
RN [2]
RP SEQUENCE REVISION.
RA Yenofsky R.L.;
RL Submitted (DEC-1988) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE, AND MUTAGENESIS OF ASN-713.
RC STRAIN=cv. Provar;
RX PubMed=7999759; DOI=10.1021/bi00254a010;
RA Kramer J.A., Johnson K.R., Dunham W.R., Sands R.H., Funk M.O. Jr.;
RT "Position 713 is critical for catalysis but not iron binding in soybean
RT lipoxygenase 3.";
RL Biochemistry 33:15017-15022(1994).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RC STRAIN=cv. Provar;
RX PubMed=9294864;
RX DOI=10.1002/(sici)1097-0134(199709)29:1<15::aid-prot2>3.0.co;2-e;
RA Skrzypczak-Jankun E., Amzel L.M., Kroa B.A., Funk M.O. Jr.;
RT "Structure of soybean lipoxygenase L3 and a comparison with its L1
RT isoenzyme.";
RL Proteins 29:15-31(1997).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RC STRAIN=cv. Provar;
RX PubMed=9922163; DOI=10.1021/bi981989t;
RA Pham C., Jankun J., Skrzypczak-Jankun E., Flowers R.A., Funk M.O. Jr.;
RT "Structural and thermochemical characterization of lipoxygenase-catechol
RT complexes.";
RL Biochemistry 37:17952-17957(1998).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH IRON IONS AND
RP SUBSTRATE.
RC STRAIN=cv. Provar;
RX PubMed=11686682; DOI=10.1021/ja011759t;
RA Skrzypczak-Jankun E., Bross R.A., Carroll R.T., Dunham W.R., Funk M.O. Jr.;
RT "Three-dimensional structure of a purple lipoxygenase.";
RL J. Am. Chem. Soc. 123:10814-10820(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH IRON IONS AND
RP CURCUMIN.
RX PubMed=12792803;
RA Skrzypczak-Jankun E., Zhou K., McCabe N.P., Selman S.H., Jankun J.;
RT "Structure of curcumin in complex with lipoxygenase and its significance in
RT cancer.";
RL Int. J. Mol. Med. 12:17-24(2003).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH IRON IONS AND THE
RP INHIBITOR EPIGALLO-CATECHIN.
RX PubMed=12964012;
RA Skrzypczak-Jankun E., Zhou K., Jankun J.;
RT "Inhibition of lipoxygenase by (-)-epigallocatechin gallate: X-ray analysis
RT at 2.1 A reveals degradation of EGCG and shows soybean LOX-3 complex with
RT EGC instead.";
RL Int. J. Mol. Med. 12:415-420(2003).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH IRON IONS AND
RP 4-NITROCATECHOL.
RX PubMed=14993710; DOI=10.1107/s0907444904000861;
RA Skrzypczak-Jankun E., Borbulevych O.Y., Jankun J.;
RT "Soybean lipoxygenase-3 in complex with 4-nitrocatechol.";
RL Acta Crystallogr. D 60:613-615(2004).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH IRON IONS AND
RP PROTOCATECHUIC ACID.
RX PubMed=14705020; DOI=10.1002/prot.10579;
RA Borbulevych O.Y., Jankun J., Selman S.H., Skrzypczak-Jankun E.;
RT "Lipoxygenase interactions with natural flavonoid, quercetin, reveal a
RT complex with protocatechuic acid in its X-ray structure at 2.1 A
RT resolution.";
RL Proteins 54:13-19(2004).
CC -!- FUNCTION: Plant lipoxygenase may be involved in a number of diverse
CC aspects of plant physiology including growth and development, pest
CC resistance, and senescence or responses to wounding. It catalyzes the
CC hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene
CC structure.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (9S)-hydroperoxy-(10E,12Z)-
CC octadecadienoate; Xref=Rhea:RHEA:30291, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:60955; EC=1.13.11.58;
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00726};
CC Note=Binds 1 Fe cation per subunit. Iron is tightly bound.
CC {ECO:0000255|PROSITE-ProRule:PRU00726};
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis. {ECO:0000255|PROSITE-
CC ProRule:PRU00726}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11686682,
CC ECO:0000269|PubMed:12792803, ECO:0000269|PubMed:12964012,
CC ECO:0000269|PubMed:14705020, ECO:0000269|PubMed:14993710}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: Soybean contains at least 4 distinct isoenzymes, L-1, L-
CC 2, L-3a and L-3b in dry seeds, and at least two distinct isozymes in
CC the hypocotyl/radicle region of the seedling stem.
CC -!- SIMILARITY: Belongs to the lipoxygenase family. {ECO:0000305}.
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DR EMBL; X06928; CAA30016.1; -; Genomic_DNA.
DR EMBL; X13302; CAA31664.1; ALT_SEQ; mRNA.
DR EMBL; U50081; AAB41272.1; -; mRNA.
DR PIR; S01864; S01864.
DR RefSeq; NP_001235383.1; NM_001248454.1.
DR PDB; 1HU9; X-ray; 2.20 A; A=1-857.
DR PDB; 1IK3; X-ray; 2.00 A; A=1-857.
DR PDB; 1JNQ; X-ray; 2.10 A; A=1-857.
DR PDB; 1LNH; X-ray; 2.60 A; A=1-857.
DR PDB; 1N8Q; X-ray; 2.10 A; A=1-857.
DR PDB; 1NO3; X-ray; 2.15 A; A=1-857.
DR PDB; 1ROV; X-ray; 2.00 A; A=1-857.
DR PDB; 1RRH; X-ray; 2.00 A; A=1-857.
DR PDB; 1RRL; X-ray; 2.09 A; A/B=1-857.
DR PDBsum; 1HU9; -.
DR PDBsum; 1IK3; -.
DR PDBsum; 1JNQ; -.
DR PDBsum; 1LNH; -.
DR PDBsum; 1N8Q; -.
DR PDBsum; 1NO3; -.
DR PDBsum; 1ROV; -.
DR PDBsum; 1RRH; -.
DR PDBsum; 1RRL; -.
DR AlphaFoldDB; P09186; -.
DR SMR; P09186; -.
DR STRING; 3847.GLYMA15G03030.1; -.
DR BindingDB; P09186; -.
DR GeneID; 547869; -.
DR KEGG; gmx:547869; -.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR InParanoid; P09186; -.
DR OrthoDB; 385042at2759; -.
DR BRENDA; 1.13.11.B6; 2483.
DR UniPathway; UPA00382; -.
DR EvolutionaryTrace; P09186; -.
DR Proteomes; UP000008827; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990136; F:linoleate 9S-lipoxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0034440; P:lipid oxidation; IBA:GO_Central.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01751; PLAT_LH2; 1.
DR Gene3D; 4.10.372.10; -; 1.
DR InterPro; IPR000907; LipOase.
DR InterPro; IPR013819; LipOase_C.
DR InterPro; IPR036226; LipOase_C_sf.
DR InterPro; IPR020834; LipOase_CS.
DR InterPro; IPR020833; LipOase_Fe_BS.
DR InterPro; IPR001246; LipOase_plant.
DR InterPro; IPR042057; Lipoxy_PLAT/LH2.
DR InterPro; IPR027433; Lipoxygenase_dom_3.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR PANTHER; PTHR11771; PTHR11771; 1.
DR Pfam; PF00305; Lipoxygenase; 1.
DR Pfam; PF01477; PLAT; 1.
DR PRINTS; PR00087; LIPOXYGENASE.
DR PRINTS; PR00468; PLTLPOXGNASE.
DR SMART; SM00308; LH2; 1.
DR SUPFAM; SSF48484; SSF48484; 1.
DR SUPFAM; SSF49723; SSF49723; 1.
DR PROSITE; PS00711; LIPOXYGENASE_1; 1.
DR PROSITE; PS00081; LIPOXYGENASE_2; 1.
DR PROSITE; PS51393; LIPOXYGENASE_3; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Dioxygenase; Fatty acid biosynthesis;
KW Fatty acid metabolism; Iron; Lipid biosynthesis; Lipid metabolism;
KW Metal-binding; Oxidoreductase; Oxylipin biosynthesis; Reference proteome.
FT CHAIN 1..857
FT /note="Seed linoleate 9S-lipoxygenase-3"
FT /id="PRO_0000220719"
FT DOMAIN 38..163
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT DOMAIN 166..857
FT /note="Lipoxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00726"
FT REGION 212..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 518
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT BINDING 523
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT BINDING 709
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT BINDING 713
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT BINDING 857
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT VARIANT 25
FT /note="H -> D (in strain: cv. Provar)"
FT VARIANT 57
FT /note="P -> S (in strain: cv. Provar)"
FT VARIANT 112
FT /note="L -> P (in strain: cv. Provar)"
FT VARIANT 201
FT /note="V -> I (in strain: cv. Provar)"
FT VARIANT 382
FT /note="E -> D (in strain: cv. Provar)"
FT VARIANT 428
FT /note="G -> D (in strain: cv. Provar)"
FT VARIANT 630
FT /note="A -> T (in strain: cv. Provar)"
FT MUTAGEN 713
FT /note="N->A,S: No loss of iron-binding; loss of catalytic
FT activity."
FT /evidence="ECO:0000269|PubMed:7999759"
FT MUTAGEN 713
FT /note="N->H: No loss of iron-binding; no change in
FT catalytic activity."
FT /evidence="ECO:0000269|PubMed:7999759"
FT STRAND 10..20
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:1IK3"
FT TURN 26..30
FT /evidence="ECO:0007829|PDB:1IK3"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:1RRL"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:1RRL"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 55..68
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:1RRH"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:1LNH"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:1RRH"
FT STRAND 112..119
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 125..133
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 141..149
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1JNQ"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:1IK3"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:1IK3"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 177..188
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:1RRH"
FT STRAND 224..230
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:1JNQ"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:1RRH"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:1RRH"
FT HELIX 273..278
FT /evidence="ECO:0007829|PDB:1IK3"
FT TURN 279..283
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 284..293
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 304..308
FT /evidence="ECO:0007829|PDB:1IK3"
FT TURN 309..313
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 319..324
FT /evidence="ECO:0007829|PDB:1IK3"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 361..370
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:1JNQ"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 393..396
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 415..420
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 424..428
FT /evidence="ECO:0007829|PDB:1IK3"
FT TURN 431..433
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 434..436
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 437..441
FT /evidence="ECO:0007829|PDB:1IK3"
FT TURN 442..444
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 449..456
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 462..472
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 474..477
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 482..486
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 492..515
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 516..522
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 523..536
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 542..547
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 548..551
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 554..564
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 566..569
FT /evidence="ECO:0007829|PDB:1JNQ"
FT HELIX 571..575
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 579..581
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 582..589
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 590..592
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 595..598
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 600..606
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 609..612
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 619..625
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 628..651
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 656..659
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 662..673
FT /evidence="ECO:0007829|PDB:1IK3"
FT TURN 674..676
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 677..679
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 688..690
FT /evidence="ECO:0007829|PDB:1N8Q"
FT HELIX 691..705
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 707..713
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 716..720
FT /evidence="ECO:0007829|PDB:1IK3"
FT TURN 723..725
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 730..732
FT /evidence="ECO:0007829|PDB:1N8Q"
FT STRAND 737..739
FT /evidence="ECO:0007829|PDB:1ROV"
FT HELIX 740..747
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 749..754
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 760..773
FT /evidence="ECO:0007829|PDB:1IK3"
FT TURN 783..785
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 795..818
FT /evidence="ECO:0007829|PDB:1IK3"
FT HELIX 825..827
FT /evidence="ECO:0007829|PDB:1IK3"
FT TURN 828..832
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 844..846
FT /evidence="ECO:0007829|PDB:1IK3"
FT STRAND 852..854
FT /evidence="ECO:0007829|PDB:1IK3"
SQ SEQUENCE 857 AA; 96758 MW; 5DFC33D0F6FD32F0 CRC64;
MLGGLLHRGH KIKGTVVLMR KNVLHVNSVT SVGGIIGQGL DLVGSTLDTL TAFLGRPVSL
QLISATKADA NGKGKLGKAT FLEGIITSLP TLGAGQSAFK INFEWDDGSG ILGAFYIKNF
MQTEFFLVSL TLEDIPNHGS IHFVCNSWIY NAKLFKSDRI FFANQTYLPS ETPAPLVKYR
EEELHNLRGD GTGERKEWER VYDYDVYNDL GDPDKGENHA RPVLGGNDTF PYPRRGRTGR
KPTRKDPNSE SRSNDVYLPR DEAFGHLKSS DFLTYGLKSV SQNVLPLLQS AFDLNFTPRE
FDSFDEVHGL YSGGIKLPTD IISKISPLPV LKEIFRTDGE QALKFPPPKV IQVSKSAWMT
DEEFAREMLA GVNPNLIRCL KEFPPRSKLD SQVYGDHTSQ ITKEHLEPNL EGLTVDEAIQ
NKRLFLLGHH DPIMPYLRRI NATSTKAYAT RTILFLKNDG TLRPLAIELS LPHPQGDQSG
AFSQVFLPAD EGVESSIWLL AKAYVVVNDS CYHQLVSHWL NTHAVVEPFI IATNRHLSVV
HPIYKLLHPH YRDTMNINGL ARLSLVNDGG VIEQTFLWGR YSVEMSAVVY KDWVFTDQAL
PADLIKRGMA IEDPSCPHGI RLVIEDYPYA VDGLEIWDAI KTWVHEYVFL YYKSDDTLRE
DPELQACWKE LVEVGHGDKK NEPWWPKMQT REELVEACAI IIWTASALHA AVNFGQYPYG
GLILNRPTLS RRFMPEKGSA EYEELRKNPQ KAYLKTITPK FQTLIDLSVI EILSRHASDE
VYLGERDNPN WTSDTRALEA FKRFGNKLAQ IENKLSERNN DEKLRNRCGP VQMPYTLLLP
SSKEGLTFRG IPNSISI
