ID   IELA_ASPFL              Reviewed;          68 AA.
AC   P86036;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 24.
DE   RecName: Full=Elastase inhibitor AFLEI {ECO:0000303|PubMed:16940957, ECO:0000303|PubMed:17287718};
OS   Aspergillus flavus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5059;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, AND DISULFIDE BOND.
RX   PubMed=17287718; DOI=10.3314/jjmm.48.13;
RA   Okumura Y., Ogawa K., Uchiya K.;
RT   "Characterization and primary structure of elastase inhibitor, AFLEI, from
RT   Aspergillus flavus.";
RL   Nippon Ishinkin Gakkai Zasshi 48:13-18(2007).
RN   [2] {ECO:0000305}
RP   MASS SPECTROMETRY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=16940957; DOI=10.3314/jjmm.47.219;
RA   Okumura Y., Ogawa K., Uchiya K., Nikai T.;
RT   "Isolation and characterization of a novel elastase inhibitor, AFLEI from
RT   Aspergillus flavus.";
RL   Nippon Ishinkin Gakkai Zasshi 47:219-224(2006).
CC   -!- FUNCTION: Elastase inhibitor. Inhibitor of A.flavus elastase with a Ki
CC       of 40 nM. Inhibitor of A.fumigatus elastase and human leukocyte
CC       elastase. Inhibits the fibrinogenase and collagenase activities of
CC       A.flavus elastase. Does not inhibit porcine pancreatic elastase,
CC       trypsin, chymotrypsin, thrombin or A.acutus AC1-proteinase.
CC       {ECO:0000269|PubMed:16940957, ECO:0000269|PubMed:17287718}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Stable from pH 6 to 10. {ECO:0000269|PubMed:16940957};
CC       Temperature dependence:
CC         Stable at temperatures below 80 degrees Celsius.
CC         {ECO:0000269|PubMed:16940957};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=7525.8; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:16940957};
CC   -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is: 7.4.
CC       {ECO:0000269|PubMed:16940957}.
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DR   AlphaFoldDB; P86036; -.
DR   SMR; P86036; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB.
DR   InterPro; IPR021719; Prot_inh_I78.
DR   Pfam; PF11720; Inhibitor_I78; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Protease inhibitor; Secreted;
KW   Serine protease inhibitor.
FT   CHAIN           1..68
FT                   /note="Elastase inhibitor AFLEI"
FT                   /id="PRO_0000352771"
FT   DISULFID        5..67
FT                   /evidence="ECO:0000269|PubMed:17287718"
SQ   SEQUENCE   68 AA;  7525 MW;  A45BF75192D5B332 CRC64;
     DPATCEKEAQ FVKQELIGQP YTDAVANALQ SNPIRVLHPG DMITMEYIAS RLNIQVNENN
     EIISAHCA