CSP_PLAFA
ID CSP_PLAFA Reviewed; 412 AA.
AC P02893;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Circumsporozoite protein {ECO:0000303|PubMed:6204383};
DE Short=CS {ECO:0000303|PubMed:6204383};
DE Short=PfCSP {ECO:0000303|PubMed:29195810};
DE Contains:
DE RecName: Full=Circumsporozoite protein C-terminus {ECO:0000305};
DE Flags: Precursor;
GN Name=CSP {ECO:0000303|PubMed:15630135};
OS Plasmodium falciparum.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5833;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DEVELOPMENTAL STAGE, AND REPEATS.
RX PubMed=6204383; DOI=10.1126/science.6204383;
RA Dame J.B., Williams J.L., McCutchan T.F., Weber J.L., Wirtz R.A.,
RA Hochmeyer W.T., Maloy W.L., Haynes J.D., Schneider I., Roberts D.,
RA Sanders G.S., Reddy E.P., Diggs C.L., Miller L.H.;
RT "Structure of the gene encoding the immunodominant surface antigen on the
RT sporozoite of the human malaria parasite Plasmodium falciparum.";
RL Science 225:593-599(1984).
RN [2]
RP DEVELOPMENTAL STAGE, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=15630135; DOI=10.1084/jem.20040989;
RA Coppi A., Pinzon-Ortiz C., Hutter C., Sinnis P.;
RT "The Plasmodium circumsporozoite protein is proteolytically processed
RT during cell invasion.";
RL J. Exp. Med. 201:27-33(2005).
RN [3]
RP BIOTECHNOLOGY.
RX PubMed=25913272; DOI=10.1016/s0140-6736(15)60721-8;
RG RTS,S Clinical Trials Partnership;
RT "Efficacy and safety of RTS,S/AS01 malaria vaccine with or without a
RT booster dose in infants and children in Africa: final results of a phase 3,
RT individually randomised, controlled trial.";
RL Lancet 386:31-45(2015).
RN [4] {ECO:0007744|PDB:2MSA}
RP STRUCTURE BY NMR OF 67-75.
RX PubMed=18930095; DOI=10.1016/j.vaccine.2008.09.071;
RA Bermudez A., Vanegas M., Patarroyo M.E.;
RT "Structural and immunological analysis of circumsporozoite protein
RT peptides: a further step in the identification of potential components of a
RT minimal subunit-based, chemically synthesised antimalarial vaccine.";
RL Vaccine 26:6908-6918(2008).
RN [5] {ECO:0007744|PDB:5BK0, ECO:0007744|PDB:6AZM}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 268-287 IN COMPLEX WITH ANTIBODY,
RP FUNCTION, DEVELOPMENTAL STAGE, AND BIOTECHNOLOGY.
RX PubMed=29195810; DOI=10.1016/j.immuni.2017.11.007;
RA Triller G., Scally S.W., Costa G., Pissarev M., Kreschel C., Bosch A.,
RA Marois E., Sack B.K., Murugan R., Salman A.M., Janse C.J., Khan S.M.,
RA Kappe S.H.I., Adegnika A.A., Mordmueller B., Levashina E.A., Julien J.P.,
RA Wardemann H.;
RT "Natural Parasite Exposure Induces Protective Human Anti-Malarial
RT Antibodies.";
RL Immunity 47:1197-1209.e10(2017).
RN [6] {ECO:0007744|PDB:6B5L, ECO:0007744|PDB:6B5M, ECO:0007744|PDB:6B5N, ECO:0007744|PDB:6B5O, ECO:0007744|PDB:6B5P, ECO:0007744|PDB:6B5R, ECO:0007744|PDB:6B5S, ECO:0007744|PDB:6B5T}
RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 120-134 IN COMPLEX WITH ANTIBODY
RP CIS4, FUNCTION, DEVELOPMENTAL STAGE, PROTEOLYTIC CLEAVAGE, AND
RP BIOTECHNOLOGY.
RX PubMed=29554083; DOI=10.1038/nm.4512;
RA Kisalu N.K., Idris A.H., Weidle C., Flores-Garcia Y., Flynn B.J.,
RA Sack B.K., Murphy S., Schoen A., Freire E., Francica J.R., Miller A.B.,
RA Gregory J., March S., Liao H.X., Haynes B.F., Wiehe K., Trama A.M.,
RA Saunders K.O., Gladden M.A., Monroe A., Bonsignori M., Kanekiyo M.,
RA Wheatley A.K., McDermott A.B., Farney S.K., Chuang G.Y., Zhang B., Kc N.,
RA Chakravarty S., Kwong P.D., Sinnis P., Bhatia S.N., Kappe S.H.I.,
RA Sim B.K.L., Hoffman S.L., Zavala F., Pancera M., Seder R.A.;
RT "A human monoclonal antibody prevents malaria infection by targeting a new
RT site of vulnerability on the parasite.";
RL Nat. Med. 24:408-416(2018).
RN [7]
RP ERRATUM OF PUBMED:29554083.
RX PubMed=30552419; DOI=10.1038/s41591-018-0315-0;
RA Kisalu N.K., Idris A.H., Weidle C., Flores-Garcia Y., Flynn B.J.,
RA Sack B.K., Murphy S., Schoen A., Freire E., Francica J.R., Miller A.B.,
RA Gregory J., March S., Liao H.X., Haynes B.F., Wiehe K., Trama A.M.,
RA Saunders K.O., Gladden M.A., Monroe A., Bonsignori M., Kanekiyo M.,
RA Wheatley A.K., McDermott A.B., Farney S.K., Chuang G.Y., Zhang B., Kc N.,
RA Chakravarty S., Kwong P.D., Sinnis P., Bhatia S.N., Kappe S.H.I.,
RA Sim B.K.L., Hoffman S.L., Zavala F., Pancera M., Seder R.A.;
RL Nat. Med. 25:188-189(2019).
CC -!- FUNCTION: Essential sporozoite protein (PubMed:29195810,
CC PubMed:29554083). 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:29195810,
CC PubMed:29554083). 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:29195810, ECO:0000269|PubMed:29554083}.
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 -!- DEVELOPMENTAL STAGE: Expressed in sporozoites (at protein level).
CC {ECO:0000269|PubMed:15630135, ECO:0000269|PubMed:29195810,
CC ECO:0000269|PubMed:29554083, ECO:0000269|PubMed:6204383}.
CC -!- DOMAIN: The N-terminus is involved in the initial binding to heparan
CC sulfate proteoglycans (HSPGs) on the surface of host hepatocytes (By
CC similarity). The N-terminus masks the TSP type-1 (TSR) domain which
CC 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:0000250|UniProtKB:Q7K740}.
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 (PubMed:15630135, PubMed:29554083). Cleavage is triggered by the
CC sporozoite contact with highly sulfated heparan sulfate proteoglycans
CC (HSPGs) present on the host hepatocyte cell surface (By similarity).
CC Cleavage exposes the TSP type-1 (TSR) domain and is required for
CC productive invasion of host hepatocytes but not for adhesion to the
CC host cell membrane (PubMed:15630135). Cleavage is dispensable for
CC sporozoite development in the oocyst, motility and for traversal of
CC host and vector cells (By similarity). {ECO:0000250|UniProtKB:P23093,
CC ECO:0000269|PubMed:15630135, ECO:0000269|PubMed:29554083}.
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:29195810, PubMed:29554083). Antibodies
CC against CSP and particularly against the central repeats can neutralize
CC infection at the pre-liver stage and thus makes CSP an attractive
CC candidate for the development of vaccines (PubMed:29195810,
CC PubMed:29554083). CSP is the major component of the leading malaria
CC vaccine RTS,S/AS01, which provides partial protection against malaria
CC in young children (PubMed:25913272). {ECO:0000269|PubMed:25913272,
CC ECO:0000269|PubMed:29195810, ECO:0000269|PubMed:29554083}.
CC -!- SIMILARITY: Belongs to the plasmodium circumsporozoite protein family.
CC {ECO:0000305}.
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DR EMBL; K02194; AAA29524.1; -; Genomic_DNA.
DR PIR; A03388; OZZQAF.
DR PDB; 2MSA; NMR; -; A=67-75.
DR PDB; 5BK0; X-ray; 3.15 A; E=268-287.
DR PDB; 6AXK; X-ray; 2.10 A; E=274-285.
DR PDB; 6AXL; X-ray; 2.40 A; G/I=274-285.
DR PDB; 6AZM; X-ray; 1.60 A; E/F=268-287.
DR PDB; 6B5L; X-ray; 2.40 A; A=120-130.
DR PDB; 6B5M; X-ray; 1.79 A; A=120-134.
DR PDB; 6B5N; X-ray; 1.98 A; A=136-150.
DR PDB; 6B5O; X-ray; 2.19 A; A=272-286.
DR PDB; 6B5P; X-ray; 2.30 A; A=120-130.
DR PDB; 6B5R; X-ray; 1.77 A; A=120-134.
DR PDB; 6B5S; X-ray; 1.98 A; A=136-150.
DR PDB; 6B5T; X-ray; 2.22 A; A=272-286.
DR PDB; 6D01; X-ray; 3.20 A; I/J=268-287.
DR PDB; 6D0X; X-ray; 1.85 A; C=276-287.
DR PDB; 6D11; X-ray; 3.40 A; E=268-287.
DR PDB; 6UC5; X-ray; 1.75 A; P=278-288.
DR PDB; 6UUD; X-ray; 1.85 A; A=100-116.
DR PDB; 6W00; X-ray; 1.85 A; P=278-285.
DR PDB; 6W05; X-ray; 2.52 A; P=278-285.
DR PDB; 6WFW; X-ray; 2.09 A; P=278-285.
DR PDB; 6WFX; X-ray; 2.59 A; P=278-285.
DR PDB; 6WFY; X-ray; 1.23 A; P=270-285.
DR PDB; 6WFZ; X-ray; 1.84 A; C/P=274-285.
DR PDB; 6WG0; X-ray; 1.60 A; P=278-288.
DR PDB; 6WG1; X-ray; 2.09 A; C=262-285.
DR PDB; 6WG2; X-ray; 2.53 A; P=270-285.
DR PDB; 7LKB; X-ray; 1.80 A; A/D=120-134.
DR PDB; 7LKG; X-ray; 2.02 A; C/F=120-134.
DR PDB; 7RCS; X-ray; 2.40 A; C/D=120-134.
DR PDB; 7RD3; X-ray; 1.81 A; C/D=120-134.
DR PDB; 7RD4; X-ray; 1.75 A; G/I=120-134.
DR PDB; 7RD9; X-ray; 1.91 A; C=120-134.
DR PDB; 7RDA; X-ray; 1.92 A; C=120-134.
DR PDBsum; 2MSA; -.
DR PDBsum; 5BK0; -.
DR PDBsum; 6AXK; -.
DR PDBsum; 6AXL; -.
DR PDBsum; 6AZM; -.
DR PDBsum; 6B5L; -.
DR PDBsum; 6B5M; -.
DR PDBsum; 6B5N; -.
DR PDBsum; 6B5O; -.
DR PDBsum; 6B5P; -.
DR PDBsum; 6B5R; -.
DR PDBsum; 6B5S; -.
DR PDBsum; 6B5T; -.
DR PDBsum; 6D01; -.
DR PDBsum; 6D0X; -.
DR PDBsum; 6D11; -.
DR PDBsum; 6UC5; -.
DR PDBsum; 6UUD; -.
DR PDBsum; 6W00; -.
DR PDBsum; 6W05; -.
DR PDBsum; 6WFW; -.
DR PDBsum; 6WFX; -.
DR PDBsum; 6WFY; -.
DR PDBsum; 6WFZ; -.
DR PDBsum; 6WG0; -.
DR PDBsum; 6WG1; -.
DR PDBsum; 6WG2; -.
DR PDBsum; 7LKB; -.
DR PDBsum; 7LKG; -.
DR PDBsum; 7RCS; -.
DR PDBsum; 7RD3; -.
DR PDBsum; 7RD4; -.
DR PDBsum; 7RD9; -.
DR PDBsum; 7RDA; -.
DR AlphaFoldDB; P02893; -.
DR SMR; P02893; -.
DR ABCD; P02893; 49 sequenced antibodies.
DR VEuPathDB; PlasmoDB:PF3D7_0304600; -.
DR VEuPathDB; PlasmoDB:Pf7G8-2_000074100; -.
DR VEuPathDB; PlasmoDB:Pf7G8_030010400; -.
DR VEuPathDB; PlasmoDB:PfCD01_030010000; -.
DR VEuPathDB; PlasmoDB:PfDd2_030009600; -.
DR VEuPathDB; PlasmoDB:PfGA01_030011200; -.
DR VEuPathDB; PlasmoDB:PfGB4_030010200; -.
DR VEuPathDB; PlasmoDB:PfGN01_030010200; -.
DR VEuPathDB; PlasmoDB:PfHB3_030008400; -.
DR VEuPathDB; PlasmoDB:PfIT_030009400; -.
DR VEuPathDB; PlasmoDB:PfKE01_030009000; -.
DR VEuPathDB; PlasmoDB:PfKH01_030009500; -.
DR VEuPathDB; PlasmoDB:PfKH02_030010100; -.
DR VEuPathDB; PlasmoDB:PfML01_030009600; -.
DR VEuPathDB; PlasmoDB:PfNF135_030009700; -.
DR VEuPathDB; PlasmoDB:PfNF166_030008000; -.
DR VEuPathDB; PlasmoDB:PfNF54_030009700; -.
DR VEuPathDB; PlasmoDB:PfSD01_030009700; -.
DR VEuPathDB; PlasmoDB:PfSN01_030010300; -.
DR VEuPathDB; PlasmoDB:PfTG01_030011000; -.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; Repeat; Signal; Sporozoite.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..389
FT /note="Circumsporozoite protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000024526"
FT CHAIN ?..389
FT /note="Circumsporozoite protein C-terminus"
FT /evidence="ECO:0000250|UniProtKB:P23093"
FT /id="PRO_0000455485"
FT PROPEP 390..412
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000455486"
FT REPEAT 123..126
FT /note="1"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 127..130
FT /note="2"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 131..134
FT /note="3"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 135..138
FT /note="4"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 139..142
FT /note="5"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 143..146
FT /note="6"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 147..150
FT /note="7"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 151..154
FT /note="8"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 155..158
FT /note="9"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 159..162
FT /note="10"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 163..166
FT /note="11"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 167..170
FT /note="12"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 171..174
FT /note="13"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 175..178
FT /note="14"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 179..182
FT /note="15"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 183..186
FT /note="16"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 187..190
FT /note="17"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 191..194
FT /note="18"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 195..198
FT /note="19"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 199..202
FT /note="20"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 203..206
FT /note="21"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 207..210
FT /note="22"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 211..214
FT /note="23"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 215..218
FT /note="24"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 219..222
FT /note="25"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 223..226
FT /note="26"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 227..230
FT /note="27"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 231..234
FT /note="28"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 235..238
FT /note="29"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 239..242
FT /note="30"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 243..246
FT /note="31"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 247..250
FT /note="32"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 251..254
FT /note="33"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 255..258
FT /note="34"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 259..262
FT /note="35"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 263..266
FT /note="36"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 267..270
FT /note="37"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 271..274
FT /note="38"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 275..278
FT /note="39"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 279..282
FT /note="40"
FT /evidence="ECO:0000305|PubMed:6204383"
FT REPEAT 283..286
FT /note="41"
FT /evidence="ECO:0000305|PubMed:6204383"
FT DOMAIN 337..390
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 69..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..111
FT /note="Required for the binding to heparan sulfate
FT proteoglycans (HSPGs) on the surface of host hepatocytes"
FT /evidence="ECO:0000250|UniProtKB:Q7K740"
FT REGION 112..116
FT /note="Region I; contains the proteolytic cleavage site"
FT /evidence="ECO:0000250|UniProtKB:P23093"
FT REGION 123..286
FT /note="41 X 4 AA tandem repeats of P-N-[AV]-[ND]"
FT /evidence="ECO:0000305|PubMed:6204383"
FT COMPBIAS 81..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 389
FT /note="GPI-anchor amidated cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="O-linked (Fuc) threonine"
FT /evidence="ECO:0000250|UniProtKB:P19597"
FT DISULFID 349..384
FT /evidence="ECO:0000250|UniProtKB:Q7K740"
FT DISULFID 353..389
FT /evidence="ECO:0000250|UniProtKB:Q7K740"
FT HELIX 103..110
FT /evidence="ECO:0007829|PDB:6UUD"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:6WG1"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:6WFY"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:6WFY"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:6WG1"
SQ SEQUENCE 412 AA; 44421 MW; 1EEEED3DE90965F8 CRC64;
MMRKLAILSV SSFLFVEALF QEYQCYGSSS NTRVLNELNY DNAGTNLYNE LEMNYYGKQE
NWYSLKKNSR SLGENDDGNN NNGDNGREGK DEDKRDGNNE DNEKLRKPKH KKLKQPGDGN
PDPNANPNVD PNANPNVDPN ANPNVDPNAN PNANPNANPN ANPNANPNAN PNANPNANPN
ANPNANPNAN PNANPNANPN ANPNANPNVD PNANPNANPN ANPNANPNAN PNANPNANPN
ANPNANPNAN PNANPNANPN ANPNANPNAN PNANPNANPN ANPNANPNKN NQGNGQGHNM
PNDPNRNVDE NANANNAVKN NNNEEPSDKH IEQYLKKIKN SISTEWSPCS VTCGNGIQVR
IKPGSANKPK DELDYENDIE KKICKMEKCS SVFNVVNSSI GLIMVLSFLF LN
