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Reviewed, UniProtKB/Swiss-Prot P14080 (PAPA2_CARPA)

Last modified June 16, 2009. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

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Names and origin

Protein namesRecommended name:
    Chymopapain
    EC=3.4.22.6
Alternative name(s):
    Papaya proteinase II
      Short name=PPII
OrganismCarica papaya (Papaya)
Taxonomic identifier3649 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Caricaceae › Carica

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Protein attributes

Sequence length352 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

Specificity similar to that of papain.

Sequence similarities

Belongs to the peptidase C1 family.

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Ontologies

Keywords
   DomainSignal
   Molecular functionHydrolase
Protease
Thiol protease
   PTMDisulfide bond
Zymogen
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Molecular functioncysteine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Propeptide19 – 134116Activation peptide Ref.2 Ref.3
PRO_0000026408
Chain135 – 352218Chymopapain
PRO_0000026409

Sites

Active site1591
Active site2931
Active site3131

Amino acid modifications

Disulfide bond156 ↔ 197
Disulfide bond190 ↔ 229
Disulfide bond287 ↔ 338

Secondary structure

1 ...................................... 352
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P14080-1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 50EA31EBFCF0AF9F

FASTA35239,415
        10         20         30         40         50         60 
MATMSSISKI IFLATCLIIH MGLSSADFYT VGYSQDDLTS IERLIQLFDS WMLKHNKIYE 

        70         80         90        100        110        120 
SIDEKIYRFE IFRDNLMYID ETNKKNNSYW LGLNGFADLS NDEFKKKYVG FVAEDFTGLE 

       130        140        150        160        170        180 
HFDNEDFTYK HVTNYPQSID WRAKGAVTPV KNQGACGSCW AFSTIATVEG INKIVTGNLL 

       190        200        210        220        230        240 
ELSEQELVDC DKHSYGCKGG YQTTSLQYVA NNGVHTSKVY PYQAKQYKCR ATDKPGPKVK 

       250        260        270        280        290        300 
ITGYKRVPSN CETSFLGALA NQPLSVLVEA GGKPFQLYKS GVFDGPCGTK LDHAVTAVGY 

       310        320        330        340        350 
GTSDGKNYII IKNSWGPNWG EKGYMRLKRQ SGNSQGTCGV YKSSYYPFKG FA

« Hide

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References

[1]Connerton I.F.
Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Leaf.
[2]"The amino acid sequence of chymopapain from Carica papaya."
Watson D.C., Yaguchi M., Lynn K.R.
Biochem. J. 266:75-81(1990) [PubMed: 2106878] [Abstract]
Cited for: PROTEIN SEQUENCE OF 135-352.
[3]"The thiol proteinases from the latex of Carica papaya L. III. The primary structure of chymopapain."
Jacquet A., Kleinschmidt T., Schnek A.G., Looze Y., Braunitzer G.
Biol. Chem. Hoppe-Seyler 370:425-434(1989) [PubMed: 2500950] [Abstract]
Cited for: PROTEIN SEQUENCE OF 135-352.
[4]"Structure of chymopapain at 1.7-A resolution."
Maes D., Bouckaert J., Poortmans F., Wyns L., Looze Y.
Biochemistry 35:16292-16298(1996) [PubMed: 8973203] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).

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Cross-references

Sequence databases

X97789 mRNA. Translation: CAA66378.1.
PIRT09760.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1YALX-ray1.70A135-352[»]
SMRP14080. Positions 38-349.
ModBaseSearch...

Protein family/group databases

MEROPSC01.002.

Enzyme and pathway databases

BRENDA3.4.22.6. 18730.

Family and domain databases

InterProIPR000169. Pept_cys_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERPTHR12411. Peptidase_C1A. 1 hit.
PfamPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
ProDomPD000158. Peptidase_C1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00645. Pept_C1. 1 hit.
[Graphical view]
PROSITEPS00640. THIOL_PROTEASE_ASN. 1 hit.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePAPA2_CARPA
AccessionPrimary (citable) accession number: P14080
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 1, 1997
Last modified: June 16, 2009
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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