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P18276 (CHYM_SHEEP) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismOvis aries (Sheep)
Taxonomic identifier9940 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeCaprinaeOvis

Protein attributes

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

General annotation (Comments)

Function

Chymosin is synthesized in the mucosa of the stomach. The enzyme hydrolyzes casein to paracasein.

Catalytic activity

Broad specificity similar to that of pepsin A. Clots milk by cleavage of a single 105-Ser-Phe-|-Met-Ala-108 bond in kappa-chain of casein.

Subunit structure

Monomer.

Sequence similarities

Belongs to the peptidase A1 family.

Ontologies

Keywords
   Biological processDigestion
   DomainSignal
   Molecular functionAspartyl protease
Hydrolase
Protease
   PTMDisulfide bond
Zymogen
Gene Ontology (GO)
   Biological processdigestion

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

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
Propeptide17 – 5842Activation peptide
PRO_0000025994
Chain59 – 381323Chymosin
PRO_0000025995

Sites

Active site921 By similarity
Active site2741 By similarity

Amino acid modifications

Disulfide bond105 ↔ 110 By similarity
Disulfide bond265 ↔ 269 By similarity
Disulfide bond308 ↔ 341 By similarity

Sequences

Sequence LengthMass (Da)Tools
P18276 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: D9903528FA071C47

FASTA38142,075
        10         20         30         40         50         60 
MRCLVVLLAV FALSQGAEIT RIPLYKGKPL RKALKERGLL EDFLQKQQYG VSSEYSGFGE 

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

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

       190        200        210        220        230        240 
LGMAYPSLAS EYSVPVFDNM MDRRLVAQDL FSVYMDRSGQ GSMLTLGAID PSYYTGSLHW 

       250        260        270        280        290        300 
VPVTLQKYWQ FTVDSVTISG AVVACEGGCQ AILDTGTSKL VGPSSDILNI QQAIGATQNQ 

       310        320        330        340        350        360 
YGEFDIDCDS LSSMPTVVFE INGKMYPLTP YAYTSQEEGF CTSGFQGENH SHQWILGDVF 

       370        380 
IREYYSVFDR ANNLVGLAKA I 

« Hide

References

[1]"Complete primary structure of lamb preprochymosin deduced from cDNA."
Pungecar J., Strukelj B., Gubensek F., Turk V., Kregar I.
Nucleic Acids Res. 18:4602-4602(1990) [PubMed: 2117748] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53037 mRNA. Translation: CAA37209.1.
PIRCMSHB. S10996.
RefSeqNP_001009804.1. NM_001009804.1.
UniGeneOar.447.

3D structure databases

ProteinModelPortalP18276.
SMRP18276. Positions 59-381.
ModBaseSearch...

Protein family/group databases

MEROPSA01.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID443399.

Organism-specific databases

CTD229697.

Phylogenomic databases

HOVERGENHBG000482.

Family and domain databases

InterProIPR001461. Peptidase_A1.
IPR021109. Peptidase_aspartic.
IPR001969. Peptidase_aspartic_AS.
IPR009007. Peptidase_aspartic_catalytic.
IPR012848. Propep_A1.
[Graphical view]
Gene3DG3DSA:2.40.70.10. Pept_Aspartc_cat. 2 hits.
PANTHERPTHR13683. Peptidase_A1. 1 hit.
PfamPF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR00792. PEPSIN.
SUPFAMSSF50630. Pept_Aspartic. 1 hit.
PROSITEPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCHYM_SHEEP
AccessionPrimary (citable) accession number: P18276
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: November 16, 2011
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families