VILI_CHICK
ID VILI_CHICK Reviewed; 826 AA.
AC P02640;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Villin-1;
GN Name=VIL1; Synonyms=VIL;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2839826; DOI=10.1073/pnas.85.14.4986;
RA Bazari W.L., Matsudaira P., Wallek M., Smeal T., Jakes R., Ahmed Y.;
RT "Villin sequence and peptide map identify six homologous domains.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:4986-4990(1988).
RN [2]
RP PROTEIN SEQUENCE OF 751-826.
RX PubMed=6790532; DOI=10.1016/s0021-9258(18)43401-1;
RA Glenney J.R. Jr., Geisler N., Kaulfus P., Weber K.;
RT "Demonstration of at least two different actin-binding sites in villin, a
RT calcium-regulated modulator of F-actin organization.";
RL J. Biol. Chem. 256:8156-8161(1981).
RN [3]
RP CALCIUM-BINDING SITES.
RX PubMed=6848508; DOI=10.1016/s0021-9258(18)33266-6;
RA Hesterberg L.K., Weber K.;
RT "Demonstration of three distinct calcium-binding sites in villin, a
RT modulator of actin assembly.";
RL J. Biol. Chem. 258:365-369(1983).
RN [4]
RP FUNCTION, ASSOCIATION WITH F-ACTIN, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=3793760; DOI=10.1083/jcb.104.1.29;
RA Burgess D.R., Broschat K.O., Hayden J.M.;
RT "Tropomyosin distinguishes between the two actin-binding sites of villin
RT and affects actin-binding properties of other brush border proteins.";
RL J. Cell Biol. 104:29-40(1987).
RN [5]
RP FUNCTION, ASSOCIATION WITH F-ACTIN, AND MUTAGENESIS OF ARG-138; HIS-141;
RP GLY-144; LYS-145 AND LYS-146.
RX PubMed=1618806; DOI=10.1016/s0021-9258(18)42383-6;
RA de Arruda M.V., Bazari H., Wallek M., Matsudaira P.;
RT "An actin footprint on villin. Single site substitutions in a cluster of
RT basic residues inhibit the actin severing but not capping activity of
RT villin.";
RL J. Biol. Chem. 267:13079-13085(1992).
RN [6]
RP STRUCTURE BY NMR OF 1-127.
RX PubMed=8142900; DOI=10.1002/pro.5560030110;
RA Markus M.A., Nakayama T., Matsudaira P., Wagner G.;
RT "Solution structure of villin 14T, a domain conserved among actin-severing
RT proteins.";
RL Protein Sci. 3:70-81(1994).
RN [7]
RP STRUCTURE BY NMR OF 1-127.
RX PubMed=9194180; DOI=10.1002/pro.5560060608;
RA Markus M.A., Matsudaira P., Wagner G.;
RT "Refined structure of villin 14T and a detailed comparison with other
RT actin-severing domains.";
RL Protein Sci. 6:1197-1209(1997).
RN [8]
RP STRUCTURE BY NMR OF 792-826.
RX PubMed=9164455; DOI=10.1038/nsb0397-180;
RA McKnight C.J., Matsudaira P.T., Kim P.S.;
RT "NMR structure of the 35-residue villin headpiece subdomain.";
RL Nat. Struct. Biol. 4:180-184(1997).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 760-826, AND MUTAGENESIS OF
RP ARG-787 AND TRP-814.
RX PubMed=16142894; DOI=10.1021/bi050850x;
RA Meng J., Vardar D., Wang Y., Guo H.-C., Head J.F., McKnight C.J.;
RT "High-resolution crystal structures of villin headpiece and mutants with
RT reduced F-actin binding activity.";
RL Biochemistry 44:11963-11973(2005).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (0.95 ANGSTROMS) OF 792-826.
RX PubMed=15894611; DOI=10.1073/pnas.0502495102;
RA Chiu T.K., Kubelka J., Herbst-Irmer R., Eaton W.A., Hofrichter J.,
RA Davies D.R.;
RT "High-resolution X-ray crystal structures of the villin headpiece
RT subdomain, an ultrafast folding protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:7517-7522(2005).
CC -!- FUNCTION: Epithelial cell-specific Ca(2+)-regulated actin-modifying
CC protein that modulates the reorganization of microvillar actin
CC filaments. Plays a role in the actin nucleation, actin filament bundle
CC assembly, actin filament capping and severing. Binds
CC phosphatidylinositol 4,5-bisphosphate (PIP2) and lysophosphatidic acid
CC (LPA); binds LPA with higher affinity than PIP2. Binding to LPA
CC increases its phosphorylation by SRC and inhibits all actin-modifying
CC activities. Binding to PIP2 inhibits actin-capping and -severing
CC activities but enhances actin-bundling activity. Regulates the
CC intestinal epithelial cell morphology, cell invasion, cell migration
CC and apoptosis. Protects against apoptosis induced by dextran sodium
CC sulfate (DSS) in the gastrointestinal epithelium. Appears to regulate
CC cell death by maintaining mitochondrial integrity. Enhances hepatocyte
CC growth factor (HGF)-induced epithelial cell motility, chemotaxis and
CC wound repair (By similarity). Its actin-bundling activity is inhibited
CC by tropomyosin. {ECO:0000250, ECO:0000269|PubMed:1618806,
CC ECO:0000269|PubMed:3793760}.
CC -!- SUBUNIT: Monomer. Homodimer (By similarity). Associates with F-actin;
CC the association with F-actin is inhibited by tropomyosin.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:3793760}. Cell projection, microvillus
CC {ECO:0000269|PubMed:3793760}. Cell projection, lamellipodium
CC {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cell projection,
CC filopodium tip {ECO:0000250}. Cell projection, filopodium
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in epithelial cells.
CC Component of brush border microvilli. {ECO:0000269|PubMed:3793760}.
CC -!- DOMAIN: Consists of a large core fragment in the N-terminal portion and
CC a small headpiece (HP) in the C-terminal portion. The core fragment is
CC necessary for both actin-nucleating and -severing activities, whereas
CC the HP binds F-actin strongly in both the presence and absence of
CC calcium and is necessary in actin-bundling activity. The Gelsolin-like
CC 1 repeat is necessary for the actin-capping activity. The entire core
CC fragment is necessary for the actin-severing activity (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated on tyrosine residues. The unphosphorylated form
CC increases the initial rate of actin-nucleating activity, whereas the
CC tyrosine-phosphorylated form inhibits actin-nucleating activity,
CC enhances actin-bundling activity and enhances actin-severing activity
CC by reducing high Ca(2+) requirements. The tyrosine-phosphorylated form
CC does not regulate actin-capping activity. Tyrosine phosphorylation is
CC essential for cell migration: tyrosine phosphorylation sites in the N-
CC terminus half regulate actin reorganization and cell morphology,
CC whereas tyrosine phosphorylation sites in the C-terminus half regulate
CC cell migration. Tyrosine phosphorylation is induced by epidermal growth
CC factor (EGF) and stimulates cell migration (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the villin/gelsolin family. {ECO:0000305}.
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DR EMBL; J03781; AAA49133.1; -; mRNA.
DR PIR; A31822; A31822.
DR RefSeq; NP_990773.1; NM_205442.1.
DR PDB; 1QQV; NMR; -; A=760-826.
DR PDB; 1VII; NMR; -; A=792-826.
DR PDB; 1WY3; X-ray; 0.95 A; A=792-826.
DR PDB; 1WY4; X-ray; 1.55 A; A=792-826.
DR PDB; 1YRF; X-ray; 1.07 A; A=792-826.
DR PDB; 1YRI; X-ray; 1.00 A; A=792-826.
DR PDB; 1YU5; X-ray; 1.40 A; X=760-826.
DR PDB; 1YU7; X-ray; 1.50 A; X=760-826.
DR PDB; 1YU8; X-ray; 1.45 A; X=760-826.
DR PDB; 2F4K; X-ray; 1.05 A; A=792-826.
DR PDB; 2JM0; NMR; -; A=792-826.
DR PDB; 2LLF; NMR; -; A=619-725.
DR PDB; 2PPZ; NMR; -; A=792-826.
DR PDB; 2RJV; X-ray; 1.45 A; A=760-826.
DR PDB; 2RJW; X-ray; 1.55 A; A/B=760-826.
DR PDB; 2RJX; X-ray; 1.70 A; A/B=760-826.
DR PDB; 2RJY; X-ray; 1.40 A; A=760-826.
DR PDB; 2VIK; NMR; -; A=2-127.
DR PDB; 2VIL; NMR; -; A=2-127.
DR PDB; 3MYA; X-ray; 2.50 A; A/B=760-826.
DR PDB; 3MYC; X-ray; 1.70 A; A=760-826.
DR PDB; 3MYE; X-ray; 1.80 A; X=760-826.
DR PDB; 3NKJ; X-ray; 1.60 A; A=760-826.
DR PDB; 3TJW; X-ray; 1.46 A; A/B=792-825.
DR PDB; 3TRV; X-ray; 1.00 A; A/B=792-826.
DR PDB; 3TRW; X-ray; 2.10 A; A/D=792-826.
DR PDB; 3TRY; X-ray; 2.30 A; A=792-826.
DR PDB; 4CZ3; NMR; -; A=803-826.
DR PDB; 4CZ4; NMR; -; A=803-826.
DR PDB; 5I1N; X-ray; 1.30 A; A/B/C/D=792-826.
DR PDB; 5I1O; X-ray; 1.35 A; A/B/C/D=792-826.
DR PDB; 5I1P; X-ray; 1.40 A; A/B/C/D=792-826.
DR PDB; 5I1S; X-ray; 1.12 A; A/B=792-826.
DR PDBsum; 1QQV; -.
DR PDBsum; 1VII; -.
DR PDBsum; 1WY3; -.
DR PDBsum; 1WY4; -.
DR PDBsum; 1YRF; -.
DR PDBsum; 1YRI; -.
DR PDBsum; 1YU5; -.
DR PDBsum; 1YU7; -.
DR PDBsum; 1YU8; -.
DR PDBsum; 2F4K; -.
DR PDBsum; 2JM0; -.
DR PDBsum; 2LLF; -.
DR PDBsum; 2PPZ; -.
DR PDBsum; 2RJV; -.
DR PDBsum; 2RJW; -.
DR PDBsum; 2RJX; -.
DR PDBsum; 2RJY; -.
DR PDBsum; 2VIK; -.
DR PDBsum; 2VIL; -.
DR PDBsum; 3MYA; -.
DR PDBsum; 3MYC; -.
DR PDBsum; 3MYE; -.
DR PDBsum; 3NKJ; -.
DR PDBsum; 3TJW; -.
DR PDBsum; 3TRV; -.
DR PDBsum; 3TRW; -.
DR PDBsum; 3TRY; -.
DR PDBsum; 4CZ3; -.
DR PDBsum; 4CZ4; -.
DR PDBsum; 5I1N; -.
DR PDBsum; 5I1O; -.
DR PDBsum; 5I1P; -.
DR PDBsum; 5I1S; -.
DR AlphaFoldDB; P02640; -.
DR BMRB; P02640; -.
DR SMR; P02640; -.
DR DIP; DIP-48339N; -.
DR IntAct; P02640; 1.
DR STRING; 9031.ENSGALP00000037398; -.
DR PaxDb; P02640; -.
DR PRIDE; P02640; -.
DR GeneID; 396423; -.
DR KEGG; gga:396423; -.
DR CTD; 7429; -.
DR VEuPathDB; HostDB:geneid_396423; -.
DR eggNOG; KOG0443; Eukaryota.
DR InParanoid; P02640; -.
DR OrthoDB; 1376537at2759; -.
DR PhylomeDB; P02640; -.
DR EvolutionaryTrace; P02640; -.
DR PRO; PR:P02640; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0032432; C:actin filament bundle; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR GO; GO:0032433; C:filopodium tip; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0005902; C:microvillus; ISS:UniProtKB.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0035727; F:lysophosphatidic acid binding; ISS:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0051693; P:actin filament capping; ISS:UniProtKB.
DR GO; GO:0030042; P:actin filament depolymerization; ISS:UniProtKB.
DR GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0051014; P:actin filament severing; ISS:UniProtKB.
DR GO; GO:0045010; P:actin nucleation; IEA:InterPro.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IBA:GO_Central.
DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0060327; P:cytoplasmic actin-based contraction involved in cell motility; ISS:UniProtKB.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0032233; P:positive regulation of actin filament bundle assembly; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISS:UniProtKB.
DR GO; GO:0051125; P:regulation of actin nucleation; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:2000392; P:regulation of lamellipodium morphogenesis; ISS:UniProtKB.
DR GO; GO:0061041; P:regulation of wound healing; ISS:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; ISS:UniProtKB.
DR DisProt; DP02511; -.
DR Gene3D; 1.10.950.10; -; 1.
DR Gene3D; 3.40.20.10; -; 6.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR036180; Gelsolin-like_dom_sf.
DR InterPro; IPR030007; Villin-1.
DR InterPro; IPR007122; Villin/Gelsolin.
DR InterPro; IPR003128; Villin_headpiece.
DR InterPro; IPR036886; Villin_headpiece_dom_sf.
DR PANTHER; PTHR11977; PTHR11977; 1.
DR PANTHER; PTHR11977:SF35; PTHR11977:SF35; 1.
DR Pfam; PF00626; Gelsolin; 6.
DR Pfam; PF02209; VHP; 1.
DR PRINTS; PR00597; GELSOLIN.
DR SMART; SM00262; GEL; 6.
DR SMART; SM00153; VHP; 1.
DR SUPFAM; SSF47050; SSF47050; 1.
DR SUPFAM; SSF82754; SSF82754; 2.
DR PROSITE; PS51089; HP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin capping; Actin-binding; Calcium; Cell projection;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Reference proteome;
KW Repeat.
FT CHAIN 1..826
FT /note="Villin-1"
FT /id="PRO_0000218730"
FT REPEAT 27..76
FT /note="Gelsolin-like 1"
FT REPEAT 148..188
FT /note="Gelsolin-like 2"
FT REPEAT 265..309
FT /note="Gelsolin-like 3"
FT REPEAT 408..457
FT /note="Gelsolin-like 4"
FT REPEAT 528..568
FT /note="Gelsolin-like 5"
FT REPEAT 631..672
FT /note="Gelsolin-like 6"
FT DOMAIN 760..826
FT /note="HP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00595"
FT REGION 1..734
FT /note="Core"
FT REGION 129..137
FT /note="Crucial for binding an actin filament"
FT REGION 735..826
FT /note="Headpiece"
FT REGION 820..823
FT /note="Absolutely required for activity"
FT BINDING 112..119
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250"
FT BINDING 138..146
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-4,5-bisphosphate)"
FT /ligand_id="ChEBI:CHEBI:58456"
FT /evidence="ECO:0000250"
FT MUTAGEN 138
FT /note="R->A: Reduces the actin-severing activity. Does not
FT affect actin-capping activity."
FT /evidence="ECO:0000269|PubMed:1618806"
FT MUTAGEN 141
FT /note="H->A: Does not reduce the actin-severing activity.
FT Does not affect actin-capping activity."
FT /evidence="ECO:0000269|PubMed:1618806"
FT MUTAGEN 144
FT /note="G->A: Reduces the actin-severing activity. Does not
FT affect actin-capping activity."
FT /evidence="ECO:0000269|PubMed:1618806"
FT MUTAGEN 145
FT /note="K->A: Reduces the actin-severing activity. Does not
FT affect actin-capping activity."
FT /evidence="ECO:0000269|PubMed:1618806"
FT MUTAGEN 146
FT /note="K->A: Reduces the actin-severing activity. Does not
FT affect actin-capping activity."
FT /evidence="ECO:0000269|PubMed:1618806"
FT MUTAGEN 787
FT /note="R->A: Reduces affinity for F-actin."
FT /evidence="ECO:0000269|PubMed:16142894"
FT MUTAGEN 814
FT /note="W->A: Loss of F-actin binding."
FT /evidence="ECO:0000269|PubMed:16142894"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:2VIK"
FT HELIX 9..11
FT /evidence="ECO:0007829|PDB:2VIL"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:2VIK"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:2VIK"
FT TURN 34..38
FT /evidence="ECO:0007829|PDB:2VIK"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:2VIK"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:2VIK"
FT STRAND 55..66
FT /evidence="ECO:0007829|PDB:2VIK"
FT HELIX 72..88
FT /evidence="ECO:0007829|PDB:2VIK"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:2VIK"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:2VIK"
FT HELIX 104..110
FT /evidence="ECO:0007829|PDB:2VIK"
FT STRAND 621..636
FT /evidence="ECO:0007829|PDB:2LLF"
FT STRAND 649..653
FT /evidence="ECO:0007829|PDB:2LLF"
FT STRAND 658..662
FT /evidence="ECO:0007829|PDB:2LLF"
FT STRAND 664..666
FT /evidence="ECO:0007829|PDB:2LLF"
FT HELIX 668..682
FT /evidence="ECO:0007829|PDB:2LLF"
FT HELIX 690..692
FT /evidence="ECO:0007829|PDB:2LLF"
FT STRAND 696..698
FT /evidence="ECO:0007829|PDB:2LLF"
FT HELIX 705..708
FT /evidence="ECO:0007829|PDB:2LLF"
FT STRAND 711..713
FT /evidence="ECO:0007829|PDB:2LLF"
FT HELIX 716..720
FT /evidence="ECO:0007829|PDB:2LLF"
FT TURN 721..723
FT /evidence="ECO:0007829|PDB:2LLF"
FT HELIX 768..772
FT /evidence="ECO:0007829|PDB:1YU5"
FT HELIX 776..778
FT /evidence="ECO:0007829|PDB:1YU5"
FT STRAND 785..787
FT /evidence="ECO:0007829|PDB:1QQV"
FT HELIX 788..791
FT /evidence="ECO:0007829|PDB:1YU5"
FT HELIX 794..801
FT /evidence="ECO:0007829|PDB:1WY3"
FT HELIX 805..810
FT /evidence="ECO:0007829|PDB:1WY3"
FT HELIX 813..823
FT /evidence="ECO:0007829|PDB:1WY3"
SQ SEQUENCE 826 AA; 92479 MW; 6A8898F7DF947389 CRC64;
MVELSKKVTG KLDKTTPGIQ IWRIENMEMV PVPTKSYGNF YEGDCYVLLS TRKTGSGFSY
NIHYWLGKNS SQDEQGAAAI YTTQMDEYLG SVAVQHREVQ GHESETFRAY FKQGLIYKQG
GVASGMKHVE TNTYNVQRLL HVKGKKNVVA AEVEMSWKSF NLGDVFLLDL GQLIIQWNGP
ESNRAERLRA MTLAKDIRDR ERAGRAKVGV VEGENEAASP ELMQALTHVL GEKKNIKAAT
PDEQVHQALN SALKLYHVSD ASGNLVIQEV AIRPLTQDML QHEDCYILDQ AGLKIFVWKG
KNANKEEKQQ AMSRALGFIK AKNYLASTSV ETENDGSESA VFRQLFQKWT VPNQTSGLGK
THTVGKVAKV EQVKFDATTM HVKPEVAAQQ KMVDDGSGEA EVWRVENQEL VPVEKRWLGH
FYGGDCYLVL YTYYVGPKVN RIIYIWQGRH ASTDELAASA YQAVFLDQKY NNEPVQVRVT
MGKEPAHLMA IFKGKMVVYE NGSSRAGGTE PASSTRLFHV HGTNEYNTKA FEVPVRAASL
NSNDVFVLKT PSSCYLWYGK GCSGDEREMG KMVADIISKT EKPVVAEGQE PPEFWVALGG
KTSYANSKRL QEENPSVPPR LFECSNKTGR FLATEIVDFT QDDLDENDVY LLDTWDQIFF
WIGKGANESE KEAAAETAQE YLRSHPGSRD LDTPIIVVKQ GFEPPTFTGW FMAWDPLCWS
DRKSYDELKA ELGDNASIGQ LVSGLTSKNE VFTATTTLVP TKLETFPLDV LVNTAAEDLP
RGVDPSRKEN HLSDEDFKAV FGMTRSAFAN LPLWKQQNLK KEKGLF
