CECB_BOMMO
ID CECB_BOMMO Reviewed; 63 AA.
AC P04142;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Cecropin-B;
DE AltName: Full=Lepidopteran-A/B;
DE Flags: Precursor;
GN Name=CECB1;
GN and
GN Name=CECB2;
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=7590269; DOI=10.1016/0378-1119(95)00408-x;
RA Taniai K., Kadono-Okuda K., Kato Y., Yamamoto M., Shimabukuro M.,
RA Chowdhury S., Xu J., Kotani E., Tomino S., Yamakawa M.;
RT "Structure of two cecropin B-encoding genes and bacteria-inducible DNA-
RT binding proteins which bind to the 5'-upstream regulatory region in the
RT silkworm, Bombyx mori.";
RL Gene 163:215-219(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1390892; DOI=10.1016/0167-4781(92)90013-p;
RA Taniai K., Kato Y., Hirochika H., Yamakawa M.;
RT "Isolation and nucleotide sequence of cecropin B cDNA clones from the
RT silkworm, Bombyx mori.";
RL Biochim. Biophys. Acta 1132:203-206(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8485525; DOI=10.1016/0965-1748(93)90009-h;
RA Kato Y., Taniai K., Hirochika H., Yamakawa M.;
RT "Expression and characterization of cDNAs for cecropin B, an antibacterial
RT protein of the silkworm, Bombyx mori.";
RL Insect Biochem. Mol. Biol. 23:285-290(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C108; TISSUE=Larval fat body;
RX PubMed=7765280; DOI=10.1271/bbb.58.1476;
RA Yamano Y., Matsumoto M., Inoue K., Kawabata T., Morishima I.;
RT "Cloning of cDNAs for cecropins A and B, and expression of the genes in the
RT silkworm, Bombyx mori.";
RL Biosci. Biotechnol. Biochem. 58:1476-1478(1994).
RN [5]
RP PROTEIN SEQUENCE OF 27-61.
RA Teshima T., Ueki Y., Nakai T., Shiba T.;
RT "Structure determination of lepidopteran, self-defense substance produced
RT by silkworm.";
RL Tetrahedron 42:829-834(1986).
RN [6]
RP PROTEIN SEQUENCE OF 27-61, AND HYDROXYLATION AT LYS-47.
RX PubMed=2184991; DOI=10.1016/0305-0491(90)90019-p;
RA Morishima I., Suginaka S., Ueno T., Hirano H.;
RT "Isolation and structure of cecropins, inducible antibacterial peptides,
RT from the silkworm, Bombyx mori.";
RL Comp. Biochem. Physiol. 95B:551-554(1990).
RN [7]
RP PROTEIN SEQUENCE OF 27-61, AND AMIDATION AT ILE-61.
RC TISSUE=Cuticle;
RX PubMed=8203751; DOI=10.1006/abio.1994.1113;
RA Lee W.-J., Brey P.T.;
RT "Isolation and identification of cecropin antibacterial peptides from the
RT extracellular matrix of the insect integument.";
RL Anal. Biochem. 217:231-235(1994).
CC -!- FUNCTION: Cecropins have lytic and antibacterial activity against
CC several Gram-positive and Gram-negative bacteria.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Highest expression in fat body and hemocytes. Is
CC also expressed in Malpighian tubules and to a much lesser extent in
CC midgut. Not present in silk gland.
CC -!- PTM: Lepidopteran-B differs from lepidopteran-A by its hydroxylated
CC residue. {ECO:0000269|PubMed:2184991}.
CC -!- SIMILARITY: Belongs to the cecropin family. {ECO:0000305}.
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DR EMBL; D25320; BAA04990.1; -; Genomic_DNA.
DR EMBL; D25321; BAA04991.1; -; Genomic_DNA.
DR EMBL; D11114; BAA01890.1; -; mRNA.
DR EMBL; D11113; BAA01889.1; -; mRNA.
DR EMBL; S60579; AAC60501.1; -; mRNA.
DR EMBL; S74297; AAC60514.1; -; mRNA.
DR PIR; JC2296; CKMTB.
DR RefSeq; NP_001037032.1; NM_001043567.1.
DR RefSeq; NP_001037460.1; NM_001043995.1.
DR RefSeq; NP_001096031.1; NM_001102561.1.
DR RefSeq; XP_004926103.1; XM_004926046.2.
DR RefSeq; XP_004926104.1; XM_004926047.1.
DR RefSeq; XP_004926106.1; XM_004926049.2.
DR RefSeq; XP_004926107.1; XM_004926050.2.
DR RefSeq; XP_012545761.1; XM_012690307.1.
DR AlphaFoldDB; P04142; -.
DR SMR; P04142; -.
DR STRING; 7091.BGIBMGA000021-TA; -.
DR EnsemblMetazoa; BGIBMGA000021-RA; BGIBMGA000021-TA; BGIBMGA000021.
DR EnsemblMetazoa; BGIBMGA000023-RA; BGIBMGA000023-TA; BGIBMGA000023.
DR EnsemblMetazoa; BGIBMGA000024-RA; BGIBMGA000024-TA; BGIBMGA000024.
DR EnsemblMetazoa; BGIBMGA000036-RA; BGIBMGA000036-TA; BGIBMGA000036.
DR EnsemblMetazoa; BGIBMGA000037-RA; BGIBMGA000037-TA; BGIBMGA000037.
DR EnsemblMetazoa; BGIBMGA000038-RA; BGIBMGA000038-TA; BGIBMGA000038.
DR GeneID; 101739536; -.
DR GeneID; 101739681; -.
DR GeneID; 101739958; -.
DR GeneID; 101740092; -.
DR GeneID; 693028; -.
DR GeneID; 732858; -.
DR KEGG; bmor:101739536; -.
DR KEGG; bmor:101739681; -.
DR KEGG; bmor:101739958; -.
DR KEGG; bmor:101740092; -.
DR KEGG; bmor:693028; -.
DR KEGG; bmor:732858; -.
DR CTD; 693028; -.
DR eggNOG; ENOG502T7RS; Eukaryota.
DR HOGENOM; CLU_187909_0_0_1; -.
DR InParanoid; P04142; -.
DR OMA; FACIMAF; -.
DR OrthoDB; 1635266at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
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;
KW Hydroxylation; Immunity; Innate immunity; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..26
FT /note="Removed by a dipeptidylpeptidase"
FT /evidence="ECO:0000269|PubMed:2184991,
FT ECO:0000269|PubMed:8203751, ECO:0000269|Ref.5"
FT /id="PRO_0000004826"
FT CHAIN 27..61
FT /note="Cecropin-B"
FT /evidence="ECO:0000269|PubMed:7765280"
FT /id="PRO_0000004827"
FT MOD_RES 47
FT /note="5-hydroxylysine; partial"
FT /evidence="ECO:0000269|PubMed:2184991"
FT MOD_RES 61
FT /note="Isoleucine amide"
FT /evidence="ECO:0000269|PubMed:8203751"
SQ SEQUENCE 63 AA; 6831 MW; C79C5540E45A84C8 CRC64;
MNFAKILSFV FALVLALSMT SAAPEPRWKI FKKIEKMGRN IRDGIVKAGP AIEVLGSAKA
IGK
