ID   FPIF_BOMMO              Reviewed;          77 AA.
AC   Q10731;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Fungal protease inhibitor F;
DE            Short=FPI-F;
DE   Flags: Precursor;
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].
RX   PubMed=8827441; DOI=10.1093/oxfordjournals.jbchem.a021351;
RA   Pham T.-N., Hayashi K., Takano R., Nakazawa H., Mori H., Ichida M.,
RA   Itoh M., Eguchi M., Matsubara F., Hara S.;
RT   "Expression of Bombyx family fungal protease inhibitor F from Bombyx mori
RT   by baculovirus vector.";
RL   J. Biochem. 119:1080-1085(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C124; TISSUE=Fat body;
RA   Itoh M., Takenaka T., Ashikari T., Eguchi M.;
RT   "cDNA cloning and expression of a novel type protease inhibitor (FPI-F)
RT   from the silkworm, Bombyx mori.";
RL   Nihon Sanshigaku Zasshi 65:326-333(1996).
RN   [3]
RP   PROTEIN SEQUENCE OF 23-77.
RX   PubMed=7961602; DOI=10.1093/oxfordjournals.jbchem.a124434;
RA   Eguchi M., Itoh M., Nishino K., Shibata H., Tanaka T., Kamei-Hayashi K.,
RA   Hara S.;
RT   "Amino acid sequence of an inhibitor from the silkworm (Bombyx mori)
RT   hemolymph against fungal protease.";
RL   J. Biochem. 115:881-884(1994).
RN   [4]
RP   DISULFIDE BONDS.
RX   PubMed=8830035; DOI=10.1093/oxfordjournals.jbchem.a021259;
RA   Pham T.-N., Hayashi K., Takano R., Itoh M., Eguchi M., Shibata H.,
RA   Tanaka T., Hara S.;
RT   "A new family of serine protease inhibitors (Bombyx family) as established
RT   from the unique topological relation between the positions of disulphide
RT   bridges and reactive site.";
RL   J. Biochem. 119:428-434(1996).
CC   -!- FUNCTION: Highly specific for fungal protease and subtilisin.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Hemolymph.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I40 family.
CC       {ECO:0000305}.
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DR   EMBL; S83181; AAB46908.1; -; mRNA.
DR   EMBL; D38075; BAA22409.1; -; mRNA.
DR   PIR; JC4790; JC4790.
DR   RefSeq; NP_001037532.1; NM_001044067.1.
DR   AlphaFoldDB; Q10731; -.
DR   SMR; Q10731; -.
DR   MEROPS; I08.050; -.
DR   GeneID; 693072; -.
DR   Proteomes; UP000005204; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR036084; Ser_inhib-like_sf.
DR   InterPro; IPR002919; TIL_dom.
DR   Pfam; PF01826; TIL; 1.
DR   SUPFAM; SSF57567; SSF57567; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW   Reference proteome; Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..77
FT                   /note="Fungal protease inhibitor F"
FT                   /id="PRO_0000026724"
FT   SITE            51..52
FT                   /note="Reactive bond"
FT   DISULFID        25..57
FT                   /evidence="ECO:0000269|PubMed:8830035"
FT   DISULFID        36..49
FT                   /evidence="ECO:0000269|PubMed:8830035"
FT   DISULFID        40..77
FT                   /evidence="ECO:0000269|PubMed:8830035"
FT   DISULFID        59..71
FT                   /evidence="ECO:0000269|PubMed:8830035"
SQ   SEQUENCE   77 AA;  8492 MW;  B9CFC085DDA10354 CRC64;
     MASKNLFVLF FIFALFAANI AALQCPKNSE VRNSPCPRTC NDPYGQNSCI TVIRETCHCK
     GELVFDSDSI CVPISQC