P230_PLAF7
ID P230_PLAF7 Reviewed; 3135 AA.
AC P68874; A0A143ZY09; Q08372;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Gametocyte surface protein P230;
DE Flags: Precursor;
GN Name=PFS230; Synonyms=PF230, S230; ORFNames=PF3D7_0209000;
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bhatti S., Alano P., Luo C., Hansra S., Aikawa M., Carter R., Elliott J.F.;
RT "Gene cloning of a large Plasmodium falciparum sexual stage surface
RT antigen.";
RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=9804551; DOI=10.1126/science.282.5391.1126;
RA Gardner M.J., Tettelin H., Carucci D.J., Cummings L.M., Aravind L.,
RA Koonin E.V., Shallom S.J., Mason T., Yu K., Fujii C., Pederson J., Shen K.,
RA Jing J., Aston C., Lai Z., Schwartz D.C., Pertea M., Salzberg S.L.,
RA Zhou L., Sutton G.G., Clayton R., White O., Smith H.O., Fraser C.M.,
RA Adams M.D., Venter J.C., Hoffman S.L.;
RT "Chromosome 2 sequence of the human malaria parasite Plasmodium
RT falciparum.";
RL Science 282:1126-1132(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
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 [4]
RP INTERACTION WITH PF45/48, AND DEVELOPMENTAL STAGE.
RX PubMed=1380124; DOI=10.1016/0166-6851(92)90013-a;
RA Kumar N., Wizel B.;
RT "Further characterization of interactions between gamete surface antigens
RT of Plasmodium falciparum.";
RL Mol. Biochem. Parasitol. 53:113-120(1992).
RN [5]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=8813686; DOI=10.1016/s0166-6851(96)02621-7;
RA Williamson K.C., Fujioka H., Aikawa M., Kaslow D.C.;
RT "Stage-specific processing of Pfs230, a Plasmodium falciparum transmission-
RT blocking vaccine candidate.";
RL Mol. Biochem. Parasitol. 78:161-169(1996).
RN [6]
RP REVIEW.
RX PubMed=14521577; DOI=10.1046/j.1365-3024.2003.00643.x;
RA Williamson K.C.;
RT "Pfs230: from malaria transmission-blocking vaccine candidate toward
RT function.";
RL Parasite Immunol. 25:351-359(2003).
RN [7]
RP 3D-STRUCTURE MODELING.
RX PubMed=16155126; DOI=10.1073/pnas.0502378102;
RA Gerloff D.L., Creasey A., Maslau S., Carter R.;
RT "Structural models for the protein family characterized by gamete surface
RT protein Pfs230 of Plasmodium falciparum.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13598-13603(2005).
RN [8]
RP FUNCTION.
RX PubMed=16879650; DOI=10.1111/j.1365-2958.2006.05284.x;
RA Eksi S., Czesny B., van Gemert G.J., Sauerwein R.W., Eling W.,
RA Williamson K.C.;
RT "Malaria transmission-blocking antigen, Pfs230, mediates human red blood
RT cell binding to exflagellating male parasites and oocyst production.";
RL Mol. Microbiol. 61:991-998(2006).
RN [9] {ECO:0007744|PDB:6OHG}
RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 542-736 OF MUTANT GLU-585 AND IN
RP COMPLEX WITH ANTIBODY, BIOTECHNOLOGY, AND DISULFIDE BONDS.
RX PubMed=32709983; DOI=10.1038/s42003-020-01123-9;
RA Singh K., Burkhardt M., Nakuchima S., Herrera R., Muratova O., Gittis A.G.,
RA Kelnhofer E., Reiter K., Smelkinson M., Veltri D., Swihart B.J.,
RA Shimp R. Jr., Nguyen V., Zhang B., MacDonald N.J., Duffy P.E.,
RA Garboczi D.N., Narum D.L.;
RT "Structure and function of a malaria transmission blocking vaccine
RT targeting Pfs230 and Pfs230-Pfs48/45 proteins.";
RL Commun. Biol. 3:395-395(2020).
RN [10] {ECO:0007744|PDB:7JUM}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 542-736 OF MUTANT GLU-585 AND IN
RP COMPLEX WITH ANTIBODY, BIOTECHNOLOGY, AND DISULFIDE BONDS.
RX PubMed=33741942; DOI=10.1038/s41467-021-21955-1;
RA Coelho C.H., Tang W.K., Burkhardt M., Galson J.D., Muratova O.,
RA Salinas N.D., Alves E Silva T.L., Reiter K., MacDonald N.J., Nguyen V.,
RA Herrera R., Shimp R., Narum D.L., Byrne-Steele M., Pan W., Hou X.,
RA Brown B., Eisenhower M., Han J., Jenkins B.J., Doritchamou J.Y.A.,
RA Smelkinson M.G., Vega-Rodriguez J., Trueck J., Taylor J.J., Sagara I.,
RA Renn J.P., Tolia N.H., Duffy P.E.;
RT "A human monoclonal antibody blocks malaria transmission and defines a
RT highly conserved neutralizing epitope on gametes.";
RL Nat. Commun. 12:1750-1750(2021).
CC -!- FUNCTION: Gametocyte surface protein required for male/female gamete
CC fusion. Also required for male gamete exflagellation and interaction
CC with host erythrocytes. {ECO:0000269|PubMed:16879650}.
CC -!- SUBUNIT: Heterodimer; heterodimerizes with PF45/48.
CC {ECO:0000269|PubMed:1380124}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:8813686}. Cell
CC membrane {ECO:0000269|PubMed:8813686}; Peripheral membrane protein
CC {ECO:0000305}; Extracellular side {ECO:0000250|UniProtKB:P68875}.
CC -!- DEVELOPMENTAL STAGE: Specifically expressed in gametocytes and gametes
CC (at protein level). {ECO:0000269|PubMed:1380124,
CC ECO:0000269|PubMed:8813686}.
CC -!- PTM: May be processed into a 310 kDa form as the parasite emerges from
CC the host erythrocytes. {ECO:0000269|PubMed:8813686}.
CC -!- BIOTECHNOLOGY: Promising transmission-blocking vaccine candidate:
CC targeting the protein would prevents transmission of the parasite
CC decreasing the malaria burden (PubMed:32709983, PubMed:33741942). The
CC LMIV230-01 transmission-blocking antibody against the 6-Cys domain 1
CC also binds to the heterologous P.falciparum Malian isolate 20-2217-0
CC which carries a 'Ser-605' polymorphism and to the heterologous St Lucia
CC strain which carries 'Ser-605' and 'Asn-661' polymorphisms
CC (PubMed:33741942). {ECO:0000269|PubMed:32709983,
CC ECO:0000269|PubMed:33741942}.
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DR EMBL; L04162; AAA57559.1; -; mRNA.
DR EMBL; LN999943; CZT98104.1; -; Genomic_DNA.
DR PIR; A48584; A48584.
DR RefSeq; XP_001349600.1; XM_001349564.1.
DR PDB; 6OHG; X-ray; 2.38 A; A=542-736.
DR PDB; 7JUM; X-ray; 2.00 A; A/B/C=542-736.
DR PDBsum; 6OHG; -.
DR PDBsum; 7JUM; -.
DR SMR; P68874; -.
DR STRING; 5833.PFB0405w; -.
DR PRIDE; P68874; -.
DR ABCD; P68874; 1 sequenced antibody.
DR EnsemblProtists; CZT98104; CZT98104; PF3D7_0209000.
DR GeneID; 812682; -.
DR KEGG; pfa:PF3D7_0209000; -.
DR VEuPathDB; PlasmoDB:PF3D7_0209000; -.
DR HOGENOM; CLU_227531_0_0_1; -.
DR InParanoid; P68874; -.
DR OMA; KEYVCDF; -.
DR PhylomeDB; P68874; -.
DR Proteomes; UP000001450; Chromosome 2.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 2.60.40.2860; -; 9.
DR InterPro; IPR010884; 6_CYS_dom.
DR InterPro; IPR038160; 6_CYS_dom_sf.
DR Pfam; PF07422; s48_45; 7.
DR SMART; SM00970; s48_45; 9.
DR PROSITE; PS51701; 6_CYS; 14.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein; Malaria;
KW Membrane; Reference proteome; Repeat; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..3135
FT /note="Gametocyte surface protein P230"
FT /id="PRO_0000024617"
FT DOMAIN 589..730
FT /note="6-Cys 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DOMAIN 733..887
FT /note="6-Cys 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DOMAIN 918..1133
FT /note="6-Cys 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DOMAIN 1136..1275
FT /note="6-Cys 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DOMAIN 1285..1432
FT /note="6-Cys 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DOMAIN 1435..1560
FT /note="6-Cys 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DOMAIN 1694..1907
FT /note="6-Cys 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DOMAIN 1910..2035
FT /note="6-Cys 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DOMAIN 2052..2199
FT /note="6-Cys 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DOMAIN 2204..2374
FT /note="6-Cys 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DOMAIN 2448..2663
FT /note="6-Cys 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DOMAIN 2666..2827
FT /note="6-Cys 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DOMAIN 2831..2979
FT /note="6-Cys 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DOMAIN 2982..3113
FT /note="6-Cys 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT REGION 266..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2410..2432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..323
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..347
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..443
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 585
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 821
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 829
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 889
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 961
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1079
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1089
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1508
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1621
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1624
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1753
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1804
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1882
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1920
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1954
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1972
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2504
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2586
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2611
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2650
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2677
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2688
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2952
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3011
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3016
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3066
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3093
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3096
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 593..611
FT /evidence="ECO:0000269|PubMed:32709983,
FT ECO:0000269|PubMed:33741942, ECO:0007744|PDB:6OHG,
FT ECO:0007744|PDB:7JUM"
FT DISULFID 626..706
FT /evidence="ECO:0000269|PubMed:32709983,
FT ECO:0000269|PubMed:33741942, ECO:0007744|PDB:6OHG,
FT ECO:0007744|PDB:7JUM"
FT DISULFID 737..781
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DISULFID 804..862
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DISULFID 1140..1161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DISULFID 1175..1251
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DISULFID 1200..1249
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DISULFID 1439..1459
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DISULFID 1473..1534
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DISULFID 1483..1532
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DISULFID 1698..1726
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DISULFID 1740..1881
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DISULFID 1914..1938
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DISULFID 1952..2017
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DISULFID 1963..2015
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DISULFID 2056..2074
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DISULFID 2208..2229
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DISULFID 2243..2356
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DISULFID 2254..2354
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DISULFID 2452..2476
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DISULFID 2490..2638
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DISULFID 2670..2706
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DISULFID 2720..2804
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DISULFID 2730..2802
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DISULFID 2986..3010
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DISULFID 3024..3090
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT DISULFID 3035..3088
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01038"
FT TURN 568..571
FT /evidence="ECO:0007829|PDB:7JUM"
FT STRAND 572..574
FT /evidence="ECO:0007829|PDB:6OHG"
FT HELIX 576..578
FT /evidence="ECO:0007829|PDB:7JUM"
FT STRAND 579..583
FT /evidence="ECO:0007829|PDB:7JUM"
FT STRAND 585..587
FT /evidence="ECO:0007829|PDB:7JUM"
FT STRAND 590..594
FT /evidence="ECO:0007829|PDB:7JUM"
FT TURN 596..599
FT /evidence="ECO:0007829|PDB:7JUM"
FT STRAND 602..605
FT /evidence="ECO:0007829|PDB:6OHG"
FT STRAND 608..615
FT /evidence="ECO:0007829|PDB:7JUM"
FT STRAND 617..619
FT /evidence="ECO:0007829|PDB:6OHG"
FT STRAND 621..625
FT /evidence="ECO:0007829|PDB:7JUM"
FT TURN 633..638
FT /evidence="ECO:0007829|PDB:7JUM"
FT STRAND 640..643
FT /evidence="ECO:0007829|PDB:7JUM"
FT TURN 644..648
FT /evidence="ECO:0007829|PDB:7JUM"
FT STRAND 649..654
FT /evidence="ECO:0007829|PDB:7JUM"
FT STRAND 657..662
FT /evidence="ECO:0007829|PDB:7JUM"
FT HELIX 663..666
FT /evidence="ECO:0007829|PDB:7JUM"
FT STRAND 674..676
FT /evidence="ECO:0007829|PDB:7JUM"
FT STRAND 679..682
FT /evidence="ECO:0007829|PDB:7JUM"
FT HELIX 683..685
FT /evidence="ECO:0007829|PDB:7JUM"
FT STRAND 687..691
FT /evidence="ECO:0007829|PDB:7JUM"
FT STRAND 700..707
FT /evidence="ECO:0007829|PDB:7JUM"
FT STRAND 720..727
FT /evidence="ECO:0007829|PDB:7JUM"
SQ SEQUENCE 3135 AA; 363218 MW; BE5F850C87ED9C77 CRC64;
MKKIITLKNL FLIILVYIFS EKKDLRCNVI KGNNIKDDED KRFHLFYYSH NLFKTPETKE
KKNKKECFYK NGGIYNLSKE IRMRKDTSVK IKQRTCPFHK EGSSFEMGSK NITCFYPIVG
KKERKTLDTI IIKKNVTNDH VVSSDMHSNV QEKNMILIRN IDKENKNDIQ NVEEKIQRDT
YENKDYESDD TLIEWFDDNT NEENFLLTFL KRCLMKIFSS PKRKKTVVQK KHKSNFFINS
SLKYIYMYLT PSDSFNLVRR NRNLDEEDMS PRDNFVIDDE EEEEEEEEEE EEEEEEEEEE
EEEEYDDYVY EESGDETEEQ LQEEHQEEVG AESSEESFND EDEDSVEARD GDMIRVDEYY
EDQDGDTYDS TIKNEDVDEE VGEEVGEEVG EEVGEEVGEE VGEEVGEEVG EEVGEEEGEE
VGEGVGEEVG EEEGEEVGEE EGEYVDEKER QGEIYPFGDE EEKDEGGESF TYEKSEVDKT
DLFKFIEGGE GDDVYKVDGS KVLLDDDTIS RVSKKHTARD GEYGEYGEAV EDGENVIKII
RSVLQSGALP SVGVDELDKI DLSYETTESG DTAVSEDSYD KYASNNTNKE YVCDFTDQLK
PTESGPKVKK CEVKVNEPLI KVKIICPLKG SVEKLYDNIE YVPKKSPYVV LTKEETKLKE
KLLSKLIYGL LISPTVNEKE NNFKEGVIEF TLPPVVHKAT VFYFICDNSK TEDDNKKGNR
GIVEVYVEPY GNKINGCAFL DEDEEEEKYG NQIEEDEHNE KIKMKTFFTQ NIYKKNNIYP
CYMKLYSGDI GGILFPKNIK STTCFEEMIP YNKEIKWNKE NKSLGNLVNN SVVYNKEMNA
KYFNVQYVHI PTSYKDTLNL FCSIILKEEE SNLISTSYLV YVSINEELNF SLFDFYESFV
PIKKTIQVAQ KNVNNKEHDY TCDFTDKLDK TVPSTANGKK LFICRKHLKE FDTFTLKCNV
NKTQYPNIEI FPKTLKDKKE VLKLDLDIQY QMFSKFFKFN TQNAKYLNLY PYYLIFPFNH
IGKKELKNNP TYKNHKDVKY FEQSSVLSPL SSADSLGKLL NFLDTQETVC LTEKIRYLNL
SINELGSDNN TFSVTFQVPP YIDIKEPFYF MFGCNNNKGE GNIGIVELLI SKQEEKIKGC
NFHESKLDYF NENISSDTHE CTLHAYENDI IGFNCLETTH PNEVEVEVED AEIYLQPENC
FNNVYKGLNS VDITTILKNA QTYNINNKKT PTFLKIPPYN LLEDVEISCQ CTIKQVVKKI
KVIITKNDTV LLKREVQSES TLDDKIYKCE HENFINPRVN KTFDENVEYT CNIKIENFFN
YIQIFCPAKD LGIYKNIQMY YDIVKPTRVP QFKKFNNEEL HKLIPNSEML HKTKEMLILY
NEEKVDLLHF YVFLPIYIKD IYEFNIVCDN SKTMWKNQLG GKVIYHITVS KREQKVKGCS
FDNEHAHMFS YNKTNVKNCI IDAKPKDLIG FVCPSGTLKL TNCFKDAIVH TNLTNINGIL
YLKNNLANFT YKHQFNYMEI PALMDNDISF KCICVDLKKK KYNVKSPLGP KVLRALYKKL
NIKFDNYVTG TDQNKYLMTY MDLHLSHKRN YLKELFHDLG KKKPADTDAN PESIIESLSI
NESNESGPFP TGDVDAEHLI LEGYDTWESL YDEQLEEVIY NDIESLELKD IEQYVLQVNL
KAPKLMMSAQ IHNNRHVCDF SKNNLIVPES LKKKEELGGN PVNIHCYALL KPLDTLYVKC
PTSKDNYEAA KVNISENDNE YELQVISLIE KRFHNFETLE SKKPGNGDVV VHNGVVDTGP
VLDNSTFEKY FKNIKIKPDK FFEKVINEYD DTEEEKDLES ILPGAIVSPM KVLKKKDPFT
SYAAFVVPPI VPKDLHFKVE CNNTEYKDEN QYISGYNGII HIDISNSNRK INGCDFSTNN
SSILTSSVKL VNGETKNCEI NINNNEVFGI ICDNETNLDP EKCFHEIYSK DNKTVKKFRE
VIPNIDIFSL HNSNKKKVAY AKVPLDYINK LLFSCSCKTS HTNTIGTMKV TLNKDEKEEE
DFKTAQGIKH NNVHLCNFFD NPELTFDNNK IVLCKIDAEL FSEVIIQLPI FGTKNVEEGV
QNEEYKKFSL KPSLVFDDNN NDIKVIGKEK NEVSISLALK GVYGNRIFTF DKNGKKGEGI
SFFIPPIKQD TDLKFIINET IDNSNIKQRG LIYIFVRKNV SENSFKLCDF TTGSTSLMEL
NSQVKEKKCT VKIKKGDIFG LKCPKGFAIF PQACFSNVLL EYYKSDYEDS EHINYYIHKD
KKYNLKPKDV IELMDENFRE LQNIQQYTGI SNITDVLHFK NFNLGNLPLN FKNHYSTAYA
KVPDTFNSII NFSCNCYNPE KHVYGTMQVE SDNRNFDNIK KNENVIKNFL LPNIEKYALL
LDDEERQKKI KQQQEEEQQE QILKDQDDRL SRHDDYNKNH TYILYDSNEH ICDYEKNESL
ISTLPNDTKK IQKSICKINA KALDVVTIKC PHTKNFTPKD YFPNSSLITN DKKIVITFDK
KNFVTYIDPT KKTFSLKDIY IQSFYGVSLD HLNQIKKIHE EWDDVHLFYP PHNVLHNVVL
NNHIVNLSSA LEGVLFMKSK VTGDETATKK NTTLPTDGVS SILIPPYVKE DITFHLFCGK
STTKKPNKKN TSLALIHIHI SSNRNIIHGC DFLYLENQTN DAISNNNNNS YSIFTHNKNT
ENNLICDISL IPKTVIGIKC PNKKLNPQTC FDEVYYVKQE DVPSKTITAD KYNTFSKDKI
GNILKNAISI NNPDEKDNTY TYLILPEKFE EELIDTKKVL ACTCDNKYII HMKIEKSTMD
KIKIDEKKTI GKDICKYDVT TKVATCEIID TIDSSVLKEH HTVHYSITLS RWDKLIIKYP
TNEKTHFENF FVNPFNLKDK VLYNYNKPIN IEHILPGAIT TDIYDTRTKI KQYILRIPPY
VHKDIHFSLE FNNSLSLTKQ NQNIIYGNVA KIFIHINQGY KEIHGCDFTG KYSHLFTYSK
KPLPNDDDIC NVTIGNNTFS GFACLSHFEL KPNNCFSSVY DYNEANKVKK LFDLSTKVEL
DHIKQNTSGY TLSYIIFNKE STKLKFSCTC SSNYSNYTIR ITFDPNYIIP EPQSRAIIKY
VDLQDKNFAK YLRKL
