ID   LEB3_BOMMO              Reviewed;         179 AA.
AC   P55796;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Lebocin-3;
DE            Short=LEB 3;
DE   Flags: Precursor;
GN   Name=LEB3;
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 [GENOMIC DNA].
RC   STRAIN=Tokai X Asahi;
RX   PubMed=9325165; DOI=10.1006/bbrc.1997.7386;
RA   Furukawa S., Taniai K., Ishibashi J., Hara S., Shono T., Yamakawa M.;
RT   "A novel member of lebocin gene family from the silkworm, Bombyx mori.";
RL   Biochem. Biophys. Res. Commun. 238:769-774(1997).
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. {ECO:0000269|PubMed:7654207}.
CC   -!- SIMILARITY: Belongs to the lebocin 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; AB003035; BAA22883.1; -; Genomic_DNA.
DR   PIR; JC5665; JC5665.
DR   RefSeq; NP_001119732.1; NM_001126260.1.
DR   AlphaFoldDB; P55796; -.
DR   SMR; P55796; -.
DR   STRING; 7091.BGIBMGA006775-TA; -.
DR   iPTMnet; P55796; -.
DR   GeneID; 100146108; -.
DR   KEGG; bmor:100146108; -.
DR   CTD; 100146108; -.
DR   eggNOG; ENOG502TC1F; Eukaryota.
DR   HOGENOM; CLU_128921_0_0_1; -.
DR   InParanoid; P55796; -.
DR   OrthoDB; 1613875at2759; -.
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:0000269|PubMed:7654207"
FT                   /id="PRO_0000004977"
FT   PEPTIDE         121..152
FT                   /note="Lebocin-3"
FT                   /id="PRO_0000004978"
FT   PROPEP          153..179
FT                   /id="PRO_0000004979"
FT   CARBOHYD        135
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:7654207"
SQ   SEQUENCE   179 AA;  21013 MW;  53F1FA423AB8D6AB CRC64;
     MYKFLVFSSV LVLFFAQASC QRFIQPTFRP PPTQRPITRT VRQAGQEPLW LYQGDNVPRA
     PSTADHPILP SKIDDVQLDP NRRYVRSVTN PENNEASIEH SHHTVDIGLD QPIESHRNTR
     DLRFLYPRGK LPVPTLPPFN PKPIYIDMGN RYRRHASEDQ EELRQYNEHF LIPRDIFQE