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Reviewed, UniProtKB/Swiss-Prot Q9N2D2 (CHYM_CALJA)

Last modified July 22, 2008. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Chymosin
    EC=3.4.23.4
Alternative name(s):
    Preprorennin
Gene names
Name: CYM
OrganismCallithrix jacchus (Common marmoset)
Taxonomic identifier9483 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniPlatyrrhiniCebidaeCallitrichinaeCallithrix

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

Hydrolyzes a variety of proteins.

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.

Enzyme regulation

Inhibited by pepstatin.

Subunit structure

Monomer By similarity.

Developmental stage

Expressed in adult, not neonate-specific as in other organisms.

Sequence similarities

Belongs to the peptidase A1 family.

Biophysicochemical properties

pH dependence:

Optimum pH is about 2.5.

Ontologies

Keywords

   Biological processDigestion
   DomainRepeat
Signal
   Molecular functionAspartyl protease
Hydrolase
Protease
   PTMZymogen
   Technical termDirect protein sequencing

Gene Ontology (GO)

   Molecular functionchymosin activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Signal peptide1 – 1616
Propeptide17 – 5842Activation peptide By similarity
Chain59 – 381323Chymosin

Regions

Repeat92 – 102111
Repeat274 – 284112

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
Q9N2D2-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: C5820C74C97BB96B

FASTA38141,896
        10         20         30         40         50         60 
MRGFVVLLAV FALSQASGIV RIPLHKGKSL RRALKERGLL EDFLKNHQHA VSRKHSNSRE 

        70         80         90        100        110        120 
VASEFLTNYL DCQYFGKIYI GTPPQEFTVV FDTGSSDLWV PSVYCNSVAC QNHHRFDPSK 

       130        140        150        160        170        180 
SSTFQNMDKS LSIQYGTGSM QGLLGYDTVT VSSIVDPHQT VGLSTQEPGD VFTYSEFDGI 

       190        200        210        220        230        240 
LGLAYPSLAS EYSVPVFDNM MDRHLVAQDL FSVYMSRNEQ GSMLTLGAID PSYYTGSLHW 

       250        260        270        280        290        300 
IPVTVQEYWQ FTVDSVTVDG VVVACDGGCQ AILDTGTSML VGPGSDIFNI QQAIGATEGQ 

       310        320        330        340        350        360 
YGEFDIDCGT LSSMPTVVFE INGKKYPLPP SAYTNQDQGF CTSGFQGDDS SQQWILGDVF 

       370        380 
IREYYSVFDR ASNLVGLAKA I 

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References

[1]"New World monkey pepsinogens A and C, and prochymosins. Purification, characterization of enzymatic properties, cDNA cloning, and molecular evolution."
Kageyama T.
J. Biochem. 127:761-770(2000) [PubMed: 10788784] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-26, FUNCTION, ENZYME REGULATION.
Tissue: Gastric mucosa.

Cross-references

Sequence databases

AB038386 mRNA. Translation: BAA90873.1.
PIRJC7247.

3D structure databases

HSSPHSSP built from PDB template 4CMS based on UniProtKB P00794.
SMRQ9N2D2. Positions 60-381.
ModBaseSearch...

Protein family/group databases

MEROPSA01.006.

Phylogenomic databases

HOVERGENQ9N2D2.

Family and domain databases

InterProIPR001969. Pept_Asp_AS.
IPR009007. Pept_Aspartc_cat.
IPR001461. Peptidase_A1.
IPR012848. Propep_A1.
[Graphical view]
Gene3DG3DSA:2.40.70.10. Pept_Aspartc_cat. 1 hit.
PANTHERPTHR13683. Peptidase_A1. 1 hit.
PfamPF07966. A1_Propeptide. 1 hit.
PF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR00792. PEPSIN.
PROSITEPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]
ProDomQ9N2D2.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

LinkHubQ9N2D2.
ProtoNetSearch...

Entry information

Entry nameCHYM_CALJA
AccessionPrimary (citable) accession number: Q9N2D2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: October 1, 2000
Last modified: July 22, 2008
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents