ICW3_PSOTE
ID ICW3_PSOTE Reviewed; 207 AA.
AC P10822;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 2.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Chymotrypsin inhibitor 3;
DE AltName: Full=WCI-3;
DE Flags: Precursor;
OS Psophocarpus tetragonolobus (Winged bean) (Dolichos tetragonolobus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Psophocarpus.
OX NCBI_TaxID=3891;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Peyachoknagul S., Matsui T., Shibata H., Hara S., Ikenaka T., Okada Y.,
RA Ohno T.;
RT "Sequence and expression of the mRNA encoding the chymotrypsin inhibitor in
RT winged bean (Psophocarpus tetragonolobus (L.) DC.).";
RL Plant Mol. Biol. 12:51-58(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=1569049; DOI=10.1093/oxfordjournals.jbchem.a123745;
RA Habu Y., Peyachoknagul S., Umemoto K., Sakata Y., Ohno T.;
RT "Structure and regulated expression of Kunitz chymotrypsin inhibitor genes
RT in winged bean [Psophocarpus tetragonolobus (L.) DC.].";
RL J. Biochem. 111:249-258(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8292779; DOI=10.1007/bf00042348;
RA Habu Y., Sakata Y., Fukasawa K., Ohno T.;
RT "Ubiquitous nuclear proteins bind to 5' upstream region of major Kunitz
RT chymotrypsin inhibitor gene in winged bean.";
RL Plant Mol. Biol. 23:1139-1150(1993).
RN [4]
RP PROTEIN SEQUENCE OF 25-207.
RX PubMed=3240995; DOI=10.1093/oxfordjournals.jbchem.a122506;
RA Shibata H., Hara S., Ikenaka T.;
RT "Amino acid sequence of winged bean (Psophocarpus tetragonolobus (L.) DC.)
RT chymotrypsin inhibitor, WCI-3.";
RL J. Biochem. 104:537-543(1988).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS).
RC TISSUE=Seed;
RX PubMed=15299674; DOI=10.1107/s0907444996000224;
RA Dattagupta J.K., Podder A., Chakrabarti C., Sen U., Dutta S.K., Singh M.;
RT "Structure of a Kunitz-type chymotrypsin from winged bean seeds at 2.95-A
RT resolution.";
RL Acta Crystallogr. D 52:521-528(1996).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=10328267;
RX DOI=10.1002/(sici)1097-0134(19990515)35:3<321::aid-prot6>3.0.co;2-y;
RA Dattagupta J.K., Podder A., Chakrabarti C., Sen U., Mukhopadhyay D.,
RA Dutta S.K., Singh M.;
RT "Refined crystal structure (2.3 A) of a double-headed winged bean alpha-
RT chymotrypsin inhibitor and location of its second reactive site.";
RL Proteins 35:321-331(1999).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.13 ANGSTROMS).
RX PubMed=10531477; DOI=10.1107/s0907444999009877;
RA Ravichandran S., Sen U., Chakrabarti C., Dattagupta J.K.;
RT "Cryocrystallography of a Kunitz-type serine protease inhibitor: the 90 K
RT structure of winged bean chymotrypsin inhibitor (WCI) at 2.13 A
RT resolution.";
RL Acta Crystallogr. D 55:1814-1821(1999).
CC -!- FUNCTION: Inhibits alpha-chymotrypsin at the molar ratio of 1:2 in
CC state of 1:1.
CC -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC type inhibitor) family. {ECO:0000305}.
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; S96732; AAC60535.1; -; Genomic_DNA.
DR EMBL; D13974; BAA03084.1; -; mRNA.
DR EMBL; D13975; BAA03085.1; -; Genomic_DNA.
DR EMBL; D13976; BAA03086.1; -; Genomic_DNA.
DR PIR; JX0206; JX0206.
DR PDB; 1EYL; X-ray; 1.90 A; A=25-207.
DR PDB; 1FMZ; X-ray; 2.05 A; A=25-207.
DR PDB; 1FN0; X-ray; 2.00 A; A=25-207.
DR PDB; 1WBC; X-ray; 2.95 A; A=25-207.
DR PDB; 1XG6; X-ray; 2.15 A; A=25-207.
DR PDB; 2BEA; X-ray; 2.35 A; A/B=25-207.
DR PDB; 2BEB; X-ray; 2.81 A; A/B=25-207.
DR PDB; 2ESU; X-ray; 1.94 A; A=25-207.
DR PDB; 2ET2; X-ray; 2.10 A; A=25-207.
DR PDB; 2QYI; X-ray; 2.60 A; B/D=25-207.
DR PDB; 2WBC; X-ray; 2.30 A; A=25-207.
DR PDB; 3I29; X-ray; 2.40 A; B=25-207.
DR PDB; 3I2A; X-ray; 2.30 A; A/B=25-207.
DR PDB; 3I2X; X-ray; 2.85 A; A/B=25-207.
DR PDB; 3QYD; X-ray; 2.97 A; A/B/C=25-201.
DR PDB; 3VEQ; X-ray; 2.25 A; A=25-207.
DR PDB; 4H9W; X-ray; 2.50 A; A=25-207.
DR PDB; 4HA2; X-ray; 2.90 A; A/B=25-207.
DR PDB; 4TLP; X-ray; 1.90 A; A=26-200.
DR PDB; 4WBC; X-ray; 2.14 A; A=25-207.
DR PDBsum; 1EYL; -.
DR PDBsum; 1FMZ; -.
DR PDBsum; 1FN0; -.
DR PDBsum; 1WBC; -.
DR PDBsum; 1XG6; -.
DR PDBsum; 2BEA; -.
DR PDBsum; 2BEB; -.
DR PDBsum; 2ESU; -.
DR PDBsum; 2ET2; -.
DR PDBsum; 2QYI; -.
DR PDBsum; 2WBC; -.
DR PDBsum; 3I29; -.
DR PDBsum; 3I2A; -.
DR PDBsum; 3I2X; -.
DR PDBsum; 3QYD; -.
DR PDBsum; 3VEQ; -.
DR PDBsum; 4H9W; -.
DR PDBsum; 4HA2; -.
DR PDBsum; 4TLP; -.
DR PDBsum; 4WBC; -.
DR AlphaFoldDB; P10822; -.
DR SMR; P10822; -.
DR MEROPS; I03.009; -.
DR EvolutionaryTrace; P10822; -.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00178; STI; 1.
DR InterPro; IPR011065; Kunitz_inhibitor_STI-like_sf.
DR InterPro; IPR002160; Prot_inh_Kunz-lg.
DR PANTHER; PTHR33107; PTHR33107; 1.
DR Pfam; PF00197; Kunitz_legume; 1.
DR PRINTS; PR00291; KUNITZINHBTR.
DR SMART; SM00452; STI; 1.
DR SUPFAM; SSF50386; SSF50386; 1.
DR PROSITE; PS00283; SOYBEAN_KUNITZ; 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..24
FT /evidence="ECO:0000269|PubMed:3240995"
FT CHAIN 25..207
FT /note="Chymotrypsin inhibitor 3"
FT /id="PRO_0000016893"
FT SITE 89..90
FT /note="Reactive bond for chymotrypsin"
FT DISULFID 65..109
FT DISULFID 159..168
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1EYL"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:1EYL"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:1EYL"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:1EYL"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:3VEQ"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:1EYL"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:3I29"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:1EYL"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:4TLP"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:1EYL"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:1EYL"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1EYL"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:1EYL"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:1EYL"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:1EYL"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:3VEQ"
FT STRAND 154..161
FT /evidence="ECO:0007829|PDB:1EYL"
FT STRAND 163..176
FT /evidence="ECO:0007829|PDB:1EYL"
FT STRAND 182..189
FT /evidence="ECO:0007829|PDB:1EYL"
FT STRAND 193..198
FT /evidence="ECO:0007829|PDB:1EYL"
SQ SEQUENCE 207 AA; 22774 MW; E8D164DB6D2D616A CRC64;
MKSTTFLALF LLSAIISHLP SSTADDDLVD AEGNLVENGG TYYLLPHIWA HGGGIETAKT
GNEPCPLTVV RSPNEVSKGE PIRISSQFLS LFIPRGSLVA LGFANPPSCA ASPWWTVVDS
PQGPAVKLSQ QKLPEKDILV FKFEKVSHSN IHVYKLLYCQ HDEEDVKCDQ YIGIHRDRNG
NRRLVVTEEN PLELVLLKAK SETASSH
