STMX_STOCA
ID STMX_STOCA Reviewed; 67 AA.
AC Q8T9R8;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Stomoxyn;
DE Flags: Precursor;
OS Stomoxys calcitrans (Stable fly) (Conops calcitrans).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC Muscidae; Stomoxys.
OX NCBI_TaxID=35570 {ECO:0000312|EMBL:AAL77057.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 25-57, FUNCTION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND AMIDATION AT THR-66.
RC TISSUE=Midgut {ECO:0000269|PubMed:12372834};
RX PubMed=12372834; DOI=10.1074/jbc.m206296200;
RA Boulanger N., Munks R.J.L., Hamilton J.V., Vovelle F., Brun R.,
RA Lehane M.J., Bulet P.;
RT "Epithelial innate immunity. A novel antimicrobial peptide with
RT antiparasitic activity in the blood-sucking insect Stomoxys calcitrans.";
RL J. Biol. Chem. 277:49921-49926(2002).
RN [2]
RP STRUCTURE BY NMR.
RX PubMed=16170803; DOI=10.1002/bip.20370;
RA Landon C., Meudal H., Boulanger N., Bulet P., Vovelle F.;
RT "Solution structures of stomoxyn and spinigerin, two insect antimicrobial
RT peptides with an alpha-helical conformation.";
RL Biopolymers 81:92-103(2006).
CC -!- FUNCTION: Has antimicrobial activity against most Gram-positive and
CC Gram-negative bacteria, filamentous fungi and yeasts tested. Has
CC trypanolytic effect on T.b.rhodesiense and limited hemolytic activity
CC against bovine red blood cells. {ECO:0000269|PubMed:12372834}.
CC -!- FUNCTION: May play an important role in protecting the stored blood in
CC the anterior midgut from microorganisms prior to digestion. Adopts an
CC amphipathic alpha-helical structure only in the presence of an organic
CC solvent that mimics a phospholipid membrane.
CC {ECO:0000269|PubMed:12372834, ECO:0000303|PubMed:12372834}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12372834}.
CC -!- TISSUE SPECIFICITY: Constitutively expressed in the adult anterior
CC midgut; proventriculus, thoracic and reservoir regions.
CC {ECO:0000269|PubMed:12372834}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF467987; AAL77057.1; -; mRNA.
DR PDB; 1ZRX; NMR; -; A=25-66.
DR PDBsum; 1ZRX; -.
DR AlphaFoldDB; Q8T9R8; -.
DR SMR; Q8T9R8; -.
DR VEuPathDB; VectorBase:SCAU016937; -.
DR EvolutionaryTrace; Q8T9R8; -.
DR Proteomes; UP000095300; Unplaced.
DR GO; GO:0005576; C:extracellular region; TAS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0006805; P:xenobiotic metabolic process; IDA:UniProtKB.
DR InterPro; IPR021037; Stomoxyn.
DR Pfam; PF11585; Stomoxyn; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amidation; Antibiotic; Antimicrobial;
KW Direct protein sequencing; Fungicide; Immunity; Innate immunity; Secreted;
KW Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:12372834"
FT PEPTIDE 25..66
FT /note="Stomoxyn"
FT /evidence="ECO:0000269|PubMed:12372834"
FT /id="PRO_0000004950"
FT MOD_RES 66
FT /note="Threonine amide"
FT /evidence="ECO:0000269|PubMed:12372834"
FT HELIX 28..46
FT /evidence="ECO:0007829|PDB:1ZRX"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:1ZRX"
FT TURN 52..55
FT /evidence="ECO:0007829|PDB:1ZRX"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:1ZRX"
FT HELIX 60..65
FT /evidence="ECO:0007829|PDB:1ZRX"
SQ SEQUENCE 67 AA; 7173 MW; 4D004C8298431429 CRC64;
MNFYKYLVVL VVLVLCLSAT QTEARGFRKH FNKLVKKVKH TISETAHVAK DTAVIAGSGA
AVVAATG
