ID   LEB1_BOMMO              Reviewed;         179 AA.
AC   P54684;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Lebocin-1/2;
DE   Flags: Precursor;
OS   Bombyx mori (Silk moth).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Bombycidae; Bombycinae; Bombyx.
OX   NCBI_TaxID=7091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Tokai X Asahi; TISSUE=Fat body;
RX   PubMed=7545395; DOI=10.1006/bbrc.1995.2284;
RA   Chowdhury S., Taniai K., Hara S., Kadono-Okuda K., Kato Y., Yamamoto M.,
RA   Xu J., Choi S.K., Debnath N.C., Choi H.K., Miyanoshita A., Sugiyama M.,
RA   Asaoka A., Yamakawa M.;
RT   "cDNA cloning and gene expression of lebocin, a novel member of
RT   antibacterial peptides from the silkworm, Bombyx mori.";
RL   Biochem. Biophys. Res. Commun. 214:271-278(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 121-152, AND GLYCOSYLATION AT THR-135.
RC   TISSUE=Hemolymph;
RX   PubMed=7654207; DOI=10.1042/bj3100651;
RA   Hara S., Yamakawa M.;
RT   "A novel antibacterial peptide family isolated from the silkworm, Bombyx
RT   mori.";
RL   Biochem. J. 310:651-656(1995).
CC   -!- FUNCTION: Antibacterial peptide.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Hemolymph. Produced in fat body.
CC   -!- INDUCTION: By bacterial infection.
CC   -!- PTM: O-glycosylation is important for the antibacterial activity of
CC       lebocin, O-linked glycan structure is a disaccharide (Gal-GalNAc) in
CC       case of lebocin 1 and a monosaccharide (GalNAc) in case of lebocin 2.
CC       {ECO:0000269|PubMed:7654207}.
CC   -!- SIMILARITY: Belongs to the lebocin family. {ECO:0000305}.
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DR   EMBL; S79612; AAB35218.1; -; mRNA.
DR   PIR; JC4247; JC4247.
DR   RefSeq; NP_001037468.1; NM_001044003.1.
DR   AlphaFoldDB; P54684; -.
DR   SMR; P54684; -.
DR   TCDB; 1.C.117.1.1; the antibacterial peptide lebocin (lebocin) family.
DR   iPTMnet; P54684; -.
DR   HOGENOM; CLU_128921_0_0_1; -.
DR   Proteomes; UP000005204; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Direct protein sequencing; Glycoprotein;
KW   Immunity; Innate immunity; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..120
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000004974"
FT   PEPTIDE         121..152
FT                   /note="Lebocin-1/2"
FT                   /id="PRO_0000004975"
FT   PROPEP          153..179
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000004976"
FT   REGION          93..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..116
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        135
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:7654207"
SQ   SEQUENCE   179 AA;  20955 MW;  6B45896B4A4952F1 CRC64;
     MYKFLVFSSV LVLFFAQASC QRFIQPTFRP PPTQRPIIRT ARQAGQEPLW LYQGDNVPRA
     PSTADHPILP SKIDDVQLDP NRRYVRSVTN PENNEASIEH SHHTVDTGLD QPIESHRNTR
     DLRFLYPRGK LPVPTPPPFN PKPIYIDMGN RYRRHASDDQ EELRQYNEHF LIPRDIFQE