PEPA_ASPAW
ID PEPA_ASPAW Reviewed; 394 AA.
AC P17946; Q7M512;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 107.
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 A {ECO:0000303|PubMed:2182390};
DE Short=PEPA;
DE AltName: Full=Aspergillopepsin I;
DE AltName: Full=Aspergillopeptidase A;
DE Flags: Precursor;
GN Name=pepA {ECO:0000303|PubMed:2182390};
OS Aspergillus awamori (Black koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=105351;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=UVK143F;
RX PubMed=2182390; DOI=10.1016/0378-1119(90)90274-u;
RA Berka R.M., Ward M., Wilson L.J., Hayenga K.J., Kodama K.H.,
RA Carlomagno L.P., Thompson S.A.;
RT "Molecular cloning and deletion of the gene encoding aspergillopepsin A
RT from Aspergillus awamori.";
RL Gene 86:153-162(1990).
RN [2]
RP ERRATUM OF PUBMED:2182390.
RX PubMed=2269444; DOI=10.1016/0378-1119(90)90261-o;
RA Thompson S.A.;
RL Gene 96:313-313(1990).
RN [3]
RP PRELIMINARY PROTEIN SEQUENCE OF 70-394.
RA Ostoslavskaya V.I., Revina L.P., Kotlova E.K., Surova I.A., Levin E.D.,
RA Timokhina E.A., Stepanov V.M.;
RT "The primary structure of aspergillopepsin A, aspartic proteinase from
RT Aspergillus awamori. IV. Amino acid sequence of the enzyme.";
RL Bioorg. Khim. 12:1030-1047(1986).
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; M34454; AAA78947.1; -; Genomic_DNA.
DR PIR; PN0090; PN0090.
DR PIR; PS0140; PS0140.
DR AlphaFoldDB; P17946; -.
DR SMR; P17946; -.
DR MEROPS; A01.016; -.
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:2182390, ECO:0000269|Ref.3"
FT /id="PRO_0000025918"
FT CHAIN 70..394
FT /note="Aspergillopepsin-1"
FT /id="PRO_0000025919"
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"
SQ SEQUENCE 394 AA; 41177 MW; 88C3590218B27819 CRC64;
MVVFSKTAAL VLGLSSAVSA APAPTRKGFT INQIARPANK TRTINLPGMY ARSLAKFGGT
VPQSVKEAAS KGSAVTTPQN NDEEYLTPVT VGKSTLHLDF DTGSADLWVF SDELPSSEQT
GHDLYTPSSS ATKLSGYTWD ISYGDGSSAS GDVYRDTVTV GGVTTNKQAV EAASKISSEF
VQNTANDGLL GLAFSSINTV QPKAQTTFFD TVKSQLDSPL FAVQLKHDAP GVYDFGYIDD
SKYTGSITYT DADSSQGYWG FSTDGYSIGD GSSSSSGFSA IADTGTTLIL LDDEIVSAYY
EQVSGASGET EAGGYVFSCS TNPPDFTVVI GDYKAVVPGK YINYAPISTG SSTCFGGIQS
NSGLGLSILG DVFLKSQYVV FNSEGPKLGF AAQA