ID   CARP4_RHINI             Reviewed;         398 AA.
AC   Q03700;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Rhizopuspepsin-4;
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; X56992; CAA40309.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q03700; -.
DR   SMR; Q03700; -.
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   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; Signal; Zymogen.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..74
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000025889"
FT   CHAIN           75..398
FT                   /note="Rhizopuspepsin-4"
FT                   /id="PRO_0000025890"
FT   DOMAIN          90..394
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   REGION          58..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..82
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        108
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        291
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   DISULFID        121..124
FT                   /evidence="ECO:0000250"
FT   DISULFID        325..358
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   398 AA;  41409 MW;  70CA63FEFB5C05D5 CRC64;
     MKFTLISSCV ALACMALAVE AAPSGKKINV PLSKNANYKP NAKRAIEKAN AKYARFRSSS
     SSSSSSSCGS AGTESSGSVP VTDDGNDIEY YGEVTVGTPG IKLKLDFDTG SSDLWFASTL
     CTNCGSSQTK YDPSQSSTYA KDGRTWSISY GDGSSASGIL GKDTVNLGGL KIKNQIIELA
     KREASSFSSG PSDGLLGLGF DSITTVSGVQ TPMDNLISQG LISNPVFGVY LGKESNGGGG
     EYIFGGYDSS KFSGDLTTIA VDNSNGWYGI TIDGASISGS QVSDSFSAIL DTGTTLLILP
     SNVASSVAQA YNANDNGDGT YNINCDTSEL QPLVFTIGGS TFEVPTDSLI FEQDGNTCVA
     GFGYGQDDFA IFGDVFLKNN YVVFNPQVPQ VQIAPISN