ID   SRX2A_SARPE             Reviewed;         294 AA.
AC   P14667;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Sarcotoxin-2A;
DE   AltName: Full=Sarcotoxin IIA;
DE   Flags: Precursor;
OS   Sarcophaga peregrina (Flesh fly) (Boettcherisca peregrina).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC   Sarcophagidae; Sarcophaga; Boettcherisca.
OX   NCBI_TaxID=7386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND PYROGLUTAMATE
RP   FORMATION AT GLN-25.
RC   TISSUE=Hemolymph;
RX   PubMed=2452654; DOI=10.1021/bi00405a050;
RA   Ando K., Natori S.;
RT   "Molecular cloning, sequencing, and characterization of cDNA for sarcotoxin
RT   IIA, an inducible antibacterial protein of Sarcophaga peregrina (flesh
RT   fly).";
RL   Biochemistry 27:1715-1721(1988).
CC   -!- FUNCTION: Sarcotoxin II is an antibacterial protein which plays a role
CC       in the inflammatory response of this insect. The main effect of
CC       sarcotoxin II on E.coli may be the inhibition of cell wall synthesis,
CC       including septum formation.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Synthesized by the fat body and is eventually
CC       secreted into the hemolymph.
CC   -!- INDUCTION: In response to injury of the body wall of the larvae.
CC   -!- MISCELLANEOUS: Sarcotoxin II consists of at least four structurally
CC       related proteins named sarcotoxin IIa, II-1, II-2, and II-3.
CC   -!- SIMILARITY: Belongs to the attacin/sarcotoxin-2 family. {ECO:0000305}.
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DR   EMBL; M18873; AAA29987.1; -; mRNA.
DR   PIR; A27692; A27692.
DR   AlphaFoldDB; P14667; -.
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   Amidation; Antibiotic; Antimicrobial; Direct protein sequencing; Immunity;
KW   Innate immunity; Pyrrolidone carboxylic acid; Repeat; Secreted; Signal.
FT   SIGNAL          1..22
FT   PROPEP          23..24
FT                   /note="Removed by a dipeptidylpeptidase"
FT                   /id="PRO_0000004883"
FT   CHAIN           25..293
FT                   /note="Sarcotoxin-2A"
FT                   /id="PRO_0000004884"
FT   MOD_RES         25
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:2452654"
FT   MOD_RES         293
FT                   /note="Arginine amide"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   294 AA;  30820 MW;  B29438499B2FD728 CRC64;
     MKSFVFFAAC MAIIALSSLV QAYPQKLPVP IPPPTNPPVA AFHNSVATNS KGGQDVSVKL
     AATNLGNKHV QPIAEVFAEG NTKGGNVLRG ATVGVQGHGL GASVTKSQDG IAESFRKQAE
     ANLRLGDSAS LIGKVSQTDT KIKGIDFKPQ LSSSSLALQG DRLGASISRD VNRGVSDTLT
     KSVSANLFRN DNHNLDASVF RSDVRQNNGF NFQKTGGMLD YSHANGHGLN AGLTRFSGIG
     NQATVGGYST LFRSNDGLTS LKANAGGSQW LSGPFANQRD YSFGLGLSHN AWRG