ID   CECD_HYACE              Reviewed;          62 AA.
AC   P01510;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 2.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Cecropin-D;
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 25-60, AND AMIDATION AT LYS-60.
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).
CC   -!- FUNCTION: Cecropins have lytic and antibacterial activity against
CC       several Gram-positive and Gram-negative bacteria.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the cecropin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X06673; CAA29872.1; -; mRNA.
DR   EMBL; M63846; AAA29186.1; -; Genomic_DNA.
DR   PIR; B40420; CKWKD.
DR   AlphaFoldDB; P01510; -.
DR   SMR; P01510; -.
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   Amidation; Antibiotic; Antimicrobial; Direct protein sequencing; Immunity;
KW   Innate immunity; Secreted; Signal.
FT   SIGNAL          1..22
FT   PROPEP          23..24
FT                   /note="Removed by a dipeptidylpeptidase"
FT                   /evidence="ECO:0000269|PubMed:7140755"
FT                   /id="PRO_0000004863"
FT   CHAIN           25..60
FT                   /note="Cecropin-D"
FT                   /id="PRO_0000004864"
FT   MOD_RES         60
FT                   /note="Lysine amide"
FT                   /evidence="ECO:0000269|PubMed:7140755"
FT   CONFLICT        8
FT                   /note="F -> L (in Ref. 1; CAA29872)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        18
FT                   /note="R -> G (in Ref. 1; CAA29872)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   62 AA;  6625 MW;  AD89A3F03056C44A CRC64;
     MNFTKILFFV VACVFAMRTV SAAPWNPFKE LEKVGQRVRD AVISAGPAVA TVAQATALAK
     GK