CSP_PLAF7
ID CSP_PLAF7 Reviewed; 397 AA.
AC Q7K740;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Circumsporozoite protein {ECO:0000303|PubMed:27560376};
DE Short=CS {ECO:0000250|UniProtKB:P02893};
DE Short=PfCSP {ECO:0000303|PubMed:27560376};
DE Contains:
DE RecName: Full=Circumsporozoite protein C-terminus {ECO:0000305};
DE Flags: Precursor;
GN Name=CSP {ECO:0000303|PubMed:27560376};
GN ORFNames=PF3D7_0304600 {ECO:0000312|EMBL:CAB38998.2};
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=10448855; DOI=10.1038/22964;
RA Bowman S., Lawson D., Basham D., Brown D., Chillingworth T., Churcher C.M.,
RA Craig A., Davies R.M., Devlin K., Feltwell T., Gentles S., Gwilliam R.,
RA Hamlin N., Harris D., Holroyd S., Hornsby T., Horrocks P., Jagels K.,
RA Jassal B., Kyes S., McLean J., Moule S., Mungall K.L., Murphy L.,
RA Oliver K., Quail M.A., Rajandream M.A., Rutter S., Skelton J., Squares R.,
RA Squares S., Sulston J.E., Whitehead S., Woodward J.R., Newbold C.,
RA Barrell B.G.;
RT "The complete nucleotide sequence of chromosome 3 of Plasmodium
RT falciparum.";
RL Nature 400:532-538(1999).
RN [2] {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 [3] {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 [4] {ECO:0000305}
RP DOMAIN.
RX PubMed=27560376; DOI=10.1371/journal.pone.0161607;
RA Zhao J., Bhanot P., Hu J., Wang Q.;
RT "A Comprehensive Analysis of Plasmodium Circumsporozoite Protein Binding to
RT Hepatocytes.";
RL PLoS ONE 11:e0161607-e0161607(2016).
RN [5] {ECO:0007744|PDB:3VDJ, ECO:0007744|PDB:3VDK}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 310-374, AND DISULFIDE BONDS.
RX PubMed=22547819; DOI=10.1073/pnas.1205737109;
RA Doud M.B., Koksal A.C., Mi L.Z., Song G., Lu C., Springer T.A.;
RT "Unexpected fold in the circumsporozoite protein target of malaria
RT vaccines.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:7817-7822(2012).
RN [6] {ECO:0007744|PDB:6BQB}
RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 95-108 IN COMPLEX WITH ANTIBODY
RP MGG4, FUNCTION, AND BIOTECHNOLOGY.
RX PubMed=29554084; DOI=10.1038/nm.4513;
RA Tan J., Sack B.K., Oyen D., Zenklusen I., Piccoli L., Barbieri S.,
RA Foglierini M., Fregni C.S., Marcandalli J., Jongo S., Abdulla S., Perez L.,
RA Corradin G., Varani L., Sallusto F., Sim B.K.L., Hoffman S.L.,
RA Kappe S.H.I., Daubenberger C., Wilson I.A., Lanzavecchia A.;
RT "A public antibody lineage that potently inhibits malaria infection through
RT dual binding to the circumsporozoite protein.";
RL Nat. Med. 24:401-407(2018).
RN [7] {ECO:0007744|PDB:6MB3, ECO:0007744|PDB:6MHG}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.37 ANGSTROMS) OF 26-383 IN COMPLEX WITH
RP ANTIBODY FAB311, AND REPEATS.
RX PubMed=30324137; DOI=10.1126/sciadv.aau8529;
RA Oyen D., Torres J.L., Cottrell C.A., Richter King C., Wilson I.A.,
RA Ward A.B.;
RT "Cryo-EM structure of P. falciparum circumsporozoite protein with a
RT vaccine-elicited antibody is stabilized by somatically mutated inter-Fab
RT contacts.";
RL Sci. Adv. 4:eaau8529-eaau8529(2018).
RN [8] {ECO:0007744|PDB:6PBV, ECO:0007744|PDB:6PBW}
RP X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 95-108 IN COMPLEX WITH ANTIBODY
RP FAB668, FUNCTION, AND BIOTECHNOLOGY.
RX PubMed=32150583; DOI=10.1371/journal.ppat.1008373;
RA Oyen D., Torres J.L., Aoto P.C., Flores-Garcia Y., Binter S.,
RA Pholcharee T., Carroll S., Reponen S., Wash R., Liang Q., Lemiale F.,
RA Locke E., Bradley A., King C.R., Emerling D., Kellam P., Zavala F.,
RA Ward A.B., Wilson I.A.;
RT "Structure and mechanism of monoclonal antibody binding to the junctional
RT epitope of Plasmodium falciparumcircumsporozoite protein.";
RL PLoS Pathog. 16:e1008373-e1008373(2020).
CC -!- FUNCTION: Essential sporozoite protein (PubMed:29554084,
CC PubMed:32150583). In the mosquito vector, required for sporozoite
CC development in the oocyst, migration through the vector hemolymph and
CC entry into the vector salivary glands (By similarity). In the
CC vertebrate host, required for sporozoite migration through the host
CC dermis and infection of host hepatocytes (PubMed:29554084,
CC PubMed:32150583). Binds to highly sulfated heparan sulfate
CC proteoglycans (HSPGs) on the surface of host hepatocytes (By
CC similarity). {ECO:0000250|UniProtKB:P23093,
CC ECO:0000269|PubMed:29554084, ECO:0000269|PubMed:32150583}.
CC -!- FUNCTION: [Circumsporozoite protein C-terminus]: In the vertebrate
CC host, binds to highly sulfated heparan sulfate proteoglycans (HSPGs) on
CC the surface of host hepatocytes and is required for sporozoite invasion
CC of the host hepatocytes. {ECO:0000250|UniProtKB:P23093}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P19597};
CC Lipid-anchor, GPI-anchor {ECO:0000255}. Cytoplasm
CC {ECO:0000250|UniProtKB:P23093}. Note=Localizes to the cytoplasm and the
CC cell membrane in oocysts at day 6 post infection and then gradually
CC distributes over the entire cell surface of the sporoblast and the
CC budding sporozoites. {ECO:0000250|UniProtKB:P23093}.
CC -!- DOMAIN: The N-terminus is involved in the initial binding to heparan
CC sulfate proteoglycans (HSPGs) on the surface of host hepatocytes
CC (PubMed:27560376). The N-terminus masks the TSP type-1 (TSR) domain
CC which maintains the sporozoites in a migratory state, enabling them to
CC complete their journey to the salivary gland in the mosquito vector and
CC then to the host liver. The unmasking of the TSP type-1 (TSR) domain
CC when the sporozoite interacts with the host hepatocyte also protects
CC sporozoites from host antibodies (By similarity).
CC {ECO:0000250|UniProtKB:P23093, ECO:0000269|PubMed:27560376}.
CC -!- DOMAIN: The TSP type-1 (TSR) domain is required for sporozoite
CC development and invasion. CSP has two conformational states, an
CC adhesive conformation in which the TSP type-1 (TSR) domain is exposed
CC and a nonadhesive conformation in which the TSR is masked by the N-
CC terminus. TSR-exposed conformation occurs during sporozoite development
CC in the oocyst in the mosquito vector and during host hepatocyte
CC invasion. TSR-masked conformation occurs during sporozoite migration
CC through the hemolymph to salivary glands in the mosquito vector and in
CC the host dermis. {ECO:0000250|UniProtKB:P23093}.
CC -!- DOMAIN: The GPI-anchor is essential for cell membrane localization and
CC for sporozoite formation inside the oocyst.
CC {ECO:0000250|UniProtKB:P23093}.
CC -!- PTM: During host cell invasion, proteolytically cleaved at the cell
CC membrane in the region I by a papain-like cysteine protease of parasite
CC origin (By similarity). Cleavage is triggered by the sporozoite contact
CC with highly sulfated heparan sulfate proteoglycans (HSPGs) present on
CC the host hepatocyte cell surface (By similarity). Cleavage exposes the
CC TSP type-1 (TSR) domain and is required for productive invasion of host
CC hepatocytes but not for adhesion to the host cell membrane (By
CC similarity). Cleavage is dispensable for sporozoite development in the
CC oocyst, motility and for traversal of host and vector cells (By
CC similarity). {ECO:0000250|UniProtKB:P23093}.
CC -!- PTM: O-glycosylated; maybe by POFUT2. {ECO:0000250|UniProtKB:P19597}.
CC -!- POLYMORPHISM: The sequence of the repeats varies across Plasmodium
CC species and strains. {ECO:0000250|UniProtKB:P19597}.
CC -!- BIOTECHNOLOGY: CSP immunodominant B cell epitopes are primarily located
CC in the central repeats (PubMed:29554084). Antibodies against CSP and
CC particularly against the central repeats can neutralize infection at
CC the pre-liver stage and thus makes CSP an attractive candidate for the
CC development of vaccines (PubMed:29554084, PubMed:32150583).
CC {ECO:0000269|PubMed:29554084, ECO:0000269|PubMed:32150583}.
CC -!- SIMILARITY: Belongs to the plasmodium circumsporozoite protein family.
CC {ECO:0000305}.
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DR EMBL; AL844502; CAB38998.2; -; Genomic_DNA.
DR RefSeq; XP_001351122.1; XM_001351086.1.
DR PDB; 3VDJ; X-ray; 1.70 A; A=310-374.
DR PDB; 3VDK; X-ray; 1.85 A; A=310-374.
DR PDB; 3VDL; X-ray; 2.04 A; A/B/C=310-374.
DR PDB; 6BQB; X-ray; 1.77 A; P=95-108.
DR PDB; 6MB3; EM; 3.37 A; E=26-383.
DR PDB; 6MHG; EM; 3.57 A; E=26-383.
DR PDB; 6PBV; X-ray; 1.57 A; G/I=95-108.
DR PDB; 6PBW; X-ray; 2.06 A; E=259-270.
DR PDB; 7RXI; X-ray; 2.15 A; A=310-375.
DR PDB; 7RXJ; X-ray; 2.35 A; G/I=310-375.
DR PDB; 7RXL; X-ray; 1.82 A; E/F=310-375.
DR PDB; 7RXP; X-ray; 1.76 A; A=309-375.
DR PDB; 7S0X; X-ray; 2.80 A; E/F=310-375.
DR PDBsum; 3VDJ; -.
DR PDBsum; 3VDK; -.
DR PDBsum; 3VDL; -.
DR PDBsum; 6BQB; -.
DR PDBsum; 6MB3; -.
DR PDBsum; 6MHG; -.
DR PDBsum; 6PBV; -.
DR PDBsum; 6PBW; -.
DR PDBsum; 7RXI; -.
DR PDBsum; 7RXJ; -.
DR PDBsum; 7RXL; -.
DR PDBsum; 7RXP; -.
DR PDBsum; 7S0X; -.
DR AlphaFoldDB; Q7K740; -.
DR SMR; Q7K740; -.
DR STRING; 5833.PFC0210c; -.
DR EnsemblProtists; CAB38998; CAB38998; PF3D7_0304600.
DR GeneID; 814364; -.
DR KEGG; pfa:PF3D7_0304600; -.
DR VEuPathDB; PlasmoDB:PF3D7_0304600; -.
DR HOGENOM; CLU_817555_0_0_1; -.
DR InParanoid; Q7K740; -.
DR OMA; MMRKLAI; -.
DR Proteomes; UP000001450; Chromosome 3.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:GeneDB.
DR GO; GO:0009986; C:cell surface; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; IDA:GeneDB.
DR GO; GO:0046812; F:host cell surface binding; IDA:GeneDB.
DR GO; GO:0044409; P:entry into host; IDA:GeneDB.
DR GO; GO:0085017; P:entry into host cell by a symbiont-containing vacuole; IMP:UniProtKB.
DR Gene3D; 2.20.100.10; -; 1.
DR InterPro; IPR003067; Crcmsprzoite.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01303; CRCMSPRZOITE.
DR SMART; SM00209; TSP1; 1.
DR SUPFAM; SSF82895; SSF82895; 1.
DR PROSITE; PS50092; TSP1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasm; Disulfide bond; Glycoprotein;
KW GPI-anchor; Lipoprotein; Malaria; Membrane; Reference proteome; Repeat;
KW Signal; Sporozoite.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..374
FT /note="Circumsporozoite protein"
FT /evidence="ECO:0000255"
FT /id="PRO_5004288147"
FT CHAIN ?..374
FT /note="Circumsporozoite protein C-terminus"
FT /evidence="ECO:0000250|UniProtKB:P23093"
FT /id="PRO_0000455512"
FT PROPEP 375..397
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000455513"
FT REPEAT 101..104
FT /note="1"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 105..108
FT /note="2"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 109..112
FT /note="3"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 113..116
FT /note="4"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 117..120
FT /note="5"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 121..124
FT /note="6"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 125..128
FT /note="7"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 129..132
FT /note="8"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 133..136
FT /note="9"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 137..140
FT /note="10"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 141..144
FT /note="11"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 145..148
FT /note="12"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 149..152
FT /note="13"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 153..156
FT /note="14"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 157..160
FT /note="15"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 161..164
FT /note="16"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 165..168
FT /note="17"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 169..172
FT /note="18"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 173..176
FT /note="19"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 177..180
FT /note="20"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 181..184
FT /note="21"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 185..188
FT /note="22"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 189..192
FT /note="23"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 193..196
FT /note="24"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 197..200
FT /note="25"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 201..204
FT /note="26"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 205..208
FT /note="27"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 209..212
FT /note="28"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 213..216
FT /note="29"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 217..220
FT /note="30"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 221..224
FT /note="31"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 225..228
FT /note="32"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 229..232
FT /note="33"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 233..236
FT /note="34"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 237..240
FT /note="35"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 241..244
FT /note="36"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 245..248
FT /note="37"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 249..252
FT /note="38"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 253..256
FT /note="39"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 257..260
FT /note="40"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 261..264
FT /note="41"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 265..268
FT /note="42"
FT /evidence="ECO:0000305|PubMed:30324137"
FT REPEAT 269..272
FT /note="43"
FT /evidence="ECO:0000305|PubMed:30324137"
FT DOMAIN 322..375
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 69..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..92
FT /note="Required for the binding to heparan sulfate
FT proteoglycans (HSPGs) on the surface of host hepatocytes"
FT /evidence="ECO:0000269|PubMed:27560376"
FT REGION 93..97
FT /note="Region I; contains the proteolytic cleavage site"
FT /evidence="ECO:0000250|UniProtKB:P23093"
FT REGION 101..272
FT /note="43 X 4 AA tandem repeats of N-[PVA]-[DN]-P"
FT /evidence="ECO:0000305|PubMed:30324137"
FT COMPBIAS 70..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 374
FT /note="GPI-anchor amidated cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="O-linked (Fuc) threonine"
FT /evidence="ECO:0000250|UniProtKB:P19597"
FT DISULFID 334..369
FT /evidence="ECO:0000269|PubMed:22547819,
FT ECO:0007744|PDB:3VDJ, ECO:0007744|PDB:3VDK"
FT DISULFID 338..374
FT /evidence="ECO:0000269|PubMed:22547819,
FT ECO:0007744|PDB:3VDJ, ECO:0007744|PDB:3VDK"
SQ SEQUENCE 397 AA; 42646 MW; 9E81146F59EBCEA3 CRC64;
MMRKLAILSV SSFLFVEALF QEYQCYGSSS NTRVLNELNY DNAGTNLYNE LEMNYYGKQE
NWYSLKKNSR SLGENDDGNN EDNEKLRKPK HKKLKQPADG NPDPNANPNV DPNANPNVDP
NANPNVDPNA NPNANPNANP NANPNANPNA NPNANPNANP NANPNANPNA NPNANPNANP
NANPNANPNA NPNANPNVDP NANPNANPNA NPNANPNANP NANPNANPNA NPNANPNANP
NANPNANPNA NPNANPNANP NANPNANPNA NPNKNNQGNG QGHNMPNDPN RNVDENANAN
SAVKNNNNEE PSDKHIKEYL NKIQNSLSTE WSPCSVTCGN GIQVRIKPGS ANKPKDELDY
ANDIEKKICK MEKCSSVFNV VNSSIGLIMV LSFLFLN
