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Alkaline protease 1 (ALP) (EC 3.4.21.63) (Aspergillopeptidase B) (Aspergillus proteinase B) (Elastase) (Elastinolytic serine proteinase) (Oryzin) (allergen Asp f 13)

 ORYZ_ASPFU              Reviewed;         403 AA.
P28296; Q4WQ71;
01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 2.
25-OCT-2017, entry version 128.
RecName: Full=Alkaline protease 1;
Short=ALP;
EC=3.4.21.63;
AltName: Full=Aspergillopeptidase B;
AltName: Full=Aspergillus proteinase B;
AltName: Full=Elastase;
AltName: Full=Elastinolytic serine proteinase;
AltName: Full=Oryzin;
AltName: Allergen=Asp f 13;
Flags: Precursor;
Name=alp1; Synonyms=alk1, alp; ORFNames=AFUA_4G11800;
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
A1100) (Aspergillus fumigatus).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
NCBI_TaxID=330879;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1601287; DOI=10.1016/0378-1097(92)90506-J;
Jaton-Ogay K., Suter M., Crameri R., Falchetto R., Fatih A., Monod M.;
"Nucleotide sequence of a genomic and a cDNA clone encoding an
extracellular alkaline protease of Aspergillus fumigatus.";
FEMS Microbiol. Lett. 71:163-168(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 126-158,
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
PubMed=8500876;
Kolattukudy P.E., Lee J.D., Rogers L.M., Zimmerman P., Ceselski S.,
Fox B., Stein B., Copelan E.A.;
"Evidence for possible involvement of an elastolytic serine protease
in aspergillosis.";
Infect. Immun. 61:2357-2368(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
PubMed=16372009; DOI=10.1038/nature04332;
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S.,
Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W.,
Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S.,
Farman M.L., Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R.,
Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A.,
Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J.,
Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J.,
Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S.,
Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A.,
Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M.,
Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I.,
Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
Ronning C.M., Rutter S., Salzberg S.L., Sanchez M.,
Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S.,
Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J.,
White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K.,
Machida M., Hall N., Barrell B.G., Denning D.W.;
"Genomic sequence of the pathogenic and allergenic filamentous fungus
Aspergillus fumigatus.";
Nature 438:1151-1156(2005).
[4]
PROTEIN SEQUENCE OF 102-112, IDENTIFICATION BY MASS SPECTROMETRY,
SUBCELLULAR LOCATION, AND IGE-BINDING.
PubMed=10677362; DOI=10.1042/bj3460423;
Chow L.P., Liu S.L., Yu C.J., Liao H.K., Tsai J.J., Tang T.K.;
"Identification and expression of an allergen Asp f 13 from
Aspergillus fumigatus and epitope mapping using human IgE antibodies
and rabbit polyclonal antibodies.";
Biochem. J. 346:423-431(2000).
[5]
INDUCTION.
PubMed=19564390; DOI=10.1128/IAI.00425-09;
Bergmann A., Hartmann T., Cairns T., Bignell E.M., Krappmann S.;
"A regulator of Aspergillus fumigatus extracellular proteolytic
activity is dispensable for virulence.";
Infect. Immun. 77:4041-4050(2009).
[6]
INDUCTION.
PubMed=19564385; DOI=10.1128/IAI.00426-09;
Sharon H., Hagag S., Osherov N.;
"Transcription factor PrtT controls expression of multiple secreted
proteases in the human pathogenic mold Aspergillus fumigatus.";
Infect. Immun. 77:4051-4060(2009).
[7]
SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
FUNCTION.
PubMed=20498262; DOI=10.1128/IAI.01353-09;
Behnsen J., Lessing F., Schindler S., Wartenberg D., Jacobsen I.D.,
Thoen M., Zipfel P.F., Brakhage A.A.;
"Secreted Aspergillus fumigatus protease Alp1 degrades human
complement proteins C3, C4, and C5.";
Infect. Immun. 78:3585-3594(2010).
[8]
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=20303595; DOI=10.1016/j.molimm.2010.02.010;
Rambach G., Dum D., Mohsenipour I., Hagleitner M., Wurzner R.,
Lass-Florl C., Speth C.;
"Secretion of a fungal protease represents a complement evasion
mechanism in cerebral aspergillosis.";
Mol. Immunol. 47:1438-1449(2010).
-!- FUNCTION: Secreted alkaline protease that allows assimilation of
proteinaceous substrates. Acts as a significant virulence factor
in invasive aspergillosis. Involved in immune evasion from the
human and mice complement systems during infection. Efficiently
cleaves important components of the complement cascade such as
such as C3, C4, C5, and C1q, as well as IgG, which leads to down-
regulation of complement activation at the hyphal surface.
{ECO:0000269|PubMed:20303595, ECO:0000269|PubMed:20498262,
ECO:0000269|PubMed:8500876}.
-!- CATALYTIC ACTIVITY: Hydrolysis of proteins with broad specificity,
and of Bz-Arg-OEt > Ac-Tyr-OEt. Does not hydrolyze peptide amides.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 7-8. {ECO:0000269|PubMed:8500876};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10677362,
ECO:0000269|PubMed:20303595, ECO:0000269|PubMed:20498262,
ECO:0000269|PubMed:8500876}.
-!- INDUCTION: Expression is controlled by the prtT transcription
factor. {ECO:0000269|PubMed:19564385,
ECO:0000269|PubMed:19564390}.
-!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE via
three immunodominant epitopes localized at the C-terminal part.
-!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Z11580; CAA77666.1; -; Genomic_DNA.
EMBL; M99420; AAB07672.1; -; Genomic_DNA.
EMBL; AAHF01000005; EAL89613.1; -; Genomic_DNA.
PIR; S22184; S22184.
RefSeq; XP_751651.1; XM_746558.1.
ProteinModelPortal; P28296; -.
SMR; P28296; -.
STRING; 5085.CADAFUBP00006700; -.
Allergome; 3111; Asp f 13.0101.
Allergome; 66; Asp f 13.
MEROPS; S08.053; -.
PRIDE; P28296; -.
EnsemblFungi; CADAFUAT00008008; CADAFUAP00008008; CADAFUAG00008008.
GeneID; 3509271; -.
KEGG; afm:AFUA_4G11800; -.
EuPathDB; FungiDB:Afu4g11800; -.
HOGENOM; HOG000199176; -.
InParanoid; P28296; -.
KO; K18549; -.
OMA; HVDTLGH; -.
OrthoDB; EOG092C4A4B; -.
Proteomes; UP000002530; Chromosome 4.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0070051; F:fibrinogen binding; IDA:AspGD.
GO; GO:0019863; F:IgE binding; IDA:UniProtKB.
GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0008236; F:serine-type peptidase activity; IDA:UniProtKB.
GO; GO:0042784; P:active evasion of host immune response via regulation of host complement system; IDA:UniProtKB.
GO; GO:0006956; P:complement activation; IMP:AspGD.
GO; GO:0060309; P:elastin catabolic process; IDA:AspGD.
GO; GO:0009405; P:pathogenesis; IDA:UniProtKB.
GO; GO:0030163; P:protein catabolic process; IMP:AspGD.
CDD; cd04077; Peptidases_S8_PCSK9_Proteinase; 1.
Gene3D; 3.30.70.80; -; 1.
Gene3D; 3.40.50.200; -; 1.
InterPro; IPR034193; PCSK9_ProteinaseK-like.
InterPro; IPR009020; Peptidase/Inhibitor_I9.
InterPro; IPR000209; Peptidase_S8/S53_dom.
InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
InterPro; IPR023827; Peptidase_S8_Asp-AS.
InterPro; IPR022398; Peptidase_S8_His-AS.
InterPro; IPR023828; Peptidase_S8_Ser-AS.
InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
InterPro; IPR010259; S8pro/Inhibitor_I9.
InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
Pfam; PF05922; Inhibitor_I9; 1.
Pfam; PF00082; Peptidase_S8; 1.
PRINTS; PR00723; SUBTILISIN.
SUPFAM; SSF52743; SSF52743; 1.
SUPFAM; SSF54897; SSF54897; 1.
PROSITE; PS00136; SUBTILASE_ASP; 1.
PROSITE; PS00137; SUBTILASE_HIS; 1.
PROSITE; PS00138; SUBTILASE_SER; 1.
1: Evidence at protein level;
Allergen; Complete proteome; Direct protein sequencing; Glycoprotein;
Hydrolase; Protease; Reference proteome; Secreted; Serine protease;
Signal; Virulence; Zymogen.
SIGNAL 1 21 {ECO:0000250}.
PROPEP 22 101 {ECO:0000269|PubMed:10677362}.
/FTId=PRO_0000027082.
CHAIN 102 403 Alkaline protease 1.
/FTId=PRO_0000027083.
DOMAIN 159 384 Peptidase S8.
ACT_SITE 162 162 Charge relay system. {ECO:0000250}.
ACT_SITE 193 193 Charge relay system. {ECO:0000250}.
ACT_SITE 349 349 Charge relay system. {ECO:0000250}.
CARBOHYD 253 253 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 307 307 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 367 367 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 106 107 SA -> RG (in Ref. 1; CAA77666).
{ECO:0000305}.
CONFLICT 295 295 A -> R (in Ref. 2; AAB07672).
{ECO:0000305}.
SEQUENCE 403 AA; 42190 MW; 2D900D1AE22CDD4A CRC64;
MLSIKRTLLL LGAVLPAVFG APVQETRRAA QKIPGKYIVT FKPGTDTATI ESHTLWATDL
HKRNLERRDT TSGEPPVGIE KSYKIKDFAA YAGSFDDATI EEIRKSADVA HVEEDQIWYL
DALTTQKGAP WGLGSISHKG QASTDYIYDT SAGAGTYAYV VDSGINVNHV EFESRASLAY
NAAGGSHVDS IGHGTHVAGT IGGKTYGVAK KTNLLSVKVF QGESSSTSII LDGFNWAVND
IVSKGRTKKA AINMSLGGGY SYAFNNAVEN AFDEGVLSVV AAGNENSDAS NTSPASAPNA
LTVAAINKSN ARASFSNYGS VVDIFAPGQD ILSAWIGSTT ATNTISGTSM ATPHIVGLSV
YLMGLENLSG PAAVTARIKE LATNGVVTNV KGSPNKLAYN GNA


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