ID   CECP1_ASCSU             Reviewed;          70 AA.
AC   P14661; Q5H7N7;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Cecropin-P1;
DE   Flags: Precursor;
GN   Name=ASCEC-1;
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP   INDUCTION.
RX   PubMed=15850460; DOI=10.1042/bj20050218;
RA   Pillai A., Ueno S., Zhang H., Lee J.M., Kato Y.;
RT   "Cecropin P1 and novel nematode cecropins: a bacteria-inducible
RT   antimicrobial peptide family in the nematode Ascaris suum.";
RL   Biochem. J. 390:207-214(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 14-44, SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=2512577; DOI=10.1073/pnas.86.23.9159;
RA   Lee J.-Y., Boman A., Chuanxin S., Andersson M., Joernvall H., Mutt V.,
RA   Boman H.G.;
RT   "Antibacterial peptides from pig intestine: isolation of a mammalian
RT   cecropin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:9159-9162(1989).
RN   [3]
RP   PROTEIN SEQUENCE OF 14-44, MASS SPECTROMETRY, AND REVISES SPECIES OF
RP   ORIGIN.
RX   PubMed=12737319; DOI=10.1007/s000180300051;
RA   Andersson M., Boman A., Boman H.G.;
RT   "Ascaris nematodes from pig and human make three antibacterial peptides:
RT   isolation of cecropin P1 and two ASABF peptides.";
RL   Cell. Mol. Life Sci. 60:599-606(2003).
RN   [4]
RP   STRUCTURE BY NMR OF 14-44.
RX   PubMed=1396696; DOI=10.1111/j.1432-1033.1992.tb17273.x;
RA   Sipos D., Andersson M., Ehrenberg A.;
RT   "The structure of the mammalian antibacterial peptide cecropin P1 in
RT   solution, determined by proton-NMR.";
RL   Eur. J. Biochem. 209:163-169(1992).
CC   -!- FUNCTION: Has antibacterial activity against several Gram-positive and
CC       Gram-negative bacteria. Is weakly active against yeasts. Acts by a
CC       nonpore mechanism. {ECO:0000269|PubMed:15850460,
CC       ECO:0000269|PubMed:2512577}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2512577}.
CC   -!- TISSUE SPECIFICITY: Expressed in the body wall, intestine, uterus and
CC       ovary. {ECO:0000269|PubMed:15850460}.
CC   -!- INDUCTION: By bacterial infection. {ECO:0000269|PubMed:15850460}.
CC   -!- MASS SPECTROMETRY: Mass=3339.6; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:12737319};
CC   -!- SIMILARITY: Belongs to the cecropin family. {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to originate from pig (PubMed:2512577
CC       and PubMed:1396696). It was later shown that this protein in fact
CC       originates from A.suum which is present in pig intestine
CC       (PubMed:12737319). {ECO:0000305|PubMed:12737319}.
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DR   EMBL; AB186032; BAD89085.1; -; mRNA.
DR   EMBL; AB186036; BAD89089.1; -; Genomic_DNA.
DR   PIR; A36221; A36221.
DR   PDB; 2N92; NMR; -; A=14-44.
DR   PDB; 7DEH; NMR; -; A=14-44.
DR   PDBsum; 2N92; -.
DR   PDBsum; 7DEH; -.
DR   AlphaFoldDB; P14661; -.
DR   SMR; P14661; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0019731; P:antibacterial humoral response; IEA:InterPro.
DR   GO; GO:0002776; P:antimicrobial peptide secretion; IDA:UniProtKB.
DR   GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
DR   InterPro; IPR000875; Cecropin.
DR   Pfam; PF00272; Cecropin; 1.
DR   PROSITE; PS00268; CECROPIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial; Direct protein sequencing;
KW   Secreted; Signal.
FT   SIGNAL          1..13
FT                   /evidence="ECO:0000269|PubMed:12737319,
FT                   ECO:0000269|PubMed:2512577"
FT   CHAIN           14..44
FT                   /note="Cecropin-P1"
FT                   /id="PRO_0000044676"
FT   PROPEP          45..70
FT                   /note="Removed in mature form"
FT                   /id="PRO_0000397964"
FT   STRAND          21..23
FT                   /evidence="ECO:0007829|PDB:2N92"
FT   HELIX           27..40
FT                   /evidence="ECO:0007829|PDB:2N92"
SQ   SEQUENCE   70 AA;  7876 MW;  E5F5FFE23C10B3F1 CRC64;
     MFLIYLFVQT AESSWLSKTA KKLENSAKKR ISEGIAIAIQ GGPRRRRFVA EQDAIHSRVS
     REVPTLSDSV