ORYZ_ASPFU
ID ORYZ_ASPFU Reviewed; 403 AA.
AC P28296; Q4WQ71;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Alkaline protease 1;
DE Short=ALP;
DE EC=3.4.21.63;
DE AltName: Full=Aspergillopeptidase B;
DE AltName: Full=Aspergillus proteinase B;
DE AltName: Full=Elastase;
DE AltName: Full=Elastinolytic serine proteinase;
DE AltName: Full=Oryzin;
DE AltName: Allergen=Asp f 13;
DE Flags: Precursor;
GN Name=alp1; Synonyms=alk1, alp; ORFNames=AFUA_4G11800;
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 [GENOMIC DNA].
RX PubMed=1601287; DOI=10.1016/0378-1097(92)90506-j;
RA Jaton-Ogay K., Suter M., Crameri R., Falchetto R., Fatih A., Monod M.;
RT "Nucleotide sequence of a genomic and a cDNA clone encoding an
RT extracellular alkaline protease of Aspergillus fumigatus.";
RL FEMS Microbiol. Lett. 71:163-168(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 126-158, FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=8500876; DOI=10.1128/iai.61.6.2357-2368.1993;
RA Kolattukudy P.E., Lee J.D., Rogers L.M., Zimmerman P., Ceselski S., Fox B.,
RA Stein B., Copelan E.A.;
RT "Evidence for possible involvement of an elastolytic serine protease in
RT aspergillosis.";
RL Infect. Immun. 61:2357-2368(1993).
RN [3]
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 [4]
RP PROTEIN SEQUENCE OF 102-112, IDENTIFICATION BY MASS SPECTROMETRY,
RP SUBCELLULAR LOCATION, AND IGE-BINDING.
RX PubMed=10677362; DOI=10.1042/bj3460423;
RA Chow L.P., Liu S.L., Yu C.J., Liao H.K., Tsai J.J., Tang T.K.;
RT "Identification and expression of an allergen Asp f 13 from Aspergillus
RT fumigatus and epitope mapping using human IgE antibodies and rabbit
RT polyclonal antibodies.";
RL Biochem. J. 346:423-431(2000).
RN [5]
RP INDUCTION.
RX PubMed=19564390; DOI=10.1128/iai.00425-09;
RA Bergmann A., Hartmann T., Cairns T., Bignell E.M., Krappmann S.;
RT "A regulator of Aspergillus fumigatus extracellular proteolytic activity is
RT dispensable for virulence.";
RL Infect. Immun. 77:4041-4050(2009).
RN [6]
RP INDUCTION.
RX PubMed=19564385; DOI=10.1128/iai.00426-09;
RA Sharon H., Hagag S., Osherov N.;
RT "Transcription factor PrtT controls expression of multiple secreted
RT proteases in the human pathogenic mold Aspergillus fumigatus.";
RL Infect. Immun. 77:4051-4060(2009).
RN [7]
RP SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
RX PubMed=20498262; DOI=10.1128/iai.01353-09;
RA Behnsen J., Lessing F., Schindler S., Wartenberg D., Jacobsen I.D.,
RA Thoen M., Zipfel P.F., Brakhage A.A.;
RT "Secreted Aspergillus fumigatus protease Alp1 degrades human complement
RT proteins C3, C4, and C5.";
RL Infect. Immun. 78:3585-3594(2010).
RN [8]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=20303595; DOI=10.1016/j.molimm.2010.02.010;
RA Rambach G., Dum D., Mohsenipour I., Hagleitner M., Wurzner R.,
RA Lass-Florl C., Speth C.;
RT "Secretion of a fungal protease represents a complement evasion mechanism
RT in cerebral aspergillosis.";
RL Mol. Immunol. 47:1438-1449(2010).
CC -!- FUNCTION: Secreted alkaline protease that allows assimilation of
CC proteinaceous substrates. Acts as a significant virulence factor in
CC invasive aspergillosis. Involved in immune evasion from the human and
CC mice complement systems during infection. Efficiently cleaves important
CC components of the complement cascade such as such as C3, C4, C5, and
CC C1q, as well as IgG, which leads to down-regulation of complement
CC activation at the hyphal surface. {ECO:0000269|PubMed:20303595,
CC ECO:0000269|PubMed:20498262, ECO:0000269|PubMed:8500876}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity, and of Bz-Arg-
CC OEt > Ac-Tyr-OEt. Does not hydrolyze peptide amides.; EC=3.4.21.63;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7-8. {ECO:0000269|PubMed:8500876};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10677362,
CC ECO:0000269|PubMed:20303595, ECO:0000269|PubMed:20498262,
CC ECO:0000269|PubMed:8500876}.
CC -!- INDUCTION: Expression is controlled by the prtT transcription factor.
CC {ECO:0000269|PubMed:19564385, ECO:0000269|PubMed:19564390}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE via three
CC immunodominant epitopes localized at the C-terminal part.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; Z11580; CAA77666.1; -; Genomic_DNA.
DR EMBL; M99420; AAB07672.1; -; Genomic_DNA.
DR EMBL; AAHF01000005; EAL89613.1; -; Genomic_DNA.
DR PIR; S22184; S22184.
DR RefSeq; XP_751651.1; XM_746558.1.
DR AlphaFoldDB; P28296; -.
DR SMR; P28296; -.
DR STRING; 746128.CADAFUBP00006700; -.
DR Allergome; 3111; Asp f 13.0101.
DR Allergome; 66; Asp f 13.
DR MEROPS; S08.053; -.
DR EnsemblFungi; EAL89613; EAL89613; AFUA_4G11800.
DR GeneID; 3509271; -.
DR KEGG; afm:AFUA_4G11800; -.
DR VEuPathDB; FungiDB:Afu4g11800; -.
DR eggNOG; KOG1153; Eukaryota.
DR HOGENOM; CLU_011263_1_4_1; -.
DR InParanoid; P28296; -.
DR OMA; NWAIASY; -.
DR OrthoDB; 921536at2759; -.
DR Proteomes; UP000002530; Chromosome 4.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0070051; F:fibrinogen binding; IDA:AspGD.
DR GO; GO:0019863; F:IgE binding; IDA:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008236; F:serine-type peptidase activity; IDA:UniProtKB.
DR GO; GO:0006956; P:complement activation; IMP:AspGD.
DR GO; GO:0060309; P:elastin catabolic process; IDA:AspGD.
DR GO; GO:0042784; P:evasion of host immune response via regulation of host complement system; IDA:UniProtKB.
DR GO; GO:0030163; P:protein catabolic process; IMP:AspGD.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 3.30.70.80; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW Allergen; Direct protein sequencing; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Virulence; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT PROPEP 22..101
FT /evidence="ECO:0000269|PubMed:10677362"
FT /id="PRO_0000027082"
FT CHAIN 102..403
FT /note="Alkaline protease 1"
FT /id="PRO_0000027083"
FT DOMAIN 36..120
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 130..403
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 162
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 193
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 349
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 106..107
FT /note="SA -> RG (in Ref. 1; CAA77666)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="A -> R (in Ref. 2; AAB07672)"
FT /evidence="ECO:0000305"
SQ 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
