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P10056 (PAPA3_CARPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 99. 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:
Caricain

EC=3.4.22.30
Alternative name(s):
Papaya peptidase A
Papaya proteinase III
Short name=PPIII
Papaya proteinase omega
OrganismCarica papaya (Papaya)
Taxonomic identifier3649 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesCaricaceaeCarica

Protein attributes

Sequence length348 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain.

Subunit structure

Monomer.

Sequence similarities

Belongs to the peptidase C1 family.

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: UniProtKB-KW

   Molecular_functioncysteine-type peptidase 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 Potential
Propeptide17 – 132116Activation peptide
PRO_0000026410
Chain133 – 348216Caricain
PRO_0000026411

Sites

Active site1571
Active site2911
Active site3111

Amino acid modifications

Disulfide bond154 ↔ 195
Disulfide bond188 ↔ 227
Disulfide bond285 ↔ 336

Secondary structure

.......................................................... 348
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10056 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: 328F5C6BF45B4A07

FASTA34838,788
        10         20         30         40         50         60 
MAMIPSISKL LFVAICLFVH MSVSFGDFSI VGYSQDDLTS TERLIQLFNS WMLNHNKFYE 

        70         80         90        100        110        120 
NVDEKLYRFE IFKDNLNYID ETNKKNNSYW LGLNEFADLS NDEFNEKYVG SLIDATIEQS 

       130        140        150        160        170        180 
YDEEFINEDT VNLPENVDWR KKGAVTPVRH QGSCGSCWAF SAVATVEGIN KIRTGKLVEL 

       190        200        210        220        230        240 
SEQELVDCER RSHGCKGGYP PYALEYVAKN GIHLRSKYPY KAKQGTCRAK QVGGPIVKTS 

       250        260        270        280        290        300 
GVGRVQPNNE GNLLNAIAKQ PVSVVVESKG RPFQLYKGGI FEGPCGTKVD HAVTAVGYGK 

       310        320        330        340 
SGGKGYILIK NSWGTAWGEK GYIRIKRAPG NSPGVCGLYK SSYYPTKN 

« Hide

References

[1]Baker K.C., Revell D.F., Cummings N.J., Collins M.E., Goodenough P.W.
Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Leaf.
[2]"The thiol proteinases from the latex of Carica papaya L. II. The primary structure of proteinase omega."
Dubois T., Kleinschmidt T., Schnek A.G., Looze Y., Braunitzer G.
Biol. Chem. Hoppe-Seyler 369:741-754(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 133-348.
[3]Collins M.E., Revell D.F., Sumner I.G., Pickersgill R.W., Goodenough P.W.
Submitted (FEB-1990) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 237-348.
Tissue: Leaf.
[4]"Determination of the structure of papaya protease omega."
Pickersgill R.W., Rizkallah P., Harris G.W., Goodenough P.W.
Acta Crystallogr. B 47:766-771(1991)
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[5]"Crystal structure of a caricain D158E mutant in complex with E-64."
Katerelos N.A., Taylor M.A.J., Scott M., Goodenough P.W., Pickersgill R.W.
FEBS Lett. 392:35-39(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT GLU-290.
[6]"The prosequence of procaricain forms an alpha-helical domain that prevents access to the substrate-binding cleft."
Groves M.R., Taylor M.A., Scott M., Cummings N.J., Pickersgill R.W., Jenkins J.A.
Structure 4:1193-1203(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF PRO-CARICAIN.
[7]"Theoretical model structure of a caricain D158E mutant in complex with E-64C."
Bhattacharya S., Pal A., Bera A., Chakraborty S., Banerjee A.
Submitted (APR-2000) to the PDB data bank
Cited for: 3D-STRUCTURE MODELING OF 133-348.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X66060 mRNA. Translation: CAA46862.1.
X51899 mRNA. Translation: CAA36180.1.
PIRJN0633.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1C7Xmodel-A133-348[»]
1EUXmodel-A133-348[»]
1F1Imodel-A133-348[»]
1MEGX-ray2.00A133-348[»]
1PCIX-ray3.20A/B/C27-348[»]
1PPOX-ray1.80A133-348[»]
ProteinModelPortalP10056.
SMRP10056. Positions 38-348.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome1539. Car p Endoproteinase.
MEROPSC01.003.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.4.22.30. 1191.

Family and domain databases

InterProIPR025661. Pept_asp_AS.
IPR000169. Pept_cys_AS.
IPR025660. Pept_his_AS.
IPR013128. Peptidase_C1A.
IPR000668. Peptidase_C1A_C.
IPR013201. Prot_inhib_I29.
[Graphical view]
PANTHERPTHR12411. PTHR12411. 1 hit.
PfamPF08246. Inhibitor_I29. 1 hit.
PF00112. Peptidase_C1. 1 hit.
[Graphical view]
PRINTSPR00705. PAPAIN.
SMARTSM00848. Inhibitor_I29. 1 hit.
SM00645. 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...

Other

EvolutionaryTraceP10056.

Entry information

Entry namePAPA3_CARPA
AccessionPrimary (citable) accession number: P10056
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 1, 1996
Last modified: February 19, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant 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