ID   MOR2_BOMMO              Reviewed;          66 AA.
AC   O96059; P81604;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Moricin-2;
DE   Flags: Precursor;
GN   Name=MOR2;
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 / MRNA], INDUCTION, TISSUE SPECIFICITY,
RP   AND DEVELOPMENTAL STAGE.
RC   STRAIN=CHU 602, and Tokai X Asahi; TISSUE=Fat body;
RX   PubMed=10229682; DOI=10.1042/bj3400265;
RA   Furukawa S., Tanaka H., Nakazawa H., Ishibashi J., Shono T., Yamakawa M.;
RT   "Inducible gene expression of moricin, a unique antibacterial peptide from
RT   the silkworm (Bombyx mori).";
RL   Biochem. J. 340:265-271(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-66, FUNCTION, AND MASS SPECTROMETRY.
RC   STRAIN=Tokai X Asahi; TISSUE=Hemolymph;
RX   PubMed=8530391; DOI=10.1074/jbc.270.50.29923;
RA   Hara S., Yamakawa M.;
RT   "Moricin, a novel type of antibacterial peptide isolated from the silkworm,
RT   Bombyx mori.";
RL   J. Biol. Chem. 270:29923-29927(1995).
CC   -!- FUNCTION: Has antibacterial activity against Gram-positive and Gram-
CC       negative bacteria. Probably acts by disturbing membrane functions with
CC       its amphipathic structure. {ECO:0000269|PubMed:8530391}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed in fat body and to a lesser extent in
CC       hemocyte and Malpighian tubules. {ECO:0000269|PubMed:10229682}.
CC   -!- DEVELOPMENTAL STAGE: A weak signal appears 1 hour after induction,
CC       maximum levels are reached by 8 hours and remain at a high level over a
CC       period of at least 48 hours. {ECO:0000269|PubMed:10229682}.
CC   -!- INDUCTION: By bacterial infection. {ECO:0000269|PubMed:10229682}.
CC   -!- MASS SPECTROMETRY: Mass=4543.1; Mass_error=0.6; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:8530391};
CC   -!- SIMILARITY: Belongs to the moricin family. {ECO:0000305}.
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DR   EMBL; AB014092; BAA34260.1; -; mRNA.
DR   EMBL; AB019538; BAA77338.1; -; Genomic_DNA.
DR   RefSeq; NP_001036829.2; NM_001043364.2.
DR   AlphaFoldDB; O96059; -.
DR   BMRB; O96059; -.
DR   SMR; O96059; -.
DR   GeneID; 692365; -.
DR   KEGG; bmor:692365; -.
DR   CTD; 41942; -.
DR   HOGENOM; CLU_206132_1_0_1; -.
DR   InParanoid; O96059; -.
DR   OrthoDB; 1874529at2759; -.
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.
DR   Gene3D; 1.20.5.750; -; 1.
DR   InterPro; IPR009456; Moricin_fam.
DR   InterPro; IPR037043; Moricin_sf.
DR   Pfam; PF06451; Moricin; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Direct protein sequencing; Immunity;
KW   Innate immunity; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:8530391"
FT   CHAIN           25..66
FT                   /note="Moricin-2"
FT                   /id="PRO_0000004993"
SQ   SEQUENCE   66 AA;  7129 MW;  0635DFAA2AFC3FE4 CRC64;
     MNILKLFFVF IVAMSLVSCS TAAPAKIPIK AIKTVGKAVG KGLRAINIAS TANDVFNFLK
     PKKRKH