ID   ICE1_ASCSU              Reviewed;          63 AA.
AC   P07851; O77419;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Chymotrypsin/elastase isoinhibitor 1;
DE   AltName: Full=AsC/E-1;
DE   AltName: Full=C/E-1 inhibitor;
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=6564898; DOI=10.1016/0003-9861(84)90530-7;
RA   Babin D.R., Peanasky R.J., Goos S.M.;
RT   "The isoinhibitors of chymotrypsin/elastase from Ascaris lumbricoides: the
RT   primary structure.";
RL   Arch. Biochem. Biophys. 232:143-161(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9635450; DOI=10.1006/expr.1998.4284;
RA   Lu C.C., Nguyen T., Morris S., Hill D., Sakanari J.A.;
RT   "Anisakis simplex: mutational bursts in the reactive site centers of serine
RT   protease inhibitors from an ascarid nematode.";
RL   Exp. Parasitol. 89:257-261(1998).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF COMPLEX WITH ELASTASE, AND
RP   DISULFIDE BOND.
RX   PubMed=7922044; DOI=10.1016/s0969-2126(00)00068-x;
RA   Huang K., Strynadka N.C., Bernard V.D., Peanasky R.J., James M.N.;
RT   "The molecular structure of the complex of Ascaris chymotrypsin/elastase
RT   inhibitor with porcine elastase.";
RL   Structure 2:679-689(1994).
CC   -!- FUNCTION: Defends the organism against the host's proteinases.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the serine protease inhibitor-like (TIL domain-
CC       containing) family. {ECO:0000305}.
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DR   EMBL; U94499; AAC61300.1; -; mRNA.
DR   PDB; 1EAI; X-ray; 2.40 A; C/D=1-61.
DR   PDBsum; 1EAI; -.
DR   AlphaFoldDB; P07851; -.
DR   SMR; P07851; -.
DR   MEROPS; I08.001; -.
DR   EvolutionaryTrace; P07851; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR036084; Ser_inhib-like_sf.
DR   InterPro; IPR002919; TIL_dom.
DR   Pfam; PF01826; TIL; 1.
DR   SUPFAM; SSF57567; SSF57567; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Protease inhibitor; Secreted; Serine protease inhibitor.
FT   CHAIN           1..63
FT                   /note="Chymotrypsin/elastase isoinhibitor 1"
FT                   /id="PRO_0000174329"
FT   DOMAIN          5..60
FT                   /note="TIL"
FT   SITE            31..32
FT                   /note="Reactive bond"
FT                   /evidence="ECO:0000305|PubMed:7922044"
FT   DISULFID        5..38
FT                   /evidence="ECO:0000269|PubMed:7922044,
FT                   ECO:0000312|PDB:1EAI"
FT   DISULFID        14..33
FT                   /evidence="ECO:0000269|PubMed:7922044,
FT                   ECO:0000312|PDB:1EAI"
FT   DISULFID        17..29
FT                   /evidence="ECO:0000269|PubMed:7922044,
FT                   ECO:0000312|PDB:1EAI"
FT   DISULFID        21..60
FT                   /evidence="ECO:0000269|PubMed:7922044,
FT                   ECO:0000312|PDB:1EAI"
FT   DISULFID        40..54
FT                   /evidence="ECO:0000269|PubMed:7922044,
FT                   ECO:0000312|PDB:1EAI"
FT   CONFLICT        4
FT                   /note="S -> R (in Ref. 2; AAC61300)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        23..24
FT                   /note="PD -> DP (in Ref. 2; AAC61300)"
FT                   /evidence="ECO:0000305"
FT   STRAND          10..15
FT                   /evidence="ECO:0007829|PDB:1EAI"
FT   STRAND          20..22
FT                   /evidence="ECO:0007829|PDB:1EAI"
FT   STRAND          28..32
FT                   /evidence="ECO:0007829|PDB:1EAI"
FT   STRAND          37..39
FT                   /evidence="ECO:0007829|PDB:1EAI"
FT   HELIX           42..44
FT                   /evidence="ECO:0007829|PDB:1EAI"
FT   STRAND          46..48
FT                   /evidence="ECO:0007829|PDB:1EAI"
FT   STRAND          54..56
FT                   /evidence="ECO:0007829|PDB:1EAI"
FT   HELIX           57..59
FT                   /evidence="ECO:0007829|PDB:1EAI"
SQ   SEQUENCE   63 AA;  6862 MW;  5DC10DE75B375F16 CRC64;
     GQESCGPNEV WTECTGCEMK CGPDENTPCP LMCRRPSCEC SPGRGMRRTN DGKCIPASQC
     PEH