ID   API_TRICO               Reviewed;         228 AA.
AC   P59704;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2003, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Aspartyl protease inhibitor;
DE   AltName: Full=Tco-API-1;
DE   Flags: Precursor;
OS   Trichostrongylus colubriformis (Black scour worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC   Trichostrongyloidea; Trichostrongylidae; Trichostrongylus.
OX   NCBI_TaxID=6319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=13678638; DOI=10.1016/s0020-7519(03)00157-7;
RA   Shaw R.J., McNeill M.M., Maass D.R., Hein W.R., Barber T.K., Wheeler M.,
RA   Morris C.A., Shoemaker C.B.;
RT   "Identification and characterisation of an aspartyl protease inhibitor
RT   homologue as a major allergen of Trichostrongylus colubriformis.";
RL   Int. J. Parasitol. 33:1233-1243(2003).
CC   -!- FUNCTION: Aspartyl protease inhibitor.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- ALLERGEN: Causes an allergic reaction in human.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I33 family.
CC       {ECO:0000305}.
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DR   EMBL; AY189824; AAO34715.1; -; mRNA.
DR   AlphaFoldDB; P59704; -.
DR   SMR; P59704; -.
DR   MEROPS; I33.002; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0019828; F:aspartic-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1120.50; -; 2.
DR   InterPro; IPR010480; Pepsin-I3.
DR   InterPro; IPR038412; Pepsin-I3_sf.
DR   Pfam; PF06394; Pepsin-I3; 2.
PE   1: Evidence at protein level;
KW   Allergen; Aspartic protease inhibitor; Disulfide bond; Protease inhibitor;
KW   Secreted; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..228
FT                   /note="Aspartyl protease inhibitor"
FT                   /id="PRO_0000002400"
FT   REGION          88..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..114
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        134..224
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   228 AA;  25414 MW;  C265A6ECB5EBCE85 CRC64;
     MKLIELCVLC AIAFAAPRQK RLTVGTIAVT GGVGGASGCV VTGNVLYANG FRLRELSASE
     QQELTNYEKQ VAEYKASVKQ ILKERQEKLK SRMSGKKEEK AAVTSTKDED LPKPPQKPSF
     CTEDDTTQFY FDGCMVQGNK VYVGNTFARD LDQNEIEELK EFEKKQTVYQ EYVQKQIQQQ
     VSNLFGGADF FSSFFGDAKD QTTTTVAPVL PEDAPEQPAV PNFCTRIY