CHYM_CALJA
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-AUG-2022, entry version 112.
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}.
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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 OMA; CNSDACQ; -.
DR OrthoDB; 1619495at2759; -.
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; 2.40.70.10; -; 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; PTHR47966; 1.
DR Pfam; PF07966; A1_Propeptide; 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 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