PEPA_ASPNG
ID PEPA_ASPNG Reviewed; 394 AA.
AC P55325; Q00207; Q12371;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Aspergillopepsin-1 {ECO:0000305};
DE EC=3.4.23.18 {ECO:0000250|UniProtKB:Q12567};
DE AltName: Full=Aspartic protease pepA;
DE AltName: Full=Aspergillopepsin I;
DE AltName: Full=Aspergillopeptidase A;
DE AltName: Full=Proctase B {ECO:0000303|PubMed:7787314};
DE Flags: Precursor;
GN Name=pepA {ECO:0000303|Ref.1}; Synonyms=prtB {ECO:0000303|PubMed:7787314};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=WU-2223L;
RA Shirai H.;
RT "Nucleotide sequence of the pepA gene from Aspergillus niger.";
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 70-87; 94-117; 227-242
RP AND 377-381.
RX PubMed=7787314; DOI=10.1271/bbb.59.954;
RA Lu J.F., Inoue H., Kimura T., Makabe O., Takahashi K.;
RT "Molecular cloning of a cDNA for proctase B from Aspergillus niger var.
RT macrosporus and sequence comparison with other aspergillopepsins I.";
RL Biosci. Biotechnol. Biochem. 59:954-955(1995).
CC -!- FUNCTION: Secreted aspartic endopeptidase that allows assimilation of
CC proteinaceous substrates. The scissile peptide bond is attacked by a
CC nucleophilic water molecule activated by two aspartic residues in the
CC active site. Shows a broad primary substrate specificity. Favors
CC hydrophobic residues at the P1 and P1' positions, but also accepts a
CC lysine residue in the P1 position, leading to the activation of
CC trypsinogen and chymotrypsinogen A. {ECO:0000250|UniProtKB:Q12567}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity. Generally
CC favors hydrophobic residues in P1 and P1', but also accepts Lys in
CC P1, which leads to activation of trypsinogen. Does not clot milk.;
CC EC=3.4.23.18; Evidence={ECO:0000250|UniProtKB:Q12567};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q12567}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01103}.
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DR EMBL; D49839; BAA08640.1; -; Genomic_DNA.
DR EMBL; D49838; BAA08639.1; -; mRNA.
DR EMBL; D45177; BAA08123.1; -; mRNA.
DR AlphaFoldDB; P55325; -.
DR SMR; P55325; -.
DR STRING; 5061.CADANGAP00011185; -.
DR MEROPS; A01.016; -.
DR VEuPathDB; FungiDB:An14g04710; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1141688; -.
DR VEuPathDB; FungiDB:ATCC64974_3930; -.
DR VEuPathDB; FungiDB:M747DRAFT_2667; -.
DR eggNOG; KOG1339; Eukaryota.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06097; Aspergillopepsin_like; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; PTHR47966; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Protease; Secreted; Signal; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..69
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:7787314"
FT /id="PRO_0000025920"
FT CHAIN 70..394
FT /note="Aspergillopepsin-1"
FT /id="PRO_0000025921"
FT DOMAIN 85..391
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 101
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 283
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT DISULFID 319..354
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT CONFLICT 16
FT /note="T -> S (in Ref. 2; BAA08123)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="V -> I (in Ref. 2; BAA08123)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="L -> M (in Ref. 2; BAA08123)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="G -> V (in Ref. 2; BAA08123)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="S -> T (in Ref. 2; BAA08123)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="H -> Y (in Ref. 2; BAA08123)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="Y -> E (in Ref. 2; BAA08123)"
FT /evidence="ECO:0000305"
FT CONFLICT 322..323
FT /note="DL -> NP (in Ref. 2; BAA08123)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="K -> R (in Ref. 2; BAA08123)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="V -> I (in Ref. 2; BAA08123)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="Y -> F (in Ref. 2; BAA08123)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 394 AA; 41230 MW; 1A2877C31915F154 CRC64;
MVVFSKTAAL VLGLSTAVSA APAPTRKGFT INQIARPANK TRTVNLPGLY ARSLAKFGGT
VPQSVKEAAS KGSAVTTPQN NDEEYLTPVT VGKSTLHLDF DTGSADLWGF SDELPSSEQT
GHDLYTPSSS ATKLSGYSWD ISYGDGSSAS GDVYRDTVTV GGVTTNKQAV EAASKISSEF
VQDTANDGLL GLAFSSINTV QPKAQTTFFD TVKSQLDSPL FAVQLKHDAP GVYDFGYIDD
SKYTGSITYT DADSSQGYWG FSTDGYSIGD GSSSSSGFSA IADTGTTLIL LDDEIVSAHY
EQVSGAQESY EAGGYVFSCS TDLPDFTVVI GDYKAVVPGK YINYAPVSTG SSTCYGGIQS
NSGLGLSILG DVFLKSQYVV FNSEGPKLGF AAQA
