PEPA_ASPOZ
ID PEPA_ASPOZ Reviewed; 390 AA.
AC P0CU33;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Aspergillopepsin-1 {ECO:0000305};
DE EC=3.4.23.18 {ECO:0000250|UniProtKB:Q12567};
DE AltName: Full=Aspartic protease 2 {ECO:0000303|PubMed:8540376};
DE Short=AOAP {ECO:0000303|PubMed:12595261};
DE AltName: Full=Aspergillopepsin I;
DE AltName: Full=Aspergillopeptidase A;
DE Flags: Precursor;
GN Name=pepA;
OS Aspergillus oryzae (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5062;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF N-TERMINUS,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=M-9;
RX PubMed=8540376; DOI=10.1007/978-1-4615-1871-6_77;
RA Takeuchi M., Ogura K., Hamamoto T., Kobayashi Y.;
RT "Molecular cloning and sequence analysis of a gene encoding an aspartic
RT proteinase from Aspergillus oryzae.";
RL Adv. Exp. Med. Biol. 362:577-580(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 68-390 IN COMPLEX WITH INHIBITOR,
RP AND GLYCOSYLATION AT THR-70.
RC STRAIN=M-9;
RX PubMed=12595261; DOI=10.1016/s0022-2836(03)00078-0;
RA Kamitori S., Ohtaki A., Ino H., Takeuchi M.;
RT "Crystal structures of Aspergillus oryzae aspartic proteinase and its
RT complex with an inhibitor pepstatin at 1.9A resolution.";
RL J. Mol. Biol. 326:1503-1511(2003).
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 -!- ACTIVITY REGULATION: Inhibited by the microbial peptide pepstatin.
CC {ECO:0000305|PubMed:12595261}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8540376}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01103}.
CC -!- CAUTION: The enzyme was purified from Aspergillus oryzae var. globosus
CC M-9. The sequence does however not resemble any currently known
CC A.oryzae aspartic protease and is most similar to an Aspergillus
CC pseudoglaucus (E.repens) enzyme. {ECO:0000305}.
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DR PDB; 1IZD; X-ray; 1.90 A; A=68-390.
DR PDB; 1IZE; X-ray; 1.90 A; A=68-390.
DR PDBsum; 1IZD; -.
DR PDBsum; 1IZE; -.
DR AlphaFoldDB; P0CU33; -.
DR SMR; P0CU33; -.
DR iPTMnet; P0CU33; -.
DR VEuPathDB; FungiDB:AO090120000474; -.
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 3D-structure; Aspartyl protease; Direct protein sequencing; Glycoprotein;
KW Hydrolase; Protease; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..67
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:8540376"
FT /id="PRO_0000438798"
FT CHAIN 68..390
FT /note="Aspergillopepsin-1"
FT /id="PRO_0000438799"
FT DOMAIN 84..387
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103,
FT ECO:0000305|PubMed:12595261"
FT ACT_SITE 281
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103,
FT ECO:0000305|PubMed:12595261"
FT CARBOHYD 70
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:12595261"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:1IZD"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:1IZD"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:1IZD"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:1IZD"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1IZD"
FT HELIX 115..118
FT /evidence="ECO:0007829|PDB:1IZD"
FT STRAND 131..141
FT /evidence="ECO:0007829|PDB:1IZD"
FT STRAND 147..159
FT /evidence="ECO:0007829|PDB:1IZD"
FT STRAND 162..175
FT /evidence="ECO:0007829|PDB:1IZD"
FT HELIX 177..181
FT /evidence="ECO:0007829|PDB:1IZD"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:1IZD"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:1IZD"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:1IZD"
FT HELIX 207..211
FT /evidence="ECO:0007829|PDB:1IZD"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:1IZD"
FT STRAND 215..223
FT /evidence="ECO:0007829|PDB:1IZD"
FT STRAND 230..236
FT /evidence="ECO:0007829|PDB:1IZD"
FT STRAND 241..250
FT /evidence="ECO:0007829|PDB:1IZD"
FT STRAND 259..267
FT /evidence="ECO:0007829|PDB:1IZD"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:1IZD"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:1IZD"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:1IZD"
FT HELIX 291..298
FT /evidence="ECO:0007829|PDB:1IZD"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:1IZD"
FT TURN 308..311
FT /evidence="ECO:0007829|PDB:1IZD"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:1IZD"
FT STRAND 324..328
FT /evidence="ECO:0007829|PDB:1IZD"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:1IZD"
FT HELIX 337..340
FT /evidence="ECO:0007829|PDB:1IZD"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:1IZD"
FT STRAND 349..356
FT /evidence="ECO:0007829|PDB:1IZD"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:1IZD"
FT STRAND 361..365
FT /evidence="ECO:0007829|PDB:1IZD"
FT HELIX 367..370
FT /evidence="ECO:0007829|PDB:1IZD"
FT STRAND 373..378
FT /evidence="ECO:0007829|PDB:1IZD"
FT TURN 379..382
FT /evidence="ECO:0007829|PDB:1IZD"
FT STRAND 383..389
FT /evidence="ECO:0007829|PDB:1IZD"
SQ SEQUENCE 390 AA; 40551 MW; B5E574771932F1CD CRC64;
MVNTSLLAAL TAYAVAVSAA PTAPQVKGFS VNQVAVPKGV YRHPAAQLAK AYGKYHATVP
TQVAAAAAAT GSVTTNPTSN DEEYITQVTV GDDTLGLDFD TGSADLWVFS SQTPSSERSG
HDYYTPGSSA QKIDGATWSI SYGDGSSASG DVYKDKVTVG GVSYDSQAVE SAEKVSSEFT
QDTANDGLLG LAFSSINTVQ PTPQKTFFDN VKSSLSEPIF AVALKHNAPG VYDFGYTDSS
KYTGSITYTD VDNSQGFWGF TADGYSIGSD SSSDSITGIA DTGTTLLLLD DSIVDAYYEQ
VNGASYDSSQ GGYVFPSSAS LPDFSVTIGD YTATVPGEYI SFADVGNGQT FGGIQSNSGI
GFSIFGDVFL KSQYVVFDAS GPRLGFAAQA
