ID   CARP5_RHINI             Reviewed;         392 AA.
AC   P43232;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   02-SEP-2026, entry version 93.
DE   RecName: Full=Rhizopuspepsin-5;
DE            EC=3.4.23.21;
DE   AltName: Full=Aspartate protease;
DE   Flags: Precursor;
OS   Rhizopus niveus.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=4844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NBRC 4810 / AS 3.4817;
RA   Horiuchi H., Nakamura H., Okazaki T., Yano K., Takagi M.;
RL   Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins with broad specificity similar to that
CC         of pepsin A, preferring hydrophobic residues at P1 and P1'. Clots
CC         milk and activates trypsinogen. Does not cleave 4-Gln-|-His-5, but
CC         does cleave 10-His-|-Leu-11 and 12-Val-|-Glu-13 in B chain of
CC         insulin.; EC=3.4.23.21;
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   EMBL; X56993; CAA40310.1; -; Genomic_DNA.
DR   AlphaFoldDB; P43232; -.
DR   SMR; P43232; -.
DR   MEROPS; A01.012; -.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   FunFam; 2.40.70.10:FF:000115; Lysosomal aspartic protease; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966:SF1; ASPARTYL PROTEINASE; 1.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 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; Signal; Zymogen.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..69
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000025891"
FT   CHAIN           70..392
FT                   /note="Rhizopuspepsin-5"
FT                   /id="PRO_0000025892"
FT   DOMAIN          85..389
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        103
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        286
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   DISULFID        116..119
FT                   /evidence="ECO:0000250"
FT   DISULFID        320..353
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   392 AA;  41850 MW;  015579AA94B99EAE CRC64;
     MKFSLISSCV ALAVLVLSTE AAPNGKKVNI PLTKNKDYKP NAKNAIQKVL AKYHRHRSTS
     SSSNSTSTDG IGRVPVTDYY NDIEYFGQVK VGTPGVTLKL DFDTGSSDLW FASSLCTNCG
     YSQTKYNPNQ SRTYAKDGRA WSISYGDGSS ASGILGTDTV VLGGLTIQRQ TIELARREAS
     SFQNGPSDGL LGLGFNSITT VRGVKTPVDN LISQGLISNP VFGVYLGKES NGGGGEYIFG
     GYDSSKFKGS LTTIPVDNSN GWYGVTIRGA SIGRSRVAGS FEAILDTGTS LLVLPNDVAR
     SVASAYGARD NYDGTFSISC DTSRFQPLVF TIGSSTFEVP ADSLVYEQNG YSCIAGFGYG
     DYDFAIFDDV FLKNNYVVFN PTVPQVQIAT VA
//