CHAG_TRYCR
ID CHAG_TRYCR Reviewed; 110 AA.
AC Q966X9;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Chagasin;
GN Name=cha;
OS Trypanosoma cruzi.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=5693;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=Dm28c;
RX PubMed=11719560; DOI=10.1242/jcs.114.21.3933;
RA Monteiro A.C.S., Abrahamson M., Lima A.P.C.A., Vannier-Santos M.A.,
RA Scharfstein J.;
RT "Identification, characterization and localization of chagasin, a tight-
RT binding cysteine protease inhibitor in Trypanosoma cruzi.";
RL J. Cell Sci. 114:3933-3942(2001).
CC -!- FUNCTION: Tight-binding and reversible inhibitor of papain-like
CC cysteine proteases. {ECO:0000269|PubMed:11719560}.
CC -!- INTERACTION:
CC Q966X9; Q9NBD4; Xeno; NbExp=2; IntAct=EBI-15637083, EBI-15637102;
CC -!- SUBCELLULAR LOCATION: Flagellar pocket {ECO:0000269|PubMed:11719560}.
CC Cytoplasmic vesicle {ECO:0000269|PubMed:11719560}. Cell surface
CC {ECO:0000269|PubMed:11719560}. Note=Flagellar pocket and cytoplasmic
CC vesicles of trypomastigotes and to the cell surface of amastigotes.
CC -!- SIMILARITY: Belongs to the protease inhibitor I42 family.
CC {ECO:0000305}.
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DR EMBL; AJ299433; CAC39242.1; -; mRNA.
DR PDB; 2FO8; NMR; -; A=2-110.
DR PDB; 2H7W; X-ray; 1.70 A; A/B=1-110.
DR PDB; 2NNR; X-ray; 1.70 A; A/B=1-110.
DR PDB; 2NQD; X-ray; 1.75 A; A=2-110.
DR PDB; 2OUL; X-ray; 2.20 A; B=1-110.
DR PDB; 3CBJ; X-ray; 1.80 A; B=1-110.
DR PDB; 3CBK; X-ray; 2.67 A; B=1-110.
DR PDB; 3E1Z; X-ray; 1.86 A; A=1-110.
DR PDBsum; 2FO8; -.
DR PDBsum; 2H7W; -.
DR PDBsum; 2NNR; -.
DR PDBsum; 2NQD; -.
DR PDBsum; 2OUL; -.
DR PDBsum; 3CBJ; -.
DR PDBsum; 3CBK; -.
DR PDBsum; 3E1Z; -.
DR AlphaFoldDB; Q966X9; -.
DR BMRB; Q966X9; -.
DR SMR; Q966X9; -.
DR DIP; DIP-29312N; -.
DR IntAct; Q966X9; 1.
DR MEROPS; I42.001; -.
DR PRIDE; Q966X9; -.
DR VEuPathDB; TriTrypDB:BCY84_05088; -.
DR VEuPathDB; TriTrypDB:BCY84_05574; -.
DR VEuPathDB; TriTrypDB:C3747_11g420c; -.
DR VEuPathDB; TriTrypDB:C4B63_187g86c; -.
DR VEuPathDB; TriTrypDB:C4B63_32g1409c; -.
DR VEuPathDB; TriTrypDB:TcBrA4_0010400; -.
DR VEuPathDB; TriTrypDB:TcCL_ESM08205; -.
DR VEuPathDB; TriTrypDB:TcCLB.506801.80; -.
DR VEuPathDB; TriTrypDB:TcCLB.511907.200; -.
DR VEuPathDB; TriTrypDB:TcG_08207; -.
DR VEuPathDB; TriTrypDB:TcYC6_0083230; -.
DR EvolutionaryTrace; Q966X9; -.
DR GO; GO:0009986; C:cell surface; IDA:CACAO.
DR GO; GO:0020016; C:ciliary pocket; IDA:CACAO.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:CACAO.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IDA:CACAO.
DR Gene3D; 2.60.40.2020; -; 1.
DR InterPro; IPR036331; Chagasin-like_sf.
DR InterPro; IPR018990; Prot_inh_I42_chagasin.
DR Pfam; PF09394; Inhibitor_I42; 1.
DR SUPFAM; SSF141066; SSF141066; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasmic vesicle; Protease inhibitor;
KW Thiol protease inhibitor.
FT CHAIN 1..110
FT /note="Chagasin"
FT /id="PRO_0000218291"
FT MOTIF 29..33
FT /note="NPTTG motif"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:2NNR"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:2H7W"
FT STRAND 13..17
FT /evidence="ECO:0007829|PDB:2H7W"
FT STRAND 21..28
FT /evidence="ECO:0007829|PDB:2H7W"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:2H7W"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:2H7W"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:2H7W"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:2H7W"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:2H7W"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:2H7W"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:2NQD"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:2H7W"
FT STRAND 79..90
FT /evidence="ECO:0007829|PDB:2H7W"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:2H7W"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:2FO8"
FT STRAND 101..110
FT /evidence="ECO:0007829|PDB:2H7W"
SQ SEQUENCE 110 AA; 12040 MW; 717F8448EAA38242 CRC64;
MSHKVTKAHN GATLTVAVGE LVEIQLPSNP TTGFAWYFEG GTKESPNESM FTVENKYFPP
DSKLLGAGGT EHFHVTVKAA GTHAVNLTYM RPWTGPSHDS ERFTVYLKAN
