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Fungal protease inhibitor F (FPI-F)

 FPIF_BOMMO              Reviewed;          77 AA.
Q10731;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
23-MAY-2018, entry version 71.
RecName: Full=Fungal protease inhibitor F;
Short=FPI-F;
Flags: Precursor;
Bombyx mori (Silk moth).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Lepidoptera; Glossata; Ditrysia;
Bombycoidea; Bombycidae; Bombycinae; Bombyx.
NCBI_TaxID=7091;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8827441; DOI=10.1093/oxfordjournals.jbchem.a021351;
Pham T.-N., Hayashi K., Takano R., Nakazawa H., Mori H., Ichida M.,
Itoh M., Eguchi M., Matsubara F., Hara S.;
"Expression of Bombyx family fungal protease inhibitor F from Bombyx
mori by baculovirus vector.";
J. Biochem. 119:1080-1085(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C124; TISSUE=Fat body;
Itoh M., Takenaka T., Ashikari T., Eguchi M.;
"cDNA cloning and expression of a novel type protease inhibitor (FPI-
F) from the silkworm, Bombyx mori.";
Nihon Sanshigaku Zasshi 65:326-333(1996).
[3]
PROTEIN SEQUENCE OF 23-77.
PubMed=7961602;
Eguchi M., Itoh M., Nishino K., Shibata H., Tanaka T.,
Kamei-Hayashi K., Hara S.;
"Amino acid sequence of an inhibitor from the silkworm (Bombyx mori)
hemolymph against fungal protease.";
J. Biochem. 115:881-884(1994).
[4]
DISULFIDE BONDS.
PubMed=8830035; DOI=10.1093/oxfordjournals.jbchem.a021259;
Pham T.-N., Hayashi K., Takano R., Itoh M., Eguchi M., Shibata H.,
Tanaka T., Hara S.;
"A new family of serine protease inhibitors (Bombyx family) as
established from the unique topological relation between the positions
of disulphide bridges and reactive site.";
J. Biochem. 119:428-434(1996).
-!- FUNCTION: Highly specific for fungal protease and subtilisin.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Hemolymph.
-!- SIMILARITY: Belongs to the protease inhibitor I40 family.
{ECO:0000305}.
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EMBL; S83181; AAB46908.1; -; mRNA.
EMBL; D38075; BAA22409.1; -; mRNA.
PIR; JC4790; JC4790.
RefSeq; NP_001037532.1; NM_001044067.1.
UniGene; Bmo.161; -.
SMR; Q10731; -.
MEROPS; I08.050; -.
PRIDE; Q10731; -.
GeneID; 693072; -.
KEGG; bmor:693072; -.
Proteomes; UP000005204; Unassembled WGS sequence.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
InterPro; IPR036084; Ser_inhib-like_sf.
InterPro; IPR002919; TIL_dom.
Pfam; PF01826; TIL; 1.
SUPFAM; SSF57567; SSF57567; 1.
1: Evidence at protein level;
Complete proteome; Direct protein sequencing; Disulfide bond;
Protease inhibitor; Reference proteome; Secreted;
Serine protease inhibitor; Signal.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 77 Fungal protease inhibitor F.
/FTId=PRO_0000026724.
SITE 51 52 Reactive bond.
DISULFID 25 57 {ECO:0000269|PubMed:8830035}.
DISULFID 36 49 {ECO:0000269|PubMed:8830035}.
DISULFID 40 77 {ECO:0000269|PubMed:8830035}.
DISULFID 59 71 {ECO:0000269|PubMed:8830035}.
SEQUENCE 77 AA; 8492 MW; B9CFC085DDA10354 CRC64;
MASKNLFVLF FIFALFAANI AALQCPKNSE VRNSPCPRTC NDPYGQNSCI TVIRETCHCK
GELVFDSDSI CVPISQC


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