ID   ORYZ_ASPFL              Reviewed;         403 AA.
AC   P35211;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   02-SEP-2026, entry version 119.
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   Flags: Precursor;
GN   Name=alp1; Synonyms=alk1, alp;
OS   Aspergillus flavus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; Circumdati.
OX   NCBI_TaxID=5059;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=8262652; DOI=10.1128/iai.62.1.79-85.1994;
RA   Ramesh M.V., Sirakova T., Kolattukudy P.E.;
RT   "Isolation, characterization, and cloning of cDNA and the gene for an
RT   elastinolytic serine proteinase from Aspergillus flavus.";
RL   Infect. Immun. 62:79-85(1994).
CC   -!- FUNCTION: Secreted alkaline protease that allows assimilation of
CC       proteinaceous substrates. {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR   EMBL; L08473; AAA32691.1; -; Genomic_DNA.
DR   EMBL; S67840; AAB29384.1; -; Genomic_DNA.
DR   AlphaFoldDB; P35211; -.
DR   SMR; P35211; -.
DR   MEROPS; S08.053; -.
DR   GlyCosmos; P35211; 2 sites, No reported glycans.
DR   EnsemblFungi; AFLA_000633_t1; KAF7618990.1; AFLA_000633.
DR   VEuPathDB; FungiDB:AFLA_000633; -.
DR   VEuPathDB; FungiDB:F9C07_2278087; -.
DR   BRENDA; 3.4.21.63; 506.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR   FunFam; 3.30.70.80:FF:000008; Alkaline protease 1; 1.
DR   FunFam; 3.40.50.200:FF:000014; Proteinase K; 1.
DR   Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR050131; Peptidase_S8_subtilisin-like.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   PANTHER; PTHR43806:SF58; ALKALINE PROTEASE 1-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Hydrolase; Protease; Secreted;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..121
FT                   /id="PRO_0000027080"
FT   CHAIN           122..403
FT                   /note="Alkaline protease 1"
FT                   /id="PRO_0000027081"
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        309
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   403 AA;  42769 MW;  D9E86FFBA26107C6 CRC64;
     MQSIKRTLLL LGAVLPAVLA GPIFPHRRAP TTIPGKYIVT FKSDVDQAAI DKHTAWATDI
     HKRNLQRRDS SEEDLPIGIE RNFKINKFAA YSGSFDEDTI AQIRQSDEVA AVEEDQVWHL
     FDLTTQSDAP WGLGSISHKG QPSTDYIYDT NGGEGTYAYV VDIGINVDHE EFEGRASLAY
     HAAGGQHVDG VGHGTHVSGT IGGKTYGVAK KANLLSVKVF VGESSSTSII LDGFNWAAND
     IVSKKRTGKA AINMSLGGGY SKAFNDAVEN AFNEGVLSIV AAGNENTDAS RTSPASAPDA
     FTVAAINVNN TRAYFSNYGS VVDIFAPGQN ILSAWIGSNT ATNTISGTSM ATPHIVGLSI
     YLMSLEVLSS PKAVSDRIKE LATRGVVSNV AGSPNLLAYN GNA
//