ID   API_PARTN               Reviewed;         226 AA.
AC   Q9BN10;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Aspartyl protease inhibitor;
DE   AltName: Full=Pt-API-1;
DE   Flags: Precursor;
OS   Parelaphostrongylus tenuis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Strongylida;
OC   Metastrongyloidea; Protostrongylidae; Elaphostrongylinae;
OC   Parelaphostrongylus.
OX   NCBI_TaxID=148309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX   PubMed=12093670; DOI=10.1128/cdli.9.4.763-770.2002;
RA   Duffy M.S., MacAfee N.E.A., Burt M.D.B., Appleton J.A.;
RT   "An aspartyl protease inhibitor orthologue expressed by Parelaphostrongylus
RT   tenuis is immunogenic in an atypical host.";
RL   Clin. Diagn. Lab. Immunol. 9:763-770(2002).
CC   -!- FUNCTION: Aspartyl protease inhibitor. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in L1, L3, and adult male and female
CC       worms. {ECO:0000269|PubMed:12093670}.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I33 family.
CC       {ECO:0000305}.
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DR   EMBL; AF277291; AAG50205.1; -; mRNA.
DR   AlphaFoldDB; Q9BN10; -.
DR   SMR; Q9BN10; -.
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   2: Evidence at transcript level;
KW   Aspartic protease inhibitor; Disulfide bond; Protease inhibitor; Secreted;
KW   Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..226
FT                   /note="Aspartyl protease inhibitor"
FT                   /id="PRO_0000002399"
FT   REGION          95..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          196..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..109
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        131..222
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   226 AA;  24958 MW;  16153BD25D572240 CRC64;
     MKLLFLCALI ALTAAAPRQK RLTVGTIAVS GGAGGSTGCV VTGNVLYANG FKLRELTPIE
     QQELQDYQNK VADYKATLKQ AVKERQEKLK ARLAGKKGKA VETSSEELPK APKKPSFCSP
     DDTTQFYFDG CMVQNNRVYV GNTYARDLTP SEIEELKVFE KKQTVYQDYI QKQVQQQVSN
     LFGSSDFFSS FFGGGEAKQT TTTEAPELPE EAPEQPNVPN FCTPIY