ID   FPI1_ANTMY              Reviewed;         105 AA.
AC   B0JFB8;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   25-MAY-2022, entry version 24.
DE   RecName: Full=Fungal protease inhibitor-1;
DE   Flags: Precursor;
GN   Name=fpi-1 {ECO:0000312|EMBL:CAP74000.1};
OS   Antheraea mylitta (Tasar silkworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Saturniidae; Saturniinae; Saturniini; Antheraea.
OX   NCBI_TaxID=34739;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAP74000.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-34, AND FUNCTION.
RC   TISSUE=Hemolymph {ECO:0000269|PubMed:14505696}, and
RC   Integument {ECO:0000312|EMBL:CAP74000.1};
RX   PubMed=14505696; DOI=10.1016/s0965-1748(03)00117-6;
RA   Shrivastava B., Ghosh A.K.;
RT   "Protein purification, cDNA cloning and characterization of a protease
RT   inhibitor from the Indian tasar silkworm, Antheraea mylitta.";
RL   Insect Biochem. Mol. Biol. 33:1025-1033(2003).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 20-105, AND DISULFIDE BONDS.
RX   PubMed=19263521; DOI=10.1016/j.jsb.2008.12.010;
RA   Roy S., Aravind P., Madhurantakam C., Ghosh A.K., Sankaranarayanan R.,
RA   Das A.K.;
RT   "Crystal structure of a fungal protease inhibitor from Antheraea mylitta.";
RL   J. Struct. Biol. 166:79-87(2009).
CC   -!- FUNCTION: Inhibits proteases from the fungi A.oryzae and R.oryzae,
CC       trypsin and chymotrypsin. Does not inhibit protease from the bacterium
CC       B.licheniformis or papain. {ECO:0000269|PubMed:14505696}.
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DR   EMBL; AM939570; CAP74000.1; -; mRNA.
DR   EMBL; EU375895; ABY83296.1; -; mRNA.
DR   PDB; 3BT4; X-ray; 2.10 A; A=20-105.
DR   PDBsum; 3BT4; -.
DR   AlphaFoldDB; B0JFB8; -.
DR   SMR; B0JFB8; -.
DR   MEROPS; I83.001; -.
DR   EvolutionaryTrace; B0JFB8; -.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR021066; FPI1.
DR   Pfam; PF12190; amfpi-1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Protease inhibitor; Serine protease inhibitor; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:14505696"
FT   CHAIN           20..105
FT                   /note="Fungal protease inhibitor-1"
FT                   /evidence="ECO:0000269|PubMed:14505696"
FT                   /id="PRO_5000304145"
FT   DISULFID        23..56
FT                   /evidence="ECO:0000269|PubMed:19263521"
FT   DISULFID        28..58
FT                   /evidence="ECO:0000269|PubMed:19263521"
FT   DISULFID        33..59
FT                   /evidence="ECO:0000269|PubMed:19263521"
FT   DISULFID        42..62
FT                   /evidence="ECO:0000269|PubMed:19263521"
FT   DISULFID        72..93
FT                   /evidence="ECO:0000269|PubMed:19263521"
FT   DISULFID        87..98
FT                   /evidence="ECO:0000269|PubMed:19263521"
FT   HELIX           27..30
FT                   /evidence="ECO:0007829|PDB:3BT4"
FT   HELIX           39..41
FT                   /evidence="ECO:0007829|PDB:3BT4"
FT   STRAND          46..54
FT                   /evidence="ECO:0007829|PDB:3BT4"
FT   HELIX           55..57
FT                   /evidence="ECO:0007829|PDB:3BT4"
FT   STRAND          59..66
FT                   /evidence="ECO:0007829|PDB:3BT4"
FT   TURN            77..80
FT                   /evidence="ECO:0007829|PDB:3BT4"
FT   STRAND          84..87
FT                   /evidence="ECO:0007829|PDB:3BT4"
FT   STRAND          92..94
FT                   /evidence="ECO:0007829|PDB:3BT4"
FT   STRAND          97..99
FT                   /evidence="ECO:0007829|PDB:3BT4"
SQ   SEQUENCE   105 AA;  11330 MW;  E099F90CE0837E88 CRC64;
     MKAVITLLFL ACILVVTYGD LICGTNYCKD HPCTSPIARA SCRSPATYRA NHSGKCACCP
     ACVTLLRERA ACKTYSKEIG ETPSAVCQEP LKCLNGVCTK VTPRR