GRASS_DROME
ID GRASS_DROME Reviewed; 377 AA.
AC Q9VB68; Q86PB3; Q8MR95; Q9VB67;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Serine protease grass {ECO:0000305};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU00274};
DE AltName: Full=Gram-positive specific serine protease {ECO:0000303|PubMed:16631589};
DE Flags: Precursor;
GN Name=grass {ECO:0000303|PubMed:16631589, ECO:0000312|FlyBase:FBgn0039494};
GN Synonyms=c-SP1 {ECO:0000312|FlyBase:FBgn0039494};
GN ORFNames=CG5896 {ECO:0000312|FlyBase:FBgn0039494};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAM52037.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM52037.1};
RC TISSUE=Head {ECO:0000312|EMBL:AAM52037.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000312|EMBL:AAO24994.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAO24994.1};
RC TISSUE=Larva {ECO:0000312|EMBL:AAO24994.1}, and
RC Pupae {ECO:0000312|EMBL:AAO24994.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0007744|PDB:2XXL}
RP PROTEIN SEQUENCE OF 27-30, X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN
RP COMPLEX WITH CALCIUM, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, PROTEOLYTIC
RP CLEAVAGE, GLYCOSYLATION AT ASN-230 AND ASN-270, AND DISULFIDE BONDS.
RX PubMed=21310954; DOI=10.1074/jbc.m110.182741;
RA Kellenberger C., Leone P., Coquet L., Jouenne T., Reichhart J.M.,
RA Roussel A.;
RT "Structure-function analysis of grass clip serine protease involved in
RT Drosophila Toll pathway activation.";
RL J. Biol. Chem. 286:12300-12307(2011).
RN [6] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16631589; DOI=10.1016/j.cub.2006.03.020;
RA Kambris Z., Brun S., Jang I.H., Nam H.J., Romeo Y., Takahashi K., Lee W.J.,
RA Ueda R., Lemaitre B.;
RT "Drosophila immunity: a large-scale in vivo RNAi screen identifies five
RT serine proteases required for Toll activation.";
RL Curr. Biol. 16:808-813(2006).
RN [7] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18724373; DOI=10.1038/ni.1643;
RA El Chamy L., Leclerc V., Caldelari I., Reichhart J.M.;
RT "Sensing of 'danger signals' and pathogen-associated molecular patterns
RT defines binary signaling pathways 'upstream' of Toll.";
RL Nat. Immunol. 9:1165-1170(2008).
CC -!- FUNCTION: Endopeptidase (By similarity). Plays a key role in innate
CC immunity by activating the Toll pathway in response to fungal and Gram-
CC positive bacterial infections, presumably downstream of pattern-
CC recognition receptors (PRR), such as PGRP-SA, GNBP1 and GNBP3, and
CC upstream of spz processing enzyme SPE (PubMed:16631589,
CC PubMed:18724373). {ECO:0000250|UniProtKB:Q9XXV0,
CC ECO:0000269|PubMed:16631589, ECO:0000269|PubMed:18724373}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:21310954}.
CC Note=Probably secreted in the hemolymph. {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B {ECO:0000312|FlyBase:FBgn0039494};
CC IsoId=Q9VB68-1; Sequence=Displayed;
CC Name=A {ECO:0000312|FlyBase:FBgn0039494};
CC IsoId=Q9VB68-2; Sequence=VSP_059329;
CC -!- DOMAIN: The clip domain consists of 35-55 residues which are 'knitted'
CC together usually by 3 conserved disulfide bonds forming a clip-like
CC compact structure. {ECO:0000255|PROSITE-ProRule:PRU01236}.
CC -!- PTM: Proteolytically cleaved by a tryspin-like protease which is likely
CC to activate grass. {ECO:0000269|PubMed:21310954}.
CC -!- DISRUPTION PHENOTYPE: Results in increased susceptibility to fungal or
CC Gram-positive bacterial infection and failure to induce the expression
CC of the Toll pathway-activated antifungal peptide Drs (PubMed:18724373).
CC siRNA-mediated knockdown results in increased susceptibility to Gram-
CC positive bacterial infection and severe reduction in the expression of
CC the antifungal peptide Drs (PubMed:16631589). In a protease psh mutant
CC background, complete loss of Drs induction and increased susceptibility
CC to Gram-positive bacterial infection (PubMed:18724373).
CC {ECO:0000269|PubMed:16631589, ECO:0000269|PubMed:18724373}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01236}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM52037.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014297; AAF56675.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF56676.1; -; Genomic_DNA.
DR EMBL; AY121710; AAM52037.1; ALT_INIT; mRNA.
DR EMBL; BT003238; AAO24994.1; -; mRNA.
DR RefSeq; NP_651543.1; NM_143286.3. [Q9VB68-1]
DR RefSeq; NP_733197.1; NM_170318.3. [Q9VB68-2]
DR PDB; 2XXL; X-ray; 1.80 A; A/B=1-377.
DR PDBsum; 2XXL; -.
DR AlphaFoldDB; Q9VB68; -.
DR SMR; Q9VB68; -.
DR STRING; 7227.FBpp0084482; -.
DR MEROPS; S01.502; -.
DR GlyGen; Q9VB68; 2 sites.
DR iPTMnet; Q9VB68; -.
DR PaxDb; Q9VB68; -.
DR DNASU; 43273; -.
DR EnsemblMetazoa; FBtr0085111; FBpp0084481; FBgn0039494. [Q9VB68-2]
DR EnsemblMetazoa; FBtr0085112; FBpp0084482; FBgn0039494. [Q9VB68-1]
DR GeneID; 43273; -.
DR KEGG; dme:Dmel_CG5896; -.
DR UCSC; CG5896-RA; d. melanogaster.
DR UCSC; CG5896-RB; d. melanogaster. [Q9VB68-1]
DR CTD; 43273; -.
DR FlyBase; FBgn0039494; grass.
DR VEuPathDB; VectorBase:FBgn0039494; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000169352; -.
DR InParanoid; Q9VB68; -.
DR PhylomeDB; Q9VB68; -.
DR BioGRID-ORCS; 43273; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 43273; -.
DR PRO; PR:Q9VB68; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039494; Expressed in second segment of antenna (Drosophila) and 21 other tissues.
DR ExpressionAtlas; Q9VB68; baseline and differential.
DR Genevisible; Q9VB68; DM.
DR GO; GO:0005576; C:extracellular region; HDA:FlyBase.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0017171; F:serine hydrolase activity; HDA:FlyBase.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISM:FlyBase.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR GO; GO:0006963; P:positive regulation of antibacterial peptide biosynthetic process; IGI:FlyBase.
DR GO; GO:0002804; P:positive regulation of antifungal peptide production; IMP:UniProtKB.
DR GO; GO:0045752; P:positive regulation of Toll signaling pathway; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISM:FlyBase.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 3.30.1640.30; -; 1.
DR InterPro; IPR022700; CLIP.
DR InterPro; IPR038565; CLIP_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF12032; CLIP; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00680; CLIP; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS51888; CLIP; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Immunity; Innate immunity;
KW Metal-binding; Protease; Reference proteome; Secreted; Serine protease;
KW Signal; Zymogen.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:21310954"
FT CHAIN 27..377
FT /note="Serine protease grass"
FT /evidence="ECO:0000305|PubMed:21310954"
FT /id="PRO_5004335652"
FT DOMAIN 31..89
FT /note="Clip"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236"
FT DOMAIN 119..373
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 91..118
FT /note="Linker"
FT /evidence="ECO:0000269|PubMed:21310954"
FT ACT_SITE 163
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 223
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 318
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT BINDING 179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:21310954,
FT ECO:0007744|PDB:2XXL"
FT BINDING 181
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:21310954,
FT ECO:0007744|PDB:2XXL"
FT BINDING 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:21310954,
FT ECO:0007744|PDB:2XXL"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:21310954,
FT ECO:0007744|PDB:2XXL"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21310954,
FT ECO:0007744|PDB:2XXL"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21310954,
FT ECO:0007744|PDB:2XXL"
FT DISULFID 32..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236,
FT ECO:0000269|PubMed:21310954, ECO:0007744|PDB:2XXL"
FT DISULFID 42..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236,
FT ECO:0000269|PubMed:21310954, ECO:0007744|PDB:2XXL"
FT DISULFID 48..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01236,
FT ECO:0000269|PubMed:21310954, ECO:0007744|PDB:2XXL"
FT DISULFID 111..243
FT /evidence="ECO:0000269|PubMed:21310954,
FT ECO:0007744|PDB:2XXL"
FT DISULFID 148..164
FT /evidence="ECO:0000269|PubMed:21310954,
FT ECO:0007744|PDB:2XXL"
FT DISULFID 188..197
FT /evidence="ECO:0000269|PubMed:21310954,
FT ECO:0007744|PDB:2XXL"
FT DISULFID 290..304
FT /evidence="ECO:0000269|PubMed:21310954,
FT ECO:0007744|PDB:2XXL"
FT DISULFID 314..349
FT /evidence="ECO:0000269|PubMed:21310954,
FT ECO:0007744|PDB:2XXL"
FT VAR_SEQ 1..42
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000305"
FT /id="VSP_059329"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:2XXL"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:2XXL"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:2XXL"
FT HELIX 49..60
FT /evidence="ECO:0007829|PDB:2XXL"
FT HELIX 67..76
FT /evidence="ECO:0007829|PDB:2XXL"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:2XXL"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:2XXL"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:2XXL"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:2XXL"
FT STRAND 133..139
FT /evidence="ECO:0007829|PDB:2XXL"
FT STRAND 141..154
FT /evidence="ECO:0007829|PDB:2XXL"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:2XXL"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:2XXL"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:2XXL"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:2XXL"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:2XXL"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:2XXL"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:2XXL"
FT STRAND 202..211
FT /evidence="ECO:0007829|PDB:2XXL"
FT TURN 217..220
FT /evidence="ECO:0007829|PDB:2XXL"
FT STRAND 225..231
FT /evidence="ECO:0007829|PDB:2XXL"
FT HELIX 248..253
FT /evidence="ECO:0007829|PDB:2XXL"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:2XXL"
FT STRAND 258..264
FT /evidence="ECO:0007829|PDB:2XXL"
FT STRAND 278..285
FT /evidence="ECO:0007829|PDB:2XXL"
FT HELIX 287..294
FT /evidence="ECO:0007829|PDB:2XXL"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:2XXL"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:2XXL"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:2XXL"
FT STRAND 321..326
FT /evidence="ECO:0007829|PDB:2XXL"
FT STRAND 335..344
FT /evidence="ECO:0007829|PDB:2XXL"
FT STRAND 356..360
FT /evidence="ECO:0007829|PDB:2XXL"
FT HELIX 361..364
FT /evidence="ECO:0007829|PDB:2XXL"
FT HELIX 365..375
FT /evidence="ECO:0007829|PDB:2XXL"
SQ SEQUENCE 377 AA; 41511 MW; 5B953F3D505CBDC4 CRC64;
MMIASSLAVL YGIAIVSSMG VQSARADYAD DCTTPDGDQG QCMPFSSCRT IEERLTEAQK
AGQKVPADYA SYLQKALCGE FNGVRHFCCP SANIQHNSKV MSLFKDENFD CGNFLSQRVS
NGYEVKLSSR PWMALLRYQQ FGESRFLCGG AMISERYILT AAHCVHGLQN DLYEIRLGEH
RISTEEDCRQ QGRKKKCAPP VVNVGIEKHL IHEKYDARHI MHDIALLKLN RSVPFQKHIK
PICLPITDEL KEKAEQISTY FVTGWGTTEN GSSSDVLLQA NVPLQPRSAC SQAYRRAVPL
SQLCVGGGDL QDSCKGDSGG PLQAPAQYLG EYAPKMVEFG IVSQGVVTCG QISLPGLYTN
VGEYVQWITD TMASNGL
