ID   ATTE_HYACE              Reviewed;         235 AA.
AC   P01513;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Attacin-E;
DE   AltName: Full=Immune protein P5;
DE   Contains:
DE     RecName: Full=Attacin-F;
DE   Flags: Precursor;
OS   Hyalophora cecropia (Cecropia moth) (Samia cecropia).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Saturniidae; Saturniinae; Attacini; Hyalophora.
OX   NCBI_TaxID=7123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=2001705; DOI=10.1111/j.1432-1033.1991.tb15811.x;
RA   Sun S.C., Lindstroem I., Lee J.-Y., Faye I.;
RT   "Structure and expression of the attacin genes in Hyalophora cecropia.";
RL   Eur. J. Biochem. 196:247-254(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 48-235.
RX   PubMed=16453548; DOI=10.1002/j.1460-2075.1984.tb02093.x;
RA   Kockum K., Faye I., von Hofsten P., Lee J.-Y., Xanthopoulos K.G.,
RA   Boman H.G.;
RT   "Insect immunity. Isolation and sequence of two cDNA clones corresponding
RT   to acidic and basic attacins from Hyalophora cecropia.";
RL   EMBO J. 3:2071-2075(1984).
RN   [3]
RP   NUCLEOTIDE SEQUENCE OF 48-235.
RX   PubMed=3840100; DOI=10.1016/0145-305x(85)90018-7;
RA   Boman H.G., Faye I., von Hofsten P., Kockum K., Lee J.-Y.,
RA   Xanthopoulos K.G., Bennich H., Engstroem A., Merrifield R.B., Andreu D.;
RT   "On the primary structures of lysozyme, cecropins and attacins from
RT   Hyalophora cecropia.";
RL   Dev. Comp. Immunol. 9:551-558(1985).
RN   [4]
RP   PROTEIN SEQUENCE OF 48-231.
RX   PubMed=16453547; DOI=10.1002/j.1460-2075.1984.tb02092.x;
RA   Engstroem A., Engstroem P., Tao Z.-J., Carlsson A., Bennich H.;
RT   "Insect immunity. The primary structure of the antibacterial protein
RT   attacin F and its relation to two native attacins from Hyalophora
RT   cecropia.";
RL   EMBO J. 3:2065-2070(1984).
CC   -!- FUNCTION: Hemolymph antibacterial protein.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: Attacin F appears to be derived by proteolytic digestion of
CC       attacin E.
CC   -!- MISCELLANEOUS: There are six forms of attacin that are divided into two
CC       groups: acidic (E and F) and basic (A, B, C, and D).
CC   -!- SIMILARITY: Belongs to the attacin/sarcotoxin-2 family. {ECO:0000305}.
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DR   EMBL; X57715; CAA40886.1; -; Genomic_DNA.
DR   EMBL; X00869; CAA25414.1; -; mRNA.
DR   EMBL; M34926; AAA29183.1; -; mRNA.
DR   PIR; S14104; EWWKEC.
DR   AlphaFoldDB; P01513; -.
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   InterPro; IPR005521; Attacin_C.
DR   InterPro; IPR005520; Attacin_N.
DR   Pfam; PF03769; Attacin_C; 1.
DR   Pfam; PF03768; Attacin_N; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Immunity; Innate immunity; Repeat; Secreted;
KW   Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..47
FT                   /evidence="ECO:0000269|PubMed:16453547"
FT                   /id="PRO_0000004902"
FT   CHAIN           48..235
FT                   /note="Attacin-E"
FT                   /id="PRO_0000004903"
FT   CHAIN           48..231
FT                   /note="Attacin-F"
FT                   /id="PRO_0000004904"
SQ   SEQUENCE   235 AA;  25438 MW;  35E1B549FB0417D1 CRC64;
     MFGKIVFLLL VALCAGVQSR YLIVSEPVYY IEHYEEPELL ASSRVRRDAH GALTLNSDGT
     SGAVVKVPFA GNDKNIVSAI GSVDLTDRQK LGAATAGVAL DNINGHGLSL TDTHIPGFGD
     KMTAAGKVNV FHNDNHDITA KAFATRNMPD IANVPNFNTV GGGIDYMFKD KIGASASAAH
     TDFINRNDYS LDGKLNLFKT PDTSIDFNAG FKKFDTPFMK SSWEPNFGFS LSKYF