CYRPA_PLAF7
ID CYRPA_PLAF7 Reviewed; 362 AA.
AC Q8IFM8;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Cysteine-rich protective antigen {ECO:0000303|PubMed:22593616};
DE AltName: Full=Inactive sialidase CyRPA {ECO:0000305|PubMed:28195530};
DE Flags: Precursor;
GN Name=CyRPA {ECO:0000303|PubMed:22593616};
GN Synonyms=pfd1130w {ECO:0000303|PubMed:22593616};
GN ORFNames=PF3D7_0423800 {ECO:0000312|EMBL:CAD49272.1};
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329 {ECO:0000312|Proteomes:UP000001450};
RN [1] {ECO:0000312|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450};
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [2] {ECO:0000312|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450};
RX PubMed=12368867; DOI=10.1038/nature01095;
RA Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M.,
RA Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D.,
RA Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N.,
RA Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P.,
RA Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M.,
RA Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL Nature 419:527-531(2002).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND BIOTECHNOLOGY.
RX PubMed=22593616; DOI=10.4049/jimmunol.1103177;
RA Dreyer A.M., Matile H., Papastogiannidis P., Kamber J., Favuzza P.,
RA Voss T.S., Wittlin S., Pluschke G.;
RT "Passive immunoprotection of Plasmodium falciparum-infected mice designates
RT the CyRPA as candidate malaria vaccine antigen.";
RL J. Immunol. 188:6225-6237(2012).
RN [4] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE PFRH5 ADHESION COMPLEX, SUBCELLULAR
RP LOCATION, DEVELOPMENTAL STAGE, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP BIOTECHNOLOGY.
RX PubMed=25583518; DOI=10.1073/pnas.1415466112;
RA Reddy K.S., Amlabu E., Pandey A.K., Mitra P., Chauhan V.S., Gaur D.;
RT "Multiprotein complex between the GPI-anchored CyRPA with PfRH5 and PfRipr
RT is crucial for Plasmodium falciparum erythrocyte invasion.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:1179-1184(2015).
RN [5] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE PFRH5 ADHESION COMPLEX, SUBCELLULAR
RP LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=27374406; DOI=10.1016/j.chom.2016.06.004;
RA Volz J.C., Yap A., Sisquella X., Thompson J.K., Lim N.T., Whitehead L.W.,
RA Chen L., Lampe M., Tham W.H., Wilson D., Nebl T., Marapana D., Triglia T.,
RA Wong W., Rogers K.L., Cowman A.F.;
RT "Essential Role of the PfRh5/PfRipr/CyRPA Complex during Plasmodium
RT falciparum Invasion of Erythrocytes.";
RL Cell Host Microbe 20:60-71(2016).
RN [6]
RP FUNCTION, AND IDENTIFICATION IN THE PFRH5 ADHESION COMPLEX.
RX PubMed=28186186; DOI=10.1038/ncomms14333;
RA Galaway F., Drought L.G., Fala M., Cross N., Kemp A.C., Rayner J.C.,
RA Wright G.J.;
RT "P113 is a merozoite surface protein that binds the N terminus of
RT Plasmodium falciparum RH5.";
RL Nat. Commun. 8:14333-14333(2017).
RN [7] {ECO:0007744|PDB:5TIH, ECO:0007744|PDB:5TIK}
RP X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 30-362, FUNCTION, LACK OF
RP SIALIDASE ACTIVITY, INTERACTION WITH RH5, BIOTECHNOLOGY, AND DISULFIDE
RP BONDS.
RX PubMed=28195530; DOI=10.7554/elife.21347;
RA Chen L., Xu Y., Wong W., Thompson J.K., Healer J., Goddard-Borger E.D.,
RA Lawrence M.C., Cowman A.F.;
RT "Structural basis for inhibition of erythrocyte invasion by antibodies to
RT Plasmodium falciparum protein CyRPA.";
RL Elife 6:0-0(2017).
RN [8] {ECO:0007744|PDB:5EZN, ECO:0007744|PDB:5EZO}
RP X-RAY CRYSTALLOGRAPHY (3.63 ANGSTROMS) OF 31-362, FUNCTION, LACK OF
RP SIALIDASE ACTIVITY, BIOTECHNOLOGY, GLYCOSYLATION, DISULFIDE BONDS, AND
RP MUTAGENESIS OF ASP-66; ASN-145; ASN-322 AND ASN-338.
RX PubMed=28195038; DOI=10.7554/elife.20383;
RA Favuzza P., Guffart E., Tamborrini M., Scherer B., Dreyer A.M., Rufer A.C.,
RA Erny J., Hoernschemeyer J., Thoma R., Schmid G., Gsell B., Lamelas A.,
RA Benz J., Joseph C., Matile H., Pluschke G., Rudolph M.G.;
RT "Structure of the malaria vaccine candidate antigen CyRPA and its complex
RT with a parasite invasion inhibitory antibody.";
RL Elife 6:0-0(2017).
RN [9] {ECO:0007744|PDB:6MPV}
RP STRUCTURE BY ELECTRON MICROSCOPY (7.17 ANGSTROMS) OF 31-362 IN COMPLEX WITH
RP RH5 AND RIPR, FUNCTION, IDENTIFICATION IN THE PFRH5 ADHESION COMPLEX,
RP SUBCELLULAR LOCATION, AND DISULFIDE BONDS.
RX PubMed=30542156; DOI=10.1038/s41586-018-0779-6;
RA Wong W., Huang R., Menant S., Hong C., Sandow J.J., Birkinshaw R.W.,
RA Healer J., Hodder A.N., Kanjee U., Tonkin C.J., Heckmann D., Soroka V.,
RA Sogaard T.M.M., Jorgensen T., Duraisingh M.T., Czabotar P.E.,
RA de Jongh W.A., Tham W.H., Webb A.I., Yu Z., Cowman A.F.;
RT "Structure of Plasmodium falciparum Rh5-CyRPA-Ripr invasion complex.";
RL Nature 565:118-121(2019).
CC -!- FUNCTION: Essential for the invasion of host erythrocytes by blood
CC stage merozoites (PubMed:22593616, PubMed:25583518, PubMed:27374406,
CC PubMed:28195530, PubMed:28195038). Required for the assembly of the
CC PfRH5 adhesion complex (or invasion complex) composed of CyRPA, RH5 and
CC RIPR at the interface between the merozoite and the host erythrocyte
CC membranes (PubMed:25583518, PubMed:28186186, PubMed:28195530,
CC PubMed:28195038, PubMed:30542156). This facilitates the binding of RH5
CC to host receptor BSG/basigin, which leads to the establishment of a
CC tight junction between the merozoite and host erythrocyte membranes and
CC allows Ca(2+) release into the erythrocyte (PubMed:27374406,
CC PubMed:28186186, PubMed:30542156). {ECO:0000269|PubMed:22593616,
CC ECO:0000269|PubMed:25583518, ECO:0000269|PubMed:27374406,
CC ECO:0000269|PubMed:28186186, ECO:0000269|PubMed:28195038,
CC ECO:0000269|PubMed:28195530, ECO:0000269|PubMed:30542156}.
CC -!- SUBUNIT: Component of the PfRH5 adhesion complex composed of 1 copy of
CC CyRPA, RH5 and RIPR; the complex is formed during merozoite invasion of
CC host erythrocytes specifically at the interface between the parasite
CC and host membranes (PubMed:25583518, PubMed:27374406, PubMed:30542156).
CC Following the establishment of the junction between the merozoite and
CC the erythrocyte, CyRPA dissociates from the complex (PubMed:30542156).
CC Within the complex, interacts with RH5 and RIPR (PubMed:28195530,
CC PubMed:30542156). CyRPA recruits RIPR to RH5-P113-BSG complex; the
CC formation of the PfRH5 adhesion complex increases the affinity of RH5
CC for BSG and probably leads to the release of RH5 from P113 while
CC maintaining the interaction of the PfRH5 adhesion complex with BSG
CC (PubMed:28186186, PubMed:30542156). {ECO:0000269|PubMed:25583518,
CC ECO:0000269|PubMed:27374406, ECO:0000269|PubMed:28186186,
CC ECO:0000269|PubMed:28195530, ECO:0000269|PubMed:30542156}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25583518}.
CC Cytoplasmic vesicle, secretory vesicle, microneme lumen
CC {ECO:0000269|PubMed:25583518}. Cell membrane
CC {ECO:0000269|PubMed:22593616, ECO:0000269|PubMed:25583518}; Peripheral
CC membrane protein {ECO:0000269|PubMed:22593616,
CC ECO:0000269|PubMed:25583518}; Extracellular side
CC {ECO:0000269|PubMed:22593616, ECO:0000269|PubMed:25583518}. Host cell
CC membrane {ECO:0000269|PubMed:25583518, ECO:0000269|PubMed:27374406,
CC ECO:0000269|PubMed:30542156}. Note=In late schizonts, colocalizes with
CC RIPR in the microneme lumen (PubMed:22593616, PubMed:25583518,
CC PubMed:27374406). During merozoite invasion of host erythrocytes,
CC secreted at the merozoite apical surface where it colocalizes with RIPR
CC and RH5 at the interface between the merozoite and the erythrocyte
CC (PubMed:25583518, PubMed:27374406). {ECO:0000269|PubMed:22593616,
CC ECO:0000269|PubMed:25583518, ECO:0000269|PubMed:27374406}.
CC -!- DEVELOPMENTAL STAGE: Expressed during parasite asexual blood stages,
CC specifically at the schizont stage, in free merozoites, and at the very
CC early ring stage but not in late ring and early trophozoite stages (at
CC protein level). {ECO:0000269|PubMed:22593616,
CC ECO:0000269|PubMed:25583518, ECO:0000269|PubMed:27374406}.
CC -!- PTM: N-glycosylated. {ECO:0000305|PubMed:28195038}.
CC -!- DISRUPTION PHENOTYPE: Conditional knockdown causes loss of cell growth
CC and severely impairs merozoite invasion of erythrocytes. Attachment to
CC and deformation of erythrocyte membrane is normal, however the
CC subsequent step, which triggers an increase in Ca(2+) from the attached
CC merozoite into the erythrocyte, is impaired.
CC {ECO:0000269|PubMed:27374406}.
CC -!- BIOTECHNOLOGY: Potential candidate for the development of parasite
CC blood stage vaccines. In vitro and in vivo, induces neutralizing
CC antibodies capable of inhibiting merozoite invasion of host
CC erythrocytes. {ECO:0000269|PubMed:22593616,
CC ECO:0000269|PubMed:25583518, ECO:0000269|PubMed:28195038,
CC ECO:0000269|PubMed:28195530}.
CC -!- CAUTION: CyRPA was thought to be GPI-anchored to the merozoite membrane
CC (PubMed:25583518). However, a subsequent report shows that this was not
CC the case (PubMed:27374406). {ECO:0000269|PubMed:25583518,
CC ECO:0000269|PubMed:27374406}.
CC -!- CAUTION: CyRPA shares structural homology with sialidases, however the
CC 3 conserved arginine residues involved in substrate binding and the
CC nucleophilic tyrosine residue are not conserved. Does not have
CC sialidase/neuraminidase activity in vitro.
CC {ECO:0000269|PubMed:28195038, ECO:0000269|PubMed:28195530}.
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DR EMBL; AL844503; CAD49272.1; -; Genomic_DNA.
DR RefSeq; XP_001351541.1; XM_001351505.1.
DR PDB; 5EZN; X-ray; 2.51 A; A=32-185, B=32-192, E=189-362, G=193-362.
DR PDB; 5EZO; X-ray; 3.63 A; A=31-362.
DR PDB; 5TIH; X-ray; 2.44 A; A=30-362.
DR PDB; 5TIK; X-ray; 3.09 A; A/B/C/D=30-362.
DR PDB; 6MPV; EM; 7.17 A; A=31-362.
DR PDB; 7PHV; X-ray; 3.09 A; A/D=29-362.
DR PDB; 7PHW; X-ray; 2.79 A; A/D=29-362.
DR PDB; 7PI2; X-ray; 3.14 A; A/D/G/J=29-362.
DR PDB; 7PI3; X-ray; 3.27 A; A/H/O/V=29-362.
DR PDB; 7PI7; X-ray; 2.72 A; A/D=29-362.
DR PDBsum; 5EZN; -.
DR PDBsum; 5EZO; -.
DR PDBsum; 5TIH; -.
DR PDBsum; 5TIK; -.
DR PDBsum; 6MPV; -.
DR PDBsum; 7PHV; -.
DR PDBsum; 7PHW; -.
DR PDBsum; 7PI2; -.
DR PDBsum; 7PI3; -.
DR PDBsum; 7PI7; -.
DR AlphaFoldDB; Q8IFM8; -.
DR SMR; Q8IFM8; -.
DR STRING; 5833.PFD1130w; -.
DR PRIDE; Q8IFM8; -.
DR ABCD; Q8IFM8; 2 sequenced antibodies.
DR EnsemblProtists; CAD49272; CAD49272; PF3D7_0423800.
DR GeneID; 812432; -.
DR KEGG; pfa:PF3D7_0423800; -.
DR VEuPathDB; PlasmoDB:PF3D7_0423800; -.
DR HOGENOM; CLU_757557_0_0_1; -.
DR InParanoid; Q8IFM8; -.
DR OMA; ECYLYYT; -.
DR PhylomeDB; Q8IFM8; -.
DR Proteomes; UP000001450; Chromosome 4.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:GeneDB.
DR GO; GO:0045177; C:apical part of cell; IDA:GeneDB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043655; C:host extracellular space; IDA:UniProtKB.
DR GO; GO:0020009; C:microneme; IDA:UniProtKB.
DR GO; GO:0034494; C:microneme lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0044409; P:entry into host; IMP:UniProtKB.
DR InterPro; IPR041396; CyRPA.
DR Pfam; PF18638; CyRPA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasmic vesicle; Disulfide bond;
KW Glycoprotein; Host cell membrane; Host membrane; Membrane;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..362
FT /note="Cysteine-rich protective antigen"
FT /evidence="ECO:0000255"
FT /id="PRO_5004311113"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 48..64
FT /evidence="ECO:0000269|PubMed:28195038,
FT ECO:0000269|PubMed:28195530, ECO:0000269|PubMed:30542156,
FT ECO:0007744|PDB:5EZN, ECO:0007744|PDB:5EZO,
FT ECO:0007744|PDB:5TIH, ECO:0007744|PDB:5TIK"
FT DISULFID 119..133
FT /evidence="ECO:0000269|PubMed:28195038,
FT ECO:0000269|PubMed:28195530, ECO:0000269|PubMed:30542156,
FT ECO:0007744|PDB:5EZN, ECO:0007744|PDB:5EZO,
FT ECO:0007744|PDB:5TIH, ECO:0007744|PDB:5TIK"
FT DISULFID 180..198
FT /evidence="ECO:0000269|PubMed:28195038,
FT ECO:0000269|PubMed:28195530, ECO:0000269|PubMed:30542156,
FT ECO:0007744|PDB:5EZN, ECO:0007744|PDB:5EZO,
FT ECO:0007744|PDB:5TIH, ECO:0007744|PDB:5TIK"
FT DISULFID 258..268
FT /evidence="ECO:0000269|PubMed:28195038,
FT ECO:0000269|PubMed:28195530, ECO:0000269|PubMed:30542156,
FT ECO:0007744|PDB:5EZO, ECO:0007744|PDB:5TIH,
FT ECO:0007744|PDB:5TIK"
FT DISULFID 303..327
FT /evidence="ECO:0000269|PubMed:28195038,
FT ECO:0000269|PubMed:28195530, ECO:0000269|PubMed:30542156,
FT ECO:0007744|PDB:5EZO, ECO:0007744|PDB:5TIH,
FT ECO:0007744|PDB:5TIK"
FT MUTAGEN 66
FT /note="D->K: Prevents the interaction with c2 neutralizing
FT antibodies."
FT /evidence="ECO:0000269|PubMed:28195038"
FT MUTAGEN 145
FT /note="N->D: Loss of N-glycosylation; when associated with
FT D-322 and D-338."
FT /evidence="ECO:0000269|PubMed:28195038"
FT MUTAGEN 322
FT /note="N->D: Loss of N-glycosylation; when associated with
FT D-145 and D-338."
FT /evidence="ECO:0000269|PubMed:28195038"
FT MUTAGEN 338
FT /note="N->D: Loss of N-glycosylation; when associated with
FT D-145 and D-322."
FT /evidence="ECO:0000269|PubMed:28195038"
FT STRAND 33..43
FT /evidence="ECO:0007829|PDB:5TIH"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:5TIH"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:5TIH"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:5EZN"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:5TIH"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:5TIH"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:5TIH"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:5TIH"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:5TIH"
FT STRAND 131..142
FT /evidence="ECO:0007829|PDB:5TIH"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:5TIH"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:5TIH"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:5TIH"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:5TIH"
FT STRAND 174..182
FT /evidence="ECO:0007829|PDB:5TIH"
FT STRAND 194..203
FT /evidence="ECO:0007829|PDB:5TIH"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:5TIH"
FT STRAND 225..233
FT /evidence="ECO:0007829|PDB:5TIH"
FT STRAND 236..244
FT /evidence="ECO:0007829|PDB:5TIH"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:5TIH"
FT STRAND 251..260
FT /evidence="ECO:0007829|PDB:5TIH"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:5TIH"
FT STRAND 278..286
FT /evidence="ECO:0007829|PDB:5TIH"
FT STRAND 289..297
FT /evidence="ECO:0007829|PDB:5TIH"
FT STRAND 301..307
FT /evidence="ECO:0007829|PDB:5TIH"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:5TIH"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:5TIH"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:5EZN"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:5TIH"
FT STRAND 336..347
FT /evidence="ECO:0007829|PDB:5TIH"
FT STRAND 350..360
FT /evidence="ECO:0007829|PDB:5TIH"
SQ SEQUENCE 362 AA; 42776 MW; 07626CFB3A7D6DF8 CRC64;
MIIPFHKKFI SFFQIVLVVL LLCRSINCDS RHVFIRTELS FIKNNVPCIR DMFFIYKREL
YNICLDDLKG EEDETHIYVQ KKVKDSWITL NDLFKETDLT GRPHIFAYVD VEEIIILLCE
DEEFSNRKKD MTCHRFYSND GKEYNNSEIT ISDYILKDKL LSSYVSLPLK IENREYFLIC
GVSPYKFKDD NKKDDILCMA SHDKGETWGT KIVIKYDNYK LGVQYFFLRP YISKNDLSFH
FYVGDNINNV KNVNFIECTH EKDLEFVCSN RDFLKDNKVL QDVSTLNDEY IVSYGNDNNF
AECYIFFNNE NSILIKPEKY GNTTAGCYGG TFVKIDENRT LFIYSSSQGI YNIHTIYYAN
YE
