ID   IELA_ASPFU              Reviewed;          87 AA.
AC   Q4WZ11;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 2.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Elastase inhibitor AFUEI;
DE   Flags: Precursor;
GN   ORFNames=AFUA_3G14940;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 20-87, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP   SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   STRAIN=AFU-12;
RX   PubMed=18566136; DOI=10.1099/jmm.0.47789-0;
RA   Okumura Y., Matsui T., Ogawa K., Uchiya K., Nikai T.;
RT   "Biochemical properties and primary structure of elastase inhibitor AFUEI
RT   from Aspergillus fumigatus.";
RL   J. Med. Microbiol. 57:803-808(2008).
CC   -!- FUNCTION: Elastase inhibitor. Non-competitive inhibitor of A.fumigatus
CC       elastase with a Ki of 1.6 nM. Inhibits the fibrinogenase and
CC       collagenase activities of A.fumigatus elastase. Inhibitor of A.flavus
CC       elastase and human leukocyte elastase, and weakly inhibits porcine
CC       pancreatic elastase. Does not inhibit elastase from P.aeruginosa or
CC       C.atrox venom. {ECO:0000269|PubMed:18566136}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Stable to heat treatment. Retains 33% of activity when heated to 100
CC         degrees Celsius for 10 minutes at pH 7.5.
CC         {ECO:0000269|PubMed:18566136};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18566136}.
CC   -!- MASS SPECTROMETRY: Mass=7525.1; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:18566136};
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DR   EMBL; AAHF01000002; EAL92092.2; -; Genomic_DNA.
DR   RefSeq; XP_754130.2; XM_749037.2.
DR   PDB; 3W0D; X-ray; 2.30 A; A/B=20-87.
DR   PDB; 3W0E; X-ray; 1.80 A; A/B=20-87.
DR   PDBsum; 3W0D; -.
DR   PDBsum; 3W0E; -.
DR   AlphaFoldDB; Q4WZ11; -.
DR   SMR; Q4WZ11; -.
DR   MEROPS; I78.001; -.
DR   EnsemblFungi; EAL92092; EAL92092; AFUA_3G14940.
DR   GeneID; 3511769; -.
DR   KEGG; afm:AFUA_3G14940; -.
DR   VEuPathDB; FungiDB:Afu3g14940; -.
DR   eggNOG; ENOG502RPIM; Eukaryota.
DR   HOGENOM; CLU_2483894_0_0_1; -.
DR   OMA; MITMEYI; -.
DR   OrthoDB; 1599451at2759; -.
DR   Proteomes; UP000002530; Chromosome 3.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0004857; F:enzyme inhibitor activity; IDA:AspGD.
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   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Protease inhibitor; Reference proteome; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:18566136"
FT   CHAIN           20..87
FT                   /note="Elastase inhibitor AFUEI"
FT                   /id="PRO_0000352770"
FT   DISULFID        24..86
FT                   /evidence="ECO:0000250"
FT   HELIX           21..34
FT                   /evidence="ECO:0007829|PDB:3W0E"
FT   TURN            35..37
FT                   /evidence="ECO:0007829|PDB:3W0E"
FT   HELIX           42..47
FT                   /evidence="ECO:0007829|PDB:3W0E"
FT   STRAND          51..56
FT                   /evidence="ECO:0007829|PDB:3W0E"
FT   STRAND          61..63
FT                   /evidence="ECO:0007829|PDB:3W0E"
FT   STRAND          71..75
FT                   /evidence="ECO:0007829|PDB:3W0E"
FT   STRAND          79..86
FT                   /evidence="ECO:0007829|PDB:3W0E"
SQ   SEQUENCE   87 AA;  9413 MW;  64E569B7278F9C94 CRC64;
     MKFSLACLLA LAGLQAALAD PATCEKEAQF VKQELIGQPY TDAVANALQS NPIRVLHPGD
     MITMEYIASR LNIQVNENNE IISAHCA