MOR1_BOMMO
ID MOR1_BOMMO Reviewed; 66 AA.
AC P82818;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Moricin-1;
DE Flags: Precursor;
GN Name=MOR1; Synonyms=MOR;
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], INDUCTION, TISSUE SPECIFICITY, AND
RP 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).
RN [3]
RP STRUCTURE BY NMR OF 25-66.
RX PubMed=11997013; DOI=10.1016/s0014-5793(02)02637-6;
RA Hemmi H., Ishibashi J., Hara S., Yamakawa M.;
RT "Solution structure of moricin, an antibacterial peptide, isolated from the
RT silkworm Bombyx mori.";
RL FEBS Lett. 518:33-38(2002).
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; AB006915; BAB13508.1; -; mRNA.
DR PDB; 1KV4; NMR; -; A=25-66.
DR PDBsum; 1KV4; -.
DR AlphaFoldDB; P82818; -.
DR BMRB; P82818; -.
DR SMR; P82818; -.
DR STRING; 7091.BGIBMGA011495-TA; -.
DR TCDB; 1.C.114.1.1; the membrane permeabilizing peptide, moricin (moricin) family.
DR eggNOG; ENOG502TCRK; Eukaryota.
DR HOGENOM; CLU_206132_1_0_1; -.
DR InParanoid; P82818; -.
DR EvolutionaryTrace; P82818; -.
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 3D-structure; Antibiotic; Antimicrobial; Direct protein sequencing;
KW Immunity; Innate immunity; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:8530391"
FT CHAIN 25..66
FT /note="Moricin-1"
FT /id="PRO_0000004992"
FT HELIX 29..58
FT /evidence="ECO:0007829|PDB:1KV4"
SQ SEQUENCE 66 AA; 7163 MW; 08D5DFAA20F63FEE CRC64;
MNILKFFFVF IVAMSLVSCS TAAPAKIPIK AIKTVGKAVG KGLRAINIAS TANDVFNFLK
PKKRKH
