ISC2_BOMMO
ID ISC2_BOMMO Reviewed; 62 AA.
AC P10832;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Chymotrypsin inhibitor SCI-II;
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 PROTEIN SEQUENCE.
RC TISSUE=Larval hemolymph;
RX PubMed=3072972; DOI=10.1515/bchm3.1988.369.2.1235;
RA Sasaki T.;
RT "Amino-acid sequences of two basic chymotrypsin inhibitors from silkworm
RT larval hemolymph.";
RL Biol. Chem. Hoppe-Seyler 369:1235-1241(1988).
CC -!- FUNCTION: Inhibits chymotrypsin and thus avoids the accidental
CC chymotrypsin-mediated activation of prophenoloxidase. This enzyme is
CC required by the insect immune system to produce melanin which is used
CC to engulf foreign objects.
CC -!- FUNCTION: Also inhibits trypsin weakly, this may be due to the presence
CC of a pseudo-reactive bond in positions 44-45 (Lys-Gly).
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DR PIR; S01803; S01803.
DR AlphaFoldDB; P10832; -.
DR SMR; P10832; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00109; KU; 1.
DR Gene3D; 4.10.410.10; -; 1.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 1.
DR SUPFAM; SSF57362; SSF57362; 1.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Protease inhibitor;
KW Reference proteome; Serine protease inhibitor.
FT CHAIN 1..62
FT /note="Chymotrypsin inhibitor SCI-II"
FT /id="PRO_0000155422"
FT DOMAIN 9..60
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT SITE 20..21
FT /note="Reactive bond"
FT /evidence="ECO:0000250"
FT SITE 44..45
FT /note="Pseudo reactive bond for trypsin"
FT DISULFID 9..60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 19..43
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 35..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
SQ SEQUENCE 62 AA; 7067 MW; 7E7C013DA05AC6DA CRC64;
DKPTTKPICE QAFGNSGPCF AYIKLYSYNQ KTKKCEEFIY GGCKGNDNRF DTLAECEQKC
IK