ITC_ALOMA
ID ITC_ALOMA Reviewed; 184 AA.
AC P35812;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Trypsin/chymotrypsin inhibitor;
OS Alocasia macrorrhizos (Giant taro) (Arum macrorrhizon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Araceae; Aroideae; Colocasieae;
OC Alocasia.
OX NCBI_TaxID=4456;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=cv. Fui-1;
RX PubMed=8142459; DOI=10.1016/0167-4838(94)90008-6;
RA Argall M.E., Brandbury H.J., Shaw D.C.;
RT "Amino-acid sequence of a trypsin/chymotrypsin inhibitor from giant taro
RT (Alocasia macrorrhiza).";
RL Biochim. Biophys. Acta 1204:189-194(1994).
CC -!- FUNCTION: Inhibits trypsin and alpha-chymotrypsin.
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the protease inhibitor I3 (leguminous Kunitz-
CC type inhibitor) family. {ECO:0000305}.
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DR PDB; 5WVX; X-ray; 3.00 A; A/B=1-184.
DR PDB; 5YCZ; X-ray; 2.50 A; A/B=1-184.
DR PDBsum; 5WVX; -.
DR PDBsum; 5YCZ; -.
DR AlphaFoldDB; P35812; -.
DR SMR; P35812; -.
DR MEROPS; I03.003; -.
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; IPR016308; Prot_inh_API-A/B.
DR InterPro; IPR002160; Prot_inh_Kunz-lg.
DR PANTHER; PTHR33107; PTHR33107; 1.
DR Pfam; PF00197; Kunitz_legume; 1.
DR PIRSF; PIRSF001653; API-B; 1.
DR SMART; SM00452; STI; 1.
DR SUPFAM; SSF50386; SSF50386; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Protease inhibitor; Serine protease inhibitor.
FT CHAIN 1..184
FT /note="Trypsin/chymotrypsin inhibitor"
FT /id="PRO_0000083307"
FT SITE 56..57
FT /note="Reactive bond"
FT /evidence="ECO:0000255"
FT DISULFID 39..84
FT /evidence="ECO:0000250"
FT DISULFID 136..147
FT /evidence="ECO:0000250"
FT VARIANT 24
FT /note="M -> A (in 50% of the molecules)"
FT VARIANT 50
FT /note="E -> K (in 25% of the molecules)"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:5YCZ"
FT STRAND 18..27
FT /evidence="ECO:0007829|PDB:5YCZ"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:5YCZ"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:5YCZ"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:5WVX"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:5YCZ"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:5WVX"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:5YCZ"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:5YCZ"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:5YCZ"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:5YCZ"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:5YCZ"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:5WVX"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:5YCZ"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:5WVX"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:5YCZ"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:5WVX"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:5YCZ"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:5WVX"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:5YCZ"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:5YCZ"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:5YCZ"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:5YCZ"
SQ SEQUENCE 184 AA; 19774 MW; 60536E9C15F472ED CRC64;
TNPVLDVDGN ELQRGQLYYA TSVMRPGGGL TLAAPKGSCP LNVAQAPFDE YSGRPLAFFP
ENADDDTVQE GSTLYIMFPE PTRCPQSTVW TFDREAGFVT TGGTTSKAIG PHNSRFAIRK
AGDASSQPRD YQIEVCPCST GVERPSCRMG CLGTLGLAEG GKNVLLNINN ESPHTIRFVK
VKEG
