ID   CHYM_CALJA              Reviewed;         381 AA.
AC   Q9N2D2;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-MAY-2023, entry version 115.
DE   RecName: Full=Chymosin;
DE            EC=3.4.23.4;
DE   AltName: Full=Preprorennin;
DE   Flags: Precursor;
GN   Name=CYM;
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-26, FUNCTION, AND
RP   ACTIVITY REGULATION.
RC   TISSUE=Gastric mucosa;
RX   PubMed=10788784; DOI=10.1093/oxfordjournals.jbchem.a022668;
RA   Kageyama T.;
RT   "New World monkey pepsinogens A and C, and prochymosins. Purification,
RT   characterization of enzymatic properties, cDNA cloning, and molecular
RT   evolution.";
RL   J. Biochem. 127:761-770(2000).
CC   -!- FUNCTION: Hydrolyzes a variety of proteins.
CC       {ECO:0000269|PubMed:10788784}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Broad specificity similar to that of pepsin A. Clots milk by
CC         cleavage of a single 104-Ser-Phe-|-Met-Ala-107 bond in kappa-chain of
CC         casein.; EC=3.4.23.4;
CC   -!- ACTIVITY REGULATION: Inhibited by pepstatin.
CC       {ECO:0000269|PubMed:10788784}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is about 2.5.;
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in adult, not neonate-specific as in
CC       other organisms.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB038386; BAA90873.1; -; mRNA.
DR   PIR; JC7247; JC7247.
DR   RefSeq; XP_002751243.1; XM_002751197.2.
DR   AlphaFoldDB; Q9N2D2; -.
DR   SMR; Q9N2D2; -.
DR   STRING; 9483.ENSCJAP00000006271; -.
DR   MEROPS; A01.006; -.
DR   GeneID; 100411198; -.
DR   KEGG; cjc:100411198; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_3_0_1; -.
DR   InParanoid; Q9N2D2; -.
DR   OrthoDB; 1120702at2759; -.
DR   TreeFam; TF314990; -.
DR   Proteomes; UP000008225; Unplaced.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05478; pepsin_A; 1.
DR   Gene3D; 6.10.140.60; -; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR012848; Aspartic_peptidase_N.
DR   InterPro; IPR034162; Pepsin_A.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF13; CHYMOSIN; 1.
DR   Pfam; PF07966; A1_Propeptide; 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   1: Evidence at protein level;
KW   Aspartyl protease; Digestion; Direct protein sequencing; Disulfide bond;
KW   Hydrolase; Protease; Reference proteome; Repeat; Signal; Zymogen.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000269|PubMed:10788784"
FT   PROPEP          17..58
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000025990"
FT   CHAIN           59..381
FT                   /note="Chymosin"
FT                   /id="PRO_0000025991"
FT   DOMAIN          74..378
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   REPEAT          92..102
FT                   /note="1"
FT   REPEAT          274..284
FT                   /note="2"
FT   ACT_SITE        92
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   ACT_SITE        274
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   DISULFID        105..110
FT                   /evidence="ECO:0000250"
FT   DISULFID        265..269
FT                   /evidence="ECO:0000250"
FT   DISULFID        308..341
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   381 AA;  41896 MW;  C5820C74C97BB96B CRC64;
     MRGFVVLLAV FALSQASGIV RIPLHKGKSL RRALKERGLL EDFLKNHQHA VSRKHSNSRE
     VASEFLTNYL DCQYFGKIYI GTPPQEFTVV FDTGSSDLWV PSVYCNSVAC QNHHRFDPSK
     SSTFQNMDKS LSIQYGTGSM QGLLGYDTVT VSSIVDPHQT VGLSTQEPGD VFTYSEFDGI
     LGLAYPSLAS EYSVPVFDNM MDRHLVAQDL FSVYMSRNEQ GSMLTLGAID PSYYTGSLHW
     IPVTVQEYWQ FTVDSVTVDG VVVACDGGCQ AILDTGTSML VGPGSDIFNI QQAIGATEGQ
     YGEFDIDCGT LSSMPTVVFE INGKKYPLPP SAYTNQDQGF CTSGFQGDDS SQQWILGDVF
     IREYYSVFDR ASNLVGLAKA I
//