ID   CARP3_RHINI             Reviewed;         391 AA.
AC   Q03699;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Rhizopuspepsin-3;
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 (DEC-1990) 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; X56965; CAA40285.1; -; Genomic_DNA.
DR   PIR; JU0343; JU0343.
DR   AlphaFoldDB; Q03699; -.
DR   SMR; Q03699; -.
DR   MEROPS; A01.012; -.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.70.10; -; 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; 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; Signal; Zymogen.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..68
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000025887"
FT   CHAIN           69..391
FT                   /note="Rhizopuspepsin-3"
FT                   /id="PRO_0000025888"
FT   DOMAIN          84..388
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        102
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        285
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   DISULFID        115..118
FT                   /evidence="ECO:0000250"
FT   DISULFID        319..352
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   391 AA;  41533 MW;  00814F973ED21E58 CRC64;
     MKFTLISSCV TLALMTLSIE AAPSGKKVNI PLTKNKDYKP NAKNAIQKAI AKYHRHRSVS
     SSNSTSTDGI GYVPVTDYYN DIEYYGEVTV GTPGVTLKLD FDTGSSDLWF ASSLCTNCGS
     SQTKYNPNES STYARDGRTW SISYGDGSSA SGILGTDTVI LGGLTIRHQT IELARREASQ
     FQSGPSDGLL GLGFDSITTV RGVKTPVDNL ISQGLISNPV FGVYLGKESN GGGGEYIFGG
     YDSSKFKGSL TTIPVDNSNG WYGITVRGTS IGGSRVSSSF DAILDTGTSL LVLPNDVASS
     VAEAYGASDN YDGTFSISCD TSSFEPLVFT IGSSTFEVPA DSLVYEQDGY SCIAGFGYGD
     YDFAIFGDVF LKNNYVVFNP EVPHVQIAPI A