PEPA_ASPNC
ID PEPA_ASPNC Reviewed; 394 AA.
AC A2R3L3;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 80.
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 Flags: Precursor;
GN Name=pepA; ORFNames=An14g04710;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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 -!- SUBUNIT: Monomer. {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; AM270324; CAK42031.1; -; Genomic_DNA.
DR RefSeq; XP_001401093.1; XM_001401056.2.
DR AlphaFoldDB; A2R3L3; -.
DR SMR; A2R3L3; -.
DR MEROPS; A01.016; -.
DR PaxDb; A2R3L3; -.
DR EnsemblFungi; CAK42031; CAK42031; An14g04710.
DR GeneID; 4987328; -.
DR KEGG; ang:ANI_1_654124; -.
DR VEuPathDB; FungiDB:An14g04710; -.
DR HOGENOM; CLU_013253_0_1_1; -.
DR BRENDA; 3.4.23.18; 518.
DR Proteomes; UP000006706; Chromosome 1R.
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; IDA:AspGD.
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 3: Inferred from homology;
KW Aspartyl protease; Disulfide bond; Hydrolase; Protease; Reference proteome;
KW Secreted; Signal; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..69
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q12567"
FT /id="PRO_0000407045"
FT CHAIN 70..394
FT /note="Aspergillopepsin-1"
FT /id="PRO_5000220965"
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; 41276 MW; 68874D5424F9128F 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
EQVSGAQESE EAGGYVFSCS TNPPDFTVVI GDYKAVVPGK YINYAPISTG SSTCFGGIQS
NSGLGLSILG DVFLKSQYVV FNSEGPKLGF AAQA
