CARP2_RHINI
ID CARP2_RHINI Reviewed; 391 AA.
AC P43231;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Rhizopuspepsin-2;
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; X56964; CAA40284.1; -; Genomic_DNA.
DR AlphaFoldDB; P43231; -.
DR SMR; P43231; -.
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..68
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000025885"
FT CHAIN 69..391
FT /note="Rhizopuspepsin-2"
FT /id="PRO_0000025886"
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; 41234 MW; 3F34230659DEA960 CRC64;
MKLTLISSCV ALAFMALATE AAPSGKKLSI PLTKNTNYKP SAKNAIQKAL AKYHRFRTTS
SSNSTSTEGT GSVPVTDYYN DIEYYGKVTV GTPGVTLKLD FDTGSSDLWF ASTLCTNCGS
SQTKYNPNQS STYAKDGRTW SISYGDGSSA SGILGTDTVT LGGLKITKQT IELAKREATS
FQSGPSYGLL GLGFDTITTV RGVKTPVDNL ISQGLISKPI FGVYLGKESN GGGGEYIFGG
YDSSKYSGSL TTIPVDNSNG WYGITIKGTT IGSSKVSSSF SAILDTGTTL LILPNNVASA
VARSYGASDN GDGTYTIDCD TSSFKPLVFS IGSSTFEVPA DSLVFEQDGS TCYAGFGYGD
YDFAIFGDVF LKNNYVVFNQ EVPEVQIAPI A