SRX22_SARPE
ID SRX22_SARPE Reviewed; 294 AA.
AC P24489;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Sarcotoxin II-2;
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 [GENOMIC DNA].
RX PubMed=2247051; DOI=10.1128/mcb.10.12.6114-6122.1990;
RA Kanai A., Natori S.;
RT "Analysis of a gene cluster for sarcotoxin II, a group of antibacterial
RT proteins of Sarcophaga peregrina.";
RL Mol. Cell. Biol. 10:6114-6122(1990).
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; D90154; BAA14183.1; -; Genomic_DNA.
DR PIR; B36351; B36351.
DR AlphaFoldDB; P24489; -.
DR SMR; P24489; -.
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 2: Evidence at transcript level;
KW Amidation; Antibiotic; Antimicrobial; Immunity; Innate immunity;
KW Pyrrolidone carboxylic acid; Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT PROPEP 23..24
FT /note="Removed by a dipeptidylpeptidase"
FT /id="PRO_0000004887"
FT CHAIN 25..293
FT /note="Sarcotoxin II-2"
FT /id="PRO_0000004888"
FT MOD_RES 25
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250"
FT MOD_RES 293
FT /note="Arginine amide"
FT /evidence="ECO:0000255"
SQ SEQUENCE 294 AA; 30856 MW; 3F8B69674DF67180 CRC64;
MKSFVFFAAC FAIVALNSLA HAYPQKLPVP IPPPTNPPVA AFHNSVATNS KGGQDVSVKL
AATNLGNKHV QPIAEVFAKG NTQGGNVLRG ATVGVQGHGL GASVTKTQDG IAESFRKQAE
ANLRLGDSAS LIGKVSQTDT KIKGIDFKPQ LSSSSLALQG DRLGASISRD VNRGVSDTLT
KSISANVFRN DNHNLDASVF RSDVRQNNGF NFQKTGGMLD YSHANGHGLN AGLTRFSGIG
NQANVGGYST LFRSNDGLTS LKANAGGSQW LSGPFANQRD YSFGLGLSHN AWRG