CECA_HYACE
ID CECA_HYACE Reviewed; 64 AA.
AC P01507;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Cecropin-A;
DE AltName: Full=Cecropin-C;
DE Flags: Precursor;
OS Hyalophora cecropia (Cecropia moth) (Samia cecropia).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Saturniidae; Saturniinae; Attacini; Hyalophora.
OX NCBI_TaxID=7123;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lidholm D.-A., Gudmundsson G.H., Xanthopoulos K.G., Boman H.G.;
RT "Insect immunity: cDNA clones coding for the precursor forms of cecropins A
RT and D, antibacterial proteins from Hyalophora cecropia.";
RL FEBS Lett. 226:8-12(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1711035; DOI=10.1016/s0021-9258(18)98986-6;
RA Gudmundsson G.H., Lidholm D.-A., Aasling B., Gan R., Boman H.G.;
RT "The cecropin locus. Cloning and expression of a gene cluster encoding
RT three antibacterial peptides in Hyalophora cecropia.";
RL J. Biol. Chem. 266:11510-11517(1991).
RN [3]
RP PROTEIN SEQUENCE OF 27-63, AND AMIDATION AT LYS-63.
RX PubMed=7140755; DOI=10.1111/j.1432-1033.1982.tb06857.x;
RA Hultmark D., Engstroem A., Bennich H., Kapur R., Boman H.G.;
RT "Insect immunity: isolation and structure of cecropin D and four minor
RT antibacterial components from Cecropia pupae.";
RL Eur. J. Biochem. 127:207-217(1982).
RN [4]
RP PRELIMINARY PROTEIN SEQUENCE OF 27-63.
RX PubMed=7019715; DOI=10.1038/292246a0;
RA Steiner H., Hultmark D., Engstroem A., Bennich H., Boman H.G.;
RT "Sequence and specificity of two antibacterial proteins involved in insect
RT immunity.";
RL Nature 292:246-248(1981).
RN [5]
RP STRUCTURE BY NMR OF 27-63.
RX PubMed=3207693; DOI=10.1021/bi00420a008;
RA Holak T.A., Engstroem A., Kraulis P.J., Lindeberg G., Bennich H.,
RA Jones T.A., Gronenborn A.M., Clore G.M.;
RT "The solution conformation of the antibacterial peptide cecropin A: a
RT nuclear magnetic resonance and dynamical simulated annealing study.";
RL Biochemistry 27:7620-7629(1988).
CC -!- FUNCTION: Cecropins have lytic and antibacterial activity against
CC several Gram-positive and Gram-negative bacteria.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: A protein with the same sequence as cecropin A, but lacking the
CC carboxyl blocking group, has been isolated and called cecropin C.
CC {ECO:0000269|PubMed:7140755}.
CC -!- SIMILARITY: Belongs to the cecropin family. {ECO:0000305}.
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DR EMBL; X06672; CAA29871.1; -; mRNA.
DR EMBL; M63845; AAA29185.1; -; Genomic_DNA.
DR PIR; A40420; CKWKA.
DR PDB; 1D9J; NMR; -; A=27-34.
DR PDB; 1D9L; NMR; -; A=27-34.
DR PDB; 1D9M; NMR; -; A=27-34.
DR PDB; 1D9O; NMR; -; A=27-34.
DR PDB; 1D9P; NMR; -; A=27-34.
DR PDB; 1F0D; NMR; -; A=27-34.
DR PDB; 1F0E; NMR; -; A=27-34.
DR PDB; 1F0F; NMR; -; A=27-34.
DR PDB; 1F0G; NMR; -; A=27-34.
DR PDB; 1F0H; NMR; -; A=27-34.
DR PDBsum; 1D9J; -.
DR PDBsum; 1D9L; -.
DR PDBsum; 1D9M; -.
DR PDBsum; 1D9O; -.
DR PDBsum; 1D9P; -.
DR PDBsum; 1F0D; -.
DR PDBsum; 1F0E; -.
DR PDBsum; 1F0F; -.
DR PDBsum; 1F0G; -.
DR PDBsum; 1F0H; -.
DR AlphaFoldDB; P01507; -.
DR BMRB; P01507; -.
DR SMR; P01507; -.
DR TCDB; 1.C.17.1.1; the cecropin (cecropin) family.
DR EvolutionaryTrace; P01507; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0019731; P:antibacterial humoral response; IEA:InterPro.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:UniProt.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR InterPro; IPR000875; Cecropin.
DR Pfam; PF00272; Cecropin; 1.
DR PROSITE; PS00268; CECROPIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amidation; Antibiotic; Antimicrobial;
KW Direct protein sequencing; Immunity; Innate immunity; Secreted; Signal.
FT SIGNAL 1..22
FT PROPEP 23..26
FT /note="Removed by a dipeptidylpeptidase"
FT /evidence="ECO:0000269|PubMed:7140755"
FT /id="PRO_0000004859"
FT CHAIN 27..63
FT /note="Cecropin-A"
FT /id="PRO_0000004860"
FT MOD_RES 63
FT /note="Lysine amide"
FT /evidence="ECO:0000269|PubMed:7140755"
FT HELIX 29..33
FT /evidence="ECO:0007829|PDB:1D9J"
SQ SEQUENCE 64 AA; 6952 MW; 0B3AEA15C32DB3A4 CRC64;
MNFSRIFFFV FACLTALAMV NAAPEPKWKL FKKIEKVGQN IRDGIIKAGP AVAVVGQATQ
IAKG
