ID   MOR_MANSE               Reviewed;          67 AA.
AC   Q86MA1;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Moricin {ECO:0000303|PubMed:18265434, ECO:0000312|EMBL:AAO74637.1};
DE   Flags: Precursor;
OS   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Sphinginae; Sphingini; Manduca.
OX   NCBI_TaxID=7130 {ECO:0000312|EMBL:AAO74637.1};
RN   [1] {ECO:0000312|EMBL:AAO74637.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC   TISSUE=Fat body {ECO:0000303|PubMed:12706633};
RX   PubMed=12706633; DOI=10.1016/s0965-1748(03)00028-6;
RA   Zhu Y., Johnson T.J., Myers A.A., Kanost M.R.;
RT   "Identification by subtractive suppression hybridization of bacteria-
RT   induced genes expressed in Manduca sexta fat body.";
RL   Insect Biochem. Mol. Biol. 33:541-559(2003).
RN   [2] {ECO:0000312|EMBL:AAO74637.1}
RP   FUNCTION, DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=14728663; DOI=10.1111/j.1365-2583.2004.00454.x;
RA   Gorman M.J., Kankanala P., Kanost M.R.;
RT   "Bacterial challenge stimulates innate immune responses in extra-embryonic
RT   tissues of tobacco hornworm eggs.";
RL   Insect Mol. Biol. 13:19-24(2004).
RN   [3] {ECO:0007744|PDB:2JR8}
RP   STRUCTURE BY NMR OF 26-67, FUNCTION, SUBUNIT, DEVELOPMENTAL STAGE,
RP   INDUCTION, PEPTIDE SYNTHESIS, AND CIRCULAR DICHROISM ANALYSIS.
RX   PubMed=18265434; DOI=10.1002/psc.1016;
RA   Dai H., Rayaprolu S., Gong Y., Huang R., Prakash O., Jiang H.;
RT   "Solution structure, antibacterial activity, and expression profile of
RT   Manduca sexta moricin.";
RL   J. Pept. Sci. 14:855-863(2008).
CC   -!- FUNCTION: Antimicrobial peptide. Active against a broad spectrum of
CC       Gram-positive and Gram-negative bacteria including methicillin-
CC       resistant S.aureus ATCC 43 300, S.aureus BAA-39, pathogenic strains of
CC       L.monocytogenes, K.pneumoniae, E.coli O157:H7, S.typhimurium and
CC       multidrug-resistant S.typhimurium DT104 with minimum inhibitory
CC       concentration (MIC) of 1.4 uM for all except for S.aureus BAA-39
CC       (PubMed:18265434). Also active against Serratia marcescens
CC       (PubMed:14728663). Probably acts by disturbing membrane functions with
CC       its amphipathic alpha-helical structure (PubMed:18265434). May protect
CC       a developing embryo from bacterial infection (Probable).
CC       {ECO:0000269|PubMed:14728663, ECO:0000269|PubMed:18265434,
CC       ECO:0000305}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18265434}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at low levels in nerve tissue, salivary
CC       gland, Malpighian tubule, trachea, midgut, fat body, integument and
CC       muscle from day 3, fifth instar naive larvae. Moderate levels expressed
CC       in fat body from the 4th instar larvae (day 0), 5th instar larvae (days
CC       3 and 6), wandering larvae (day 6), and adults in the absence of
CC       infection. A moderate level of expression in the hemocytes of the naive
CC       larvae. Expression increases substantially in fat body and hemocytes
CC       after fifth instar larvae are challenged with bacterial cells
CC       (PubMed:18265434). Constitutive low expression in naive eggs, but up-
CC       regulated in them in response to bacteria. Expressed in 24 h (predorsal
CC       closure stage) eggs in extra-embryonic tissues (yolk and serosa) after
CC       bacterial challenge, but not in embryos (PubMed:14728663).
CC       {ECO:0000269|PubMed:14728663, ECO:0000269|PubMed:18265434}.
CC   -!- INDUCTION: By bacterial infection. {ECO:0000269|PubMed:12706633,
CC       ECO:0000269|PubMed:14728663, ECO:0000269|PubMed:18265434}.
CC   -!- SIMILARITY: Belongs to the moricin family. {ECO:0000305}.
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DR   EMBL; AY232301; AAO74637.1; -; mRNA.
DR   PDB; 2JR8; NMR; -; A=26-67.
DR   PDBsum; 2JR8; -.
DR   AlphaFoldDB; Q86MA1; -.
DR   SMR; Q86MA1; -.
DR   TCDB; 1.C.114.1.2; the membrane permeabilizing peptide, moricin (moricin) family.
DR   EvolutionaryTrace; Q86MA1; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
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   3D-structure; Antibiotic; Antimicrobial; Immunity; Innate immunity;
KW   Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..67
FT                   /note="Moricin"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5004302503"
FT   HELIX           30..60
FT                   /evidence="ECO:0007829|PDB:2JR8"
SQ   SEQUENCE   67 AA;  7206 MW;  2BD160C00565AFA9 CRC64;
     MKLTSLFIFV IVALSLLFSS TDAAPGKIPV KAIKQAGKVI GKGLRAINIA GTTHDVVSFF
     RPKKKKH