Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P00794 (CHYM_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chymosin

EC=3.4.23.4
Alternative name(s):
Preprorennin
Gene names
Name:CYM
Synonyms:CPC
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length381 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Chymosin is synthesized in the mucosa of the abomasum (fourth stomach) of young (unweaned) ruminants. The enzyme hydrolyzes casein to paracasein.

Catalytic activity

Broad specificity similar to that of pepsin A. Clots milk by cleavage of a single 104-Ser-Phe-|-Met-Ala-107 bond in kappa-chain of casein.

Subunit structure

Monomer.

Polymorphism

Forms A and B are probably allelic variants. Form B is the predominant form and differs only in one position.

Sequence similarities

Belongs to the peptidase A1 family.

Ontologies

Keywords
   Biological processDigestion
   DomainSignal
   Molecular functionAspartyl protease
Hydrolase
Protease
   PTMDisulfide bond
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processdigestion

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionaspartic-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Ref.2 Ref.7 Ref.8
Propeptide17 – 5842Activation peptide
PRO_0000025988
Chain59 – 381323Chymosin
PRO_0000025989

Sites

Active site921 Ref.7 Ref.10
Active site2741 Ref.7 Ref.10

Amino acid modifications

Disulfide bond105 ↔ 110 Ref.9
Disulfide bond265 ↔ 269 Ref.9
Disulfide bond308 ↔ 341 Ref.9

Natural variations

Natural variant3021G → D in chymosin A. Ref.1 Ref.5

Experimental info

Mutagenesis3081C → D: Propeptide is not cleaved. Ref.14
Mutagenesis3411C → S: Propeptide is not cleaved. Ref.14
Sequence conflict171A → T in AAA30446. Ref.3
Sequence conflict1091A → G in AAA30446. Ref.3
Sequence conflict1551V → L in AAA30447. Ref.1
Sequence conflict1741Y → T AA sequence Ref.7
Sequence conflict2181N → D AA sequence Ref.7
Sequence conflict2181N → D AA sequence Ref.9
Sequence conflict2301D → N in AAA30448. Ref.2
Sequence conflict2321S → C in AAA30447. Ref.1
Sequence conflict2521T → Y AA sequence Ref.9
Sequence conflict3251M → I Ref.5
Sequence conflict3351S → G Ref.5
Sequence conflict3431S → T Ref.5
Sequence conflict3801A → T Ref.5

Secondary structure

.......................................................................... 381
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00794 [UniParc].

Last modified February 1, 2005. Version 3.
Checksum: A4425013B4E2E56A

FASTA38142,180
        10         20         30         40         50         60 
MRCLVVLLAV FALSQGAEIT RIPLYKGKSL RKALKEHGLL EDFLQKQQYG ISSKYSGFGE 

        70         80         90        100        110        120 
VASVPLTNYL DSQYFGKIYL GTPPQEFTVL FDTGSSDFWV PSIYCKSNAC KNHQRFDPRK 

       130        140        150        160        170        180 
SSTFQNLGKP LSIHYGTGSM QGILGYDTVT VSNIVDIQQT VGLSTQEPGD VFTYAEFDGI 

       190        200        210        220        230        240 
LGMAYPSLAS EYSIPVFDNM MNRHLVAQDL FSVYMDRNGQ ESMLTLGAID PSYYTGSLHW 

       250        260        270        280        290        300 
VPVTVQQYWQ FTVDSVTISG VVVACEGGCQ AILDTGTSKL VGPSSDILNI QQAIGATQNQ 

       310        320        330        340        350        360 
YGEFDIDCDN LSYMPTVVFE INGKMYPLTP SAYTSQDQGF CTSGFQSENH SQKWILGDVF 

       370        380 
IREYYSVFDR ANNLVGLAKA I 

« Hide

References

[1]"Molecular cloning and characterization of double-stranded cDNA coding for bovine chymosin."
Moir D., Mao J., Schumm J.W., Vovis G.F., Alford B.L., Taunton-Rigby A.
Gene 19:127-138(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASP-302.
[2]"Molecular cloning and nucleotide sequence of cDNA coding for calf preprochymosin."
Harris T.J.R., Lowe P.A., Lyons A., Thomas P.G., Eaton M.A.W., Millican T.A., Patel T.P., Bose C.C., Carey N.H., Doel M.T.
Nucleic Acids Res. 10:2177-2187(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Cloning and structural analysis of the calf prochymosin gene."
Hidaka M., Sasaki K., Uozumi T., Beppu T.
Gene 43:197-203(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"cDNA encoding bovine calf preprochymosin."
Sun D., Jiang Y.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"Nucleotide sequence of calf prorennin cDNA cloned in Escherichia coli."
Nishimori K., Kawaguchi Y., Hidaka M., Uozumi T., Beppu T.
J. Biochem. 91:1085-1088(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 140-381, VARIANT ASP-302.
[6]"Isolation of human, swine, and rat prepepsinogens and calf preprochymosin, and determination of the primary structures of their NH2-terminal signal sequences."
Ichihara Y., Sogawa K., Takahashi K.
J. Biochem. 98:483-492(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-30.
[7]"The complete amino acid sequence of prochymosin."
Foltmann B., Pedersen V.B., Jacobsen H., Kauffman D., Wybrandt G.
Proc. Natl. Acad. Sci. U.S.A. 74:2321-2324(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 17-381.
[8]"Amino-acid sequence of the peptide segment liberated during activation of prochymosin (prorennin)."
Pedersen V.B., Foltmann B.
Eur. J. Biochem. 55:95-103(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 17-77.
[9]"The primary structure of calf chymosin."
Foltmann B., Pedersen V.B., Kauffman D., Wybrandt G.
J. Biol. Chem. 254:8447-8456(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 59-381, DISULFIDE BONDS.
[10]"The structure and function of acid proteases. III. Isolation and characterization of the active-site peptides from bovine rennin."
Chang W.-J., Takahashi K.
J. Biochem. 76:467-474(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE PEPTIDES.
[11]"X-ray analyses of aspartic proteinases. IV. Structure and refinement at 2.2-A resolution of bovine chymosin."
Newman M., Safro M., Frazao C., Kahn G., Zdanov A., Tickle I.J., Blundell T.L., Andreeva N.
J. Mol. Biol. 221:1295-1309(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[12]"Engineering enzyme subsite specificity: preparation, kinetic characterization, and X-ray analysis at 2.0-A resolution of Val111Phe site-mutated calf chymosin."
Strop P., Sedlacek J., Stys J., Kaderabkova Z., Blaha I., Pavlickova L., Pohl J., Fabry M., Kostka V., Newman M., Frazao C., Shearer A., Tickle I.J., Blundell T.L.
Biochemistry 29:9863-9871(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT.
[13]"The three-dimensional structure of recombinant bovine chymosin at 2.3-A resolution."
Gilliland G.L., Winborne E.L., Nachman J., Wlodawer A.
Proteins 8:82-101(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[14]"Functional implication of disulfide bond, Cys250 -Cys283, in bovine chymosin."
Huang K., Zhang Z., Liu N., Zhang Y., Zhang G., Yang K.
Biochem. Biophys. Res. Commun. 187:692-696(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-308 AND CYS-341.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J00002 mRNA. Translation: AAA30447.1.
J00003 mRNA. Translation: AAA30448.1.
M14077 expand/collapse EMBL AC list , M14069, M14070, M14071, M14072, M14073, M14074, M14075 Genomic DNA. Translation: AAA30446.1.
EF541122 mRNA. Translation: ABU41411.1.
PIRCMBO. A25631.
RefSeqNP_851337.1. NM_180994.2.
UniGeneBt.394.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CMSX-ray2.30A59-381[»]
1CZIX-ray2.30E59-381[»]
3CMSX-ray2.00A59-381[»]
4AA8X-ray1.80A59-381[»]
4AUCX-ray1.60A59-381[»]
4CMSX-ray2.20A59-381[»]
ProteinModelPortalP00794.
SMRP00794. Positions 59-381.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome3882. Bos d Chymosin.
MEROPSA01.006.

Proteomic databases

PRIDEP00794.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000013970; ENSBTAP00000013970; ENSBTAG00000010565.
GeneID529879.
KEGGbta:529879.

Organism-specific databases

CTD229697.

Phylogenomic databases

eggNOGNOG248684.
GeneTreeENSGT00670000097830.
HOGENOMHOG000197681.
HOVERGENHBG000482.
InParanoidP00794.
KOK01378.
OMAQYFGKIY.
OrthoDBEOG7HQN88.
TreeFamTF314990.

Enzyme and pathway databases

SABIO-RKP00794.

Family and domain databases

Gene3D2.40.70.10. 2 hits.
InterProIPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR012848. Aspartic_peptidase_N.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERPTHR13683. PTHR13683. 1 hit.
PfamPF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR00792. PEPSIN.
SUPFAMSSF50630. SSF50630. 1 hit.
PROSITEPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00794.
NextBio20875125.

Entry information

Entry nameCHYM_BOVIN
AccessionPrimary (citable) accession number: P00794
Secondary accession number(s): A8RRP5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 2005
Last modified: May 14, 2014
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references