ID   ICIC_HIRME              Reviewed;          70 AA.
AC   P01051;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=Eglin C;
OS   Hirudo medicinalis (Medicinal leech).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Hirudinea; Hirudinida; Hirudiniformes; Hirudinidae; Hirudo.
OX   NCBI_TaxID=6421;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=6906312;
RA   Seemueller U., Eulitz M., Fritz H., Strobl A.;
RT   "Structure of the elastase-cathepsin G inhibitor of the leech Hirudo
RT   medicinalis.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 361:1841-1846(1980).
RN   [2]
RP   SEQUENCE REVISION TO 33.
RA   Fritz H., Seemuller U.;
RL   Submitted (MAR-1982) to the PIR data bank.
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) IN COMPLEX WITH SUBTILISIN.
RX   PubMed=3519213; DOI=10.1002/j.1460-2075.1986.tb04286.x;
RA   Bode W., Papamokos E., Musil D., Seemueller U., Fritz H.;
RT   "Refined 1.2 A crystal structure of the complex formed between subtilisin
RT   Carlsberg and the inhibitor eglin c. Molecular structure of eglin and its
RT   detailed interaction with subtilisin.";
RL   EMBO J. 5:813-818(1986).
RN   [4]
RP   STRUCTURE BY NMR.
RX   PubMed=2159339; DOI=10.1021/bi00458a018;
RA   Hyberts S.G., Wagner G.;
RT   "Sequence-specific 1H NMR assignments and secondary structure of eglin c.";
RL   Biochemistry 29:1465-1474(1990).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
RX   PubMed=1505678; DOI=10.1016/0014-5793(92)81082-w;
RA   Hipler K., Priestle J.P., Rahuel J., Gruetter M.G.;
RT   "X-ray crystal structure of the serine proteinase inhibitor eglin c at
RT   1.95-A resolution.";
RL   FEBS Lett. 309:139-145(1992).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=8425603; DOI=10.1016/0014-5793(93)81273-3;
RA   Betzel C., Dauter Z., Genov N., Lamzin V., Navaza J., Schnebli H.P.,
RA   Visanji M., Wilson K.S.;
RT   "Structure of the proteinase inhibitor eglin c with hydrolysed reactive
RT   centre at 2.0-A resolution.";
RL   FEBS Lett. 317:185-188(1993).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 4-70 IN COMPLEX WITH HUMAN CTRC.
RX   PubMed=23430245; DOI=10.1074/jbc.m113.457382;
RA   Batra J., Szabo A., Caulfield T.R., Soares A.S., Sahin-Toth M.,
RA   Radisky E.S.;
RT   "Long-range electrostatic complementarity governs substrate recognition by
RT   human chymotrypsin C, a key regulator of digestive enzyme activation.";
RL   J. Biol. Chem. 288:9848-9859(2013).
CC   -!- FUNCTION: Inhibits both elastase and cathepsin G.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I13 (potato type I serine
CC       protease inhibitor) family. {ECO:0000305}.
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DR   PIR; A94592; EILXCH.
DR   PDB; 1ACB; X-ray; 2.00 A; I=1-70.
DR   PDB; 1CSE; X-ray; 1.20 A; I=1-70.
DR   PDB; 1EGL; NMR; -; A=1-70.
DR   PDB; 1EGP; X-ray; 2.00 A; A=1-45, B=46-70.
DR   PDB; 1MEE; X-ray; 2.00 A; I=7-70.
DR   PDB; 1SBN; X-ray; 2.10 A; I=1-70.
DR   PDB; 1SIB; X-ray; 2.40 A; I=1-70.
DR   PDB; 1TEC; X-ray; 2.20 A; I=1-70.
DR   PDB; 2SEC; X-ray; 1.80 A; I=1-70.
DR   PDB; 2TEC; X-ray; 1.98 A; I=1-70.
DR   PDB; 3TEC; X-ray; 2.00 A; I=1-70.
DR   PDB; 4B1T; X-ray; 1.78 A; B/D=1-70.
DR   PDB; 4B2A; X-ray; 1.89 A; B/D=5-70.
DR   PDB; 4B2B; X-ray; 1.36 A; B/D=1-70.
DR   PDB; 4B2C; X-ray; 1.43 A; B/D=1-70.
DR   PDB; 4H4F; X-ray; 1.90 A; B=8-70.
DR   PDB; 7AM6; X-ray; 2.70 A; P=37-49.
DR   PDB; 7AM7; X-ray; 2.61 A; P=37-49.
DR   PDBsum; 1ACB; -.
DR   PDBsum; 1CSE; -.
DR   PDBsum; 1EGL; -.
DR   PDBsum; 1EGP; -.
DR   PDBsum; 1MEE; -.
DR   PDBsum; 1SBN; -.
DR   PDBsum; 1SIB; -.
DR   PDBsum; 1TEC; -.
DR   PDBsum; 2SEC; -.
DR   PDBsum; 2TEC; -.
DR   PDBsum; 3TEC; -.
DR   PDBsum; 4B1T; -.
DR   PDBsum; 4B2A; -.
DR   PDBsum; 4B2B; -.
DR   PDBsum; 4B2C; -.
DR   PDBsum; 4H4F; -.
DR   PDBsum; 7AM6; -.
DR   PDBsum; 7AM7; -.
DR   AlphaFoldDB; P01051; -.
DR   BMRB; P01051; -.
DR   SMR; P01051; -.
DR   DIP; DIP-6069N; -.
DR   MINT; P01051; -.
DR   MEROPS; I13.001; -.
DR   EvolutionaryTrace; P01051; -.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0009611; P:response to wounding; IEA:InterPro.
DR   InterPro; IPR000864; Prot_inh_pot1.
DR   InterPro; IPR036354; Prot_inh_pot1_sf.
DR   PANTHER; PTHR33091; PTHR33091; 1.
DR   Pfam; PF00280; potato_inhibit; 1.
DR   PRINTS; PR00292; POTATOINHBTR.
DR   SUPFAM; SSF54654; SSF54654; 1.
DR   PROSITE; PS00285; POTATO_INHIBITOR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Protease inhibitor;
KW   Serine protease inhibitor.
FT   CHAIN           1..70
FT                   /note="Eglin C"
FT                   /id="PRO_0000217645"
FT   SITE            45..46
FT                   /note="Reactive bond"
FT   HELIX           11..13
FT                   /evidence="ECO:0007829|PDB:1CSE"
FT   HELIX           18..28
FT                   /evidence="ECO:0007829|PDB:1CSE"
FT   STRAND          32..38
FT                   /evidence="ECO:0007829|PDB:1CSE"
FT   STRAND          42..44
FT                   /evidence="ECO:0007829|PDB:4B2B"
FT   STRAND          48..57
FT                   /evidence="ECO:0007829|PDB:1CSE"
FT   TURN            58..61
FT                   /evidence="ECO:0007829|PDB:1CSE"
FT   STRAND          68..70
FT                   /evidence="ECO:0007829|PDB:1CSE"
SQ   SEQUENCE   70 AA;  8091 MW;  7E5C5BBD39DC3C11 CRC64;
     TEFGSELKSF PEVVGKTVDQ AREYFTLHYP QYDVYFLPEG SPVTLDLRYN RVRVFYNPGT
     NVVNHVPHVG